SPTAN1 | ENSG00000197694 | NCBI 6709

Details for: SPTAN1

Gene ID: 6709

Symbol: SPTAN1

Ensembl ID: ENSG00000197694

Description: spectrin alpha, non-erythrocytic 1

Associated with

Apoptosis
(R-HSA-109581)
Apoptotic cleavage of cellular proteins
(R-HSA-111465)
Apoptotic execution phase
(R-HSA-75153)
Asparagine n-linked glycosylation
(R-HSA-446203)
Axon guidance
(R-HSA-422475)
Caspase-mediated cleavage of cytoskeletal proteins
(R-HSA-264870)
Cell-cell communication
(R-HSA-1500931)
Copi-mediated anterograde transport
(R-HSA-6807878)
Developmental biology
(R-HSA-1266738)
Er to golgi anterograde transport
(R-HSA-199977)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Interaction between l1 and ankyrins
(R-HSA-445095)
L1cam interactions
(R-HSA-373760)
Mapk1/mapk3 signaling
(R-HSA-5684996)
Mapk family signaling cascades
(R-HSA-5683057)
Membrane trafficking
(R-HSA-199991)
Metabolism of proteins
(R-HSA-392499)
Ncam signaling for neurite out-growth
(R-HSA-375165)
Nephrin family interactions
(R-HSA-373753)
Nervous system development
(R-HSA-9675108)
Neutrophil degranulation
(R-HSA-6798695)
Post-translational protein modification
(R-HSA-597592)
Programmed cell death
(R-HSA-5357801)
Raf/map kinase cascade
(R-HSA-5673001)
Rho gtpase cycle
(R-HSA-9012999)
Rhou gtpase cycle
(R-HSA-9013420)
Rhov gtpase cycle
(R-HSA-9013424)
Sensory perception
(R-HSA-9709957)
Sensory processing of sound
(R-HSA-9659379)
Sensory processing of sound by inner hair cells of the cochlea
(R-HSA-9662360)
Sensory processing of sound by outer hair cells of the cochlea
(R-HSA-9662361)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Transport to the golgi and subsequent modification
(R-HSA-948021)
Vesicle-mediated transport
(R-HSA-5653656)
Actin binding
(GO:0003779)
Actin cytoskeleton organization
(GO:0030036)
Actin filament binding
(GO:0051015)
Actin filament capping
(GO:0051693)
Cadherin binding
(GO:0045296)
Calcium ion binding
(GO:0005509)
Calmodulin binding
(GO:0005516)
Cell junction
(GO:0030054)
Cell projection
(GO:0042995)
Cortical actin cytoskeleton
(GO:0030864)
Cytosol
(GO:0005829)
Extracellular exosome
(GO:0070062)
Extracellular region
(GO:0005576)
Extracellular vesicle
(GO:1903561)
Intracellular membrane-bounded organelle
(GO:0043231)
Membrane
(GO:0016020)
Microtubule cytoskeleton
(GO:0015630)
Plasma membrane
(GO:0005886)
Protein binding
(GO:0005515)
Specific granule lumen
(GO:0035580)
Spectrin
(GO:0008091)
Structural constituent of cytoskeleton
(GO:0005200)
Tertiary granule lumen
(GO:1904724)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 525.9564
Cell Significance Index: -81.8100
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 314.6938
Cell Significance Index: -79.8200
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 213.4980
Cell Significance Index: -87.9500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 164.1079
Cell Significance Index: -66.6700
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 151.3652
Cell Significance Index: -77.8600
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 123.8037
Cell Significance Index: -83.0800
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 69.9246
Cell Significance Index: -66.7600
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 66.3771
Cell Significance Index: -81.8400
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 28.0978
Cell Significance Index: -75.2700
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 20.8142
Cell Significance Index: -63.9300
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 20.7980
Cell Significance Index: -82.0700
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 18.5782
Cell Significance Index: -40.6600
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: 6.3721
Cell Significance Index: 49.1200
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 5.1512
Cell Significance Index: 268.3200
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.6832
Cell Significance Index: 538.2500
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 2.3814
Cell Significance Index: 146.3700
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 2.2745
Cell Significance Index: 815.8200
Cell Name: cortical interneuron (CL0008031)
Fold Change: 1.8960
Cell Significance Index: 45.4700
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 1.7829
Cell Significance Index: 51.3700
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 1.7061
Cell Significance Index: 1180.0100
Cell Name: Purkinje cell (CL0000121)
Fold Change: 1.6660
Cell Significance Index: 36.4800
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 1.6617
Cell Significance Index: 36.0000
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: 1.4553
Cell Significance Index: 41.5300
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.4431
Cell Significance Index: 177.4500
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 1.3657
Cell Significance Index: 60.4100
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.3595
Cell Significance Index: 245.0800
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 1.3520
Cell Significance Index: 90.9100
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.2853
Cell Significance Index: 139.8100
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.2833
Cell Significance Index: 98.4800
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.2808
Cell Significance Index: 254.1800
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 1.2787
Cell Significance Index: 48.4200
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.2189
Cell Significance Index: 1100.6100
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.9849
Cell Significance Index: 1339.2200
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.9380
Cell Significance Index: 49.2500
Cell Name: peg cell (CL4033014)
Fold Change: 0.9345
Cell Significance Index: 21.5900
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.8878
Cell Significance Index: 484.8700
