SEC23IP | ENSG00000107651 | NCBI 11196

Details for: SEC23IP

Gene ID: 11196

Symbol: SEC23IP

Ensembl ID: ENSG00000107651

Description: SEC23 interacting protein

Associated with

Asparagine n-linked glycosylation
(R-HSA-446203)
Copii-mediated vesicle transport
(R-HSA-204005)
Er to golgi anterograde transport
(R-HSA-199977)
Membrane trafficking
(R-HSA-199991)
Metabolism of proteins
(R-HSA-392499)
Post-translational protein modification
(R-HSA-597592)
Transport to the golgi and subsequent modification
(R-HSA-948021)
Vesicle-mediated transport
(R-HSA-5653656)
Copii-coated er to golgi transport vesicle
(GO:0030134)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Endoplasmic reticulum
(GO:0005783)
Endoplasmic reticulum-golgi intermediate compartment
(GO:0005793)
Endoplasmic reticulum to golgi vesicle-mediated transport
(GO:0006888)
Er to golgi transport vesicle membrane
(GO:0012507)
Golgi apparatus
(GO:0005794)
Golgi organization
(GO:0007030)
Intracellular membrane-bounded organelle
(GO:0043231)
Intracellular protein transport
(GO:0006886)
Metal ion binding
(GO:0046872)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)

Other Information

Proteins

SEC23-interacting protein

Genular Protein ID: 2641860756

Symbol: S23IP_HUMAN

Name: SEC23-interacting protein

UniProtKB Accession Codes:

Q9Y6Y8 D3DRD2 Q8IXH5 Q9BUK5

Database IDs:

Citations:

PubMed ID: 10400679

Title: p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins.

PubMed ID: 10400679

DOI: 10.1074/jbc.274.29.20505

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: 11788596

Title: A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125.

PubMed ID: 11788596

DOI: 10.1074/jbc.m111092200

PubMed ID: 15623529

Title: p125 is localized in endoplasmic reticulum exit sites and involved in their organization.

PubMed ID: 15623529

DOI: 10.1074/jbc.m409673200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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: 22922100

Title: Roles of SAM and DDHD domains in mammalian intracellular phospholipase A1 KIAA0725p.

PubMed ID: 22922100

DOI: 10.1016/j.bbamcr.2012.02.002

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

Sequence Information:

Length: 1000
Mass: 111076
Checksum: DC71C274179F2CE9
Sequence:

MAERKPNGGS GGASTSSSGT NLLFSSSATE FSFNVPFIPV TQASASPASL LLPGEDSTDV 
GEEDSFLGQT SIHTSAPQTF SYFSQVSSSS DPFGNIGQSP LTTAATSVGQ SGFPKPLTAL 
PFTTGSQDVS NAFSPSISKA QPGAPPSSLM GINSYLPSQP SSLPPSYFGN QPQGIPQPGY 
NPYRHTPGSS RANPYIAPPQ LQQCQTPGPP AHPPPSGPPV QMYQMPPGSL PPVPSSVQSP 
AQQQVPARPG APSVQVPSPF LLQNQYEPVQ PHWFYCKEVE YKQLWMPFSV FDSLNLEEIY 
NSVQPDPESV VLGTDGGRYD VYLYDRIRKA AYWEEEPAEV RRCTWFYKGD TDSRFIPYTE 
EFSEKLEAEY KKAVTTNQWH RRLEFPSGET IVMHNPKVIV QFQPSSVPDE WGTTQDGQTR 
PRVVKRGIDD NLDEIPDGEM PQVDHLVFVV HGIGPVCDLR FRSIIECVDD FRVVSLKLLR 
THFKKSLDDG KVSRVEFLPV HWHSSLGGDA TGVDRNIKKI TLPSIGRFRH FTNETLLDIL 
FYNSPTYCQT IVEKVGMEIN HLHALFMSRN PDFKGGVSVA GHSLGSLILF DILSNQKDLN 
LSKCPGPLAV ANGVVKQLHF QEKQMPEEPK LTLDESYDLV VENKEVLTLQ ETLEALSLSE 
YFSTFEKEKI DMESLLMCTV DDLKEMGIPL GPRKKIANFV EHKAAKLKKA ASEKKAVAAT 
STKGQEQSAQ KTKDMASLPS ESNEPKRKLP VGACVSSVCV NYESFEVGAG QVSVAYNSLD 
FEPEIFFALG SPIAMFLTIR GVDRIDENYS LPTCKGFFNI YHPLDPVAYR LEPMIVPDLD 
LKAVLIPHHK GRKRLHLELK ESLSRMGSDL KQGFISSLKS AWQTLNEFAR AHTSSTQLQE 
ELEKVANQIK EEEEKQVVEA EKVVESPDFS KDEDYLGKVG MLNGGRRIDY VLQEKPIESF 
NEYLFALQSH LCYWESEDTA LLLLKEIYRT MNISPEQPQH

The gene details are incomplete or unavailable at the moment.

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: SEC23IP

Associated with

Other Information

p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins. PubMed ID: 10400679

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

A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125. PubMed ID: 11788596

p125 is localized in endoplasmic reticulum exit sites and involved in their organization. PubMed ID: 15623529

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

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

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

Roles of SAM and DDHD domains in mammalian intracellular phospholipase A1 KIAA0725p. PubMed ID: 22922100

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