Cell Name: preadipocyte (CL0002334)
Fold Change: 0.7392
Cell Significance Index: 14.4300
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.7251
Cell Significance Index: 85.5100
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.6776
Cell Significance Index: 93.0600
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.5990
Cell Significance Index: 264.8500
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 0.5525
Cell Significance Index: 11.8100
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.5480
Cell Significance Index: 28.4700
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.3564
Cell Significance Index: 548.6700
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.3501
Cell Significance Index: 6.0000
Cell Name: retinal rod cell (CL0000604)
Fold Change: 0.3498
Cell Significance Index: 4.1700
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.3415
Cell Significance Index: 629.8400
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.2996
Cell Significance Index: 16.8100
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.2860
Cell Significance Index: 28.2900
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.2690
Cell Significance Index: 6.7300
Cell Name: odontoblast (CL0000060)
Fold Change: 0.2481
Cell Significance Index: 31.8000
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.2352
Cell Significance Index: 442.9000
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.2041
Cell Significance Index: 13.1700
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1633
Cell Significance Index: 31.0900
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.1496
Cell Significance Index: 7.0300
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.1453
Cell Significance Index: 5.1100
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.1204
Cell Significance Index: 76.4500
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.0719
Cell Significance Index: 3.2600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.0263
Cell Significance Index: 11.9300
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0107
Cell Significance Index: 1.8200
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0014
Cell Significance Index: 0.0900
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0418
Cell Significance Index: -30.6300
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0532
Cell Significance Index: -39.3900
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0808
Cell Significance Index: -50.4700
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0824
Cell Significance Index: -62.3800
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0969
Cell Significance Index: -4.5200
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0998
Cell Significance Index: -56.2800
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -0.1184
Cell Significance Index: -19.2500
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.1333
Cell Significance Index: -3.5600
Cell Name: lactocyte (CL0002325)
Fold Change: -0.1586
Cell Significance Index: -20.5000
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.1846
Cell Significance Index: -18.8600
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.2086
Cell Significance Index: -5.9800
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.2176
Cell Significance Index: -16.2200
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2340
Cell Significance Index: -49.2800
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2476
Cell Significance Index: -71.2300
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.2584
Cell Significance Index: -7.2200
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.2735
Cell Significance Index: -31.3400
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2900
Cell Significance Index: -42.1500
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3350
Cell Significance Index: -38.2400
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: -0.3720
Cell Significance Index: -5.3500
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.4171
Cell Significance Index: -29.5000
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.4626
Cell Significance Index: -53.9100
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.5188
Cell Significance Index: -11.0500
Cell Name: OFF midget ganglion cell (CL4033047)
Fold Change: -0.5565
Cell Significance Index: -6.9400
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.6230
Cell Significance Index: -64.8700
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.6846
Cell Significance Index: -9.3400
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.7034
Cell Significance Index: -4.2500
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.7273
Cell Significance Index: -21.3600
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.7671
Cell Significance Index: -20.1700
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.7708
Cell Significance Index: -20.9800
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.8785
Cell Significance Index: -8.0900
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.8991
Cell Significance Index: -71.2100
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.9076
Cell Significance Index: -15.1900
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.9643
Cell Significance Index: -30.8900
Cell Name: ON midget ganglion cell (CL4033046)
Fold Change: -0.9920
Cell Significance Index: -12.5200
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.0400
Cell Significance Index: -63.7600
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -1.0892
Cell Significance Index: -16.0800
Cell Name: sst GABAergic cortical interneuron (CL4023017)
Fold Change: -1.2370
Cell Significance Index: -24.4600
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: -1.2547
Cell Significance Index: -26.6300
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -1.2737
Cell Significance Index: -41.7000
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -1.3000
Cell Significance Index: -41.4100

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** SPTAN1 is a member of the spectrin family, which consists of four subunits (α, β, γ, and δ). The α subunit, encoded by SPTAN1, is non-erythrocytic, meaning it is not found in red blood cells. SPTAN1 is a cytoskeletal protein that interacts with various proteins, including actin, calmodulin, and L1CAM, to regulate cell shape, movement, and signaling. The protein is also involved in the organization of the actin cytoskeleton, which is essential for maintaining cell structure and function. **Pathways and Functions** SPTAN1 is involved in various cellular pathways, including: 1. **Actin cytoskeleton organization**: SPTAN1 interacts with actin to regulate the organization and dynamics of the actin cytoskeleton, which is essential for cell shape, movement, and signaling. 2. **Cell-cell communication**: SPTAN1 is involved in the regulation of cell-cell communication through interactions with L1CAM and other adhesion molecules. 3. **Programmed cell death**: SPTAN1 has been implicated in the regulation of programmed cell death (apoptosis) through interactions with caspases and other pro-apoptotic proteins. 4. **Neuronal development**: SPTAN1 is essential for the development and maintenance of neurons, particularly in the nervous system. 5. **Endothelial cell function**: SPTAN1 is also expressed in endothelial cells of the lung and plays a role in maintaining vascular integrity and function. **Clinical Significance** Dysregulation of SPTAN1 has been implicated in various neurological and cardiovascular disorders, including: 1. **Neurodegenerative diseases**: SPTAN1 has been implicated in the pathogenesis of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. 2. **Cancer**: SPTAN1 has been found to be overexpressed in certain types of cancer, including lung cancer and breast cancer. 3. **Cardiovascular disease**: SPTAN1 has been implicated in the regulation of vascular integrity and function, and its dysregulation has been linked to cardiovascular disease. In conclusion, SPTAN1 is a critical protein involved in various cellular processes, including actin cytoskeleton organization, cell-cell communication, and programmed cell death. Its dysregulation has been implicated in various neurological and cardiovascular disorders, highlighting the importance of further research into the role of SPTAN1 in human disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Spectrin alpha chain, non-erythrocytic 1
A0A384P5S9_HUMAN

Genular Protein ID: 2441437880

Symbol: SPTN1_HUMAN

Name: Spectrin alpha chain, non-erythrocytic 1

UniProtKB Accession Codes:

Q13813 Q13186 Q15324 Q16606 Q59EF1 Q5VXV5 Q5VXV6 Q7Z6M5 Q9P0V0

Database IDs:

Citations:

PubMed ID: 2307671

Title: Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin.

PubMed ID: 2307671

DOI: 10.1016/s0021-9258(19)39582-1

PubMed ID: 10625438

Title: Brain and muscle express a unique alternative transcript of alphaII spectrin.

PubMed ID: 10625438

DOI: 10.1021/bi991458k

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 3691949

Title: Structure and evolution of a non-erythroid spectrin, human alpha-fodrin.

PubMed ID: 3691949

DOI: 10.1042/bst0150804

PubMed ID: 3038643

Title: cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin.

PubMed ID: 3038643

DOI: 10.1111/j.1432-0436.1987.tb00052.x

PubMed ID: 8993318

Title: Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility.

PubMed ID: 8993318

DOI: 10.1021/bi962034i

PubMed ID: 7607240

Title: Cloning, expression and characterization of two putative calcium-binding sites in human non-erythroid alpha-spectrin.

PubMed ID: 7607240

DOI: 10.1111/j.1432-1033.1995.0658h.x

PubMed ID: 11971983

Title: Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain.

PubMed ID: 11971983

DOI: 10.1128/mcb.22.10.3527-3536.2002

PubMed ID: 15328537

Title: Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane.

PubMed ID: 15328537

DOI: 10.1371/journal.pbio.0020231

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18621045

Title: Novel interactions of CLN3 protein link Batten disease to dysregulation of fodrin-Na+, K+ ATPase complex.

PubMed ID: 18621045

DOI: 10.1016/j.yexcr.2008.06.016

PubMed ID: 18048348

Title: The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels.

PubMed ID: 18048348

DOI: 10.1074/jbc.m709729200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 16945920

Title: Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity.

PubMed ID: 16945920

DOI: 10.1074/jbc.m604613200

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

PubMed ID: 20493457

Title: Dominant-negative mutations in alpha-II spectrin cause West syndrome with severe cerebral hypomyelination, spastic quadriplegia, and developmental delay.

PubMed ID: 20493457

DOI: 10.1016/j.ajhg.2010.04.013

PubMed ID: 22429196

Title: Early onset West syndrome with severe hypomyelination and coloboma-like optic discs in a girl with SPTAN1 mutation.

PubMed ID: 22429196

DOI: 10.1111/j.1528-1167.2012.03437.x

PubMed ID: 22656320

Title: Progressive diffuse brain atrophy in West syndrome with marked hypomyelination due to SPTAN1 gene mutation.

PubMed ID: 22656320

DOI: 10.1016/j.braindev.2012.05.002

PubMed ID: 29050398

Title: Delineating SPTAN1 associated phenotypes: from isolated epilepsy to encephalopathy with progressive brain atrophy.

PubMed ID: 29050398

DOI: 10.1093/brain/awx195

PubMed ID: 27864847

Title: Diagnostic targeted resequencing in 349 patients with drug-resistant pediatric epilepsies identifies causative mutations in 30 different genes.

PubMed ID: 27864847

DOI: 10.1002/humu.23149

PubMed ID: 31332438

Title: Nonsense mutations in alpha-II spectrin in three families with juvenile onset hereditary motor neuropathy.

PubMed ID: 31332438

DOI: 10.1093/brain/awz216

PubMed ID: 33578420

Title: A novel de novo SPTAN1 nonsense variant causes hereditary motor neuropathy in a Chinese family.

PubMed ID: 33578420

DOI: 10.1093/brain/awaa357

PubMed ID: 35150594

Title: De Novo and Dominantly Inherited SPTAN1 Mutations Cause Spastic Paraplegia and Cerebellar Ataxia.

PubMed ID: 35150594

DOI: 10.1002/mds.28959

PubMed ID: 36331550

Title: Expanding SPTAN1 monoallelic variant associated disorders: From epileptic encephalopathy to pure spastic paraplegia and ataxia.

PubMed ID: 36331550

DOI: 10.1016/j.gim.2022.09.013

Sequence Information:

Length: 2472
Mass: 284539
Checksum: 4433BF74EFCEFC8A
Sequence:

MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 
QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 
LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 
KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 
ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 
YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 
DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 
MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 
KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 
VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTRITKEAG SVSLRMKQVE ELYHSLLELG 
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL 
KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN 
YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA 
WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 
HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM 
LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 
IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 
DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG 
ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL 
LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD 
TINGRFQKIK SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ 
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE HWKELKQLAA 
ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT 
VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ 
FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK 
DQLLAAKHVQ SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA 
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF 
RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW 
IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN 
KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS 
GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF 
DYVEFTRSLF VN

Genular Protein ID: 2503477734

Symbol: A0A384P5S9_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A384P5S9

Database IDs:

Sequence Information:

Length: 2452
Mass: 282282
Checksum: A34BBE6ADCAF5A5C
Sequence:

MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 
QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 
LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 
KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 
ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 
YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 
DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 
MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 
KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 
VKKLDPAQSA SRENLLEEQG SIALRQEQID NQYHSLLELG EKRKGMLEKS CKKFMLFREA 
NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI NKVAEDLESE 
GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH TVATFNSIKE LNERWRSLQQ 
LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN YGHDLASVQA LQRKHEGFER 
DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA WSSLGKRADQ RKAKLGDSHD 
LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 
FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM LDQCLELQLF HRDCEQAENW 
MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK IAALQAFADQ LIAAGHYAKG 
DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV DEIEAWISEK LQTASDESYK 
DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW 
QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH 
QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD TINGRFQKIK SMAASRRAKL 
NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ NLRKKHKRLE AELAAHEPAI 
QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE HWKELKQLAA ARGQRLEESL EYQQFVANVE 
EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN 
NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK 
TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHVQ SKAIEARHAS 
LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA SAFNSWFENA EEDLTDPVRC 
NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF RVASNPYTWF TMEALEETWR 
NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT 
LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL 
GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS CLRSLGYDLP 
MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET ENVKSSEEIE SAFRALSSEG 
KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF DYVEFTRSLF VN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: SPTAN1

Associated with

Cells (max top 100)

Other Information

Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin. PubMed ID: 2307671

Brain and muscle express a unique alternative transcript of alphaII spectrin. PubMed ID: 10625438

DNA sequence and analysis of human chromosome 9. PubMed ID: 15164053

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Structure and evolution of a non-erythroid spectrin, human alpha-fodrin. PubMed ID: 3691949

cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin. PubMed ID: 3038643

Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility. PubMed ID: 8993318

Cloning, expression and characterization of two putative calcium-binding sites in human non-erythroid alpha-spectrin. PubMed ID: 7607240

Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain. PubMed ID: 11971983

Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PubMed ID: 15328537

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Novel interactions of CLN3 protein link Batten disease to dysregulation of fodrin-Na+, K+ ATPase complex. PubMed ID: 18621045

The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels. PubMed ID: 18048348

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity. PubMed ID: 16945920

The consensus coding sequences of human breast and colorectal cancers. PubMed ID: 16959974

Dominant-negative mutations in alpha-II spectrin cause West syndrome with severe cerebral hypomyelination, spastic quadriplegia, and developmental delay. PubMed ID: 20493457

Early onset West syndrome with severe hypomyelination and coloboma-like optic discs in a girl with SPTAN1 mutation. PubMed ID: 22429196

Progressive diffuse brain atrophy in West syndrome with marked hypomyelination due to SPTAN1 gene mutation. PubMed ID: 22656320

Delineating SPTAN1 associated phenotypes: from isolated epilepsy to encephalopathy with progressive brain atrophy. PubMed ID: 29050398

Diagnostic targeted resequencing in 349 patients with drug-resistant pediatric epilepsies identifies causative mutations in 30 different genes. PubMed ID: 27864847

Nonsense mutations in alpha-II spectrin in three families with juvenile onset hereditary motor neuropathy. PubMed ID: 31332438

A novel de novo SPTAN1 nonsense variant causes hereditary motor neuropathy in a Chinese family. PubMed ID: 33578420

De Novo and Dominantly Inherited SPTAN1 Mutations Cause Spastic Paraplegia and Cerebellar Ataxia. PubMed ID: 35150594

Expanding SPTAN1 monoallelic variant associated disorders: From epileptic encephalopathy to pure spastic paraplegia and ataxia. PubMed ID: 36331550