Genular: Defining Cellular Identity and Function

Details for: Ranbp2

Gene ID: 19386

Symbol: Ranbp2

Ensembl ID: ENSMUSG00000003226

Description: RAN binding protein 2

Associated with

Amplification of signal from the kinetochores
(R-MMU-141424)
Amplification of signal from unattached kinetochores via a mad2 inhibitory signal
(R-MMU-141444)
Cell cycle
(R-MMU-1640170)
Cell cycle, mitotic
(R-MMU-69278)
Cell cycle checkpoints
(R-MMU-69620)
Cellular responses to stimuli
(R-MMU-8953897)
Cellular responses to stress
(R-MMU-2262752)
Cellular response to heat stress
(R-MMU-3371556)
Eml4 and nudc in mitotic spindle formation
(R-MMU-9648025)
Gene expression (transcription)
(R-MMU-74160)
Gene silencing by rna
(R-MMU-211000)
Glucose metabolism
(R-MMU-70326)
Glycolysis
(R-MMU-70171)
Metabolism
(R-MMU-1430728)
Metabolism of carbohydrates
(R-MMU-71387)
Metabolism of non-coding rna
(R-MMU-194441)
Metabolism of proteins
(R-MMU-392499)
Metabolism of rna
(R-MMU-8953854)
Mitotic anaphase
(R-MMU-68882)
Mitotic metaphase and anaphase
(R-MMU-2555396)
Mitotic prometaphase
(R-MMU-68877)
Mitotic prophase
(R-MMU-68875)
Mitotic spindle checkpoint
(R-MMU-69618)
M phase
(R-MMU-68886)
Nuclear envelope breakdown
(R-MMU-2980766)
Nuclear pore complex (npc) disassembly
(R-MMU-3301854)
Post-translational protein modification
(R-MMU-597592)
Processing of capped intron-containing pre-mrna
(R-MMU-72203)
Regulation of glucokinase by glucokinase regulatory protein
(R-MMU-170822)
Regulation of hsf1-mediated heat shock response
(R-MMU-3371453)
Resolution of sister chromatid cohesion
(R-MMU-2500257)
Rho gtpase effectors
(R-MMU-195258)
Rho gtpases activate formins
(R-MMU-5663220)
Separation of sister chromatids
(R-MMU-2467813)
Signaling by rho gtpases
(R-MMU-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-MMU-9716542)
Signal transduction
(R-MMU-162582)
Snrnp assembly
(R-MMU-191859)
Sumo e3 ligases sumoylate target proteins
(R-MMU-3108232)
Sumoylation
(R-MMU-2990846)
Sumoylation of chromatin organization proteins
(R-MMU-4551638)
Sumoylation of dna damage response and repair proteins
(R-MMU-3108214)
Sumoylation of dna replication proteins
(R-MMU-4615885)
Sumoylation of rna binding proteins
(R-MMU-4570464)
Sumoylation of sumoylation proteins
(R-MMU-4085377)
Sumoylation of ubiquitinylation proteins
(R-MMU-3232142)
Transcriptional regulation by small rnas
(R-MMU-5578749)
Transport of mature mrna derived from an intron-containing transcript
(R-MMU-159236)
Transport of mature mrna derived from an intronless transcript
(R-MMU-159231)
Transport of mature mrnas derived from intronless transcripts
(R-MMU-159234)
Transport of mature transcript to cytoplasm
(R-MMU-72202)
Transport of the slbp dependant mature mrna
(R-MMU-159230)
Transport of the slbp independent mature mrna
(R-MMU-159227)
Annulate lamellae
(GO:0005642)
Cytoplasm
(GO:0005737)
Cytoplasmic periphery of the nuclear pore complex
(GO:1990723)
Gtpase activator activity
(GO:0005096)
Intracellular membrane-bounded organelle
(GO:0043231)
Intracellular transport
(GO:0046907)
Membrane
(GO:0016020)
Metal ion binding
(GO:0046872)
Mrna transport
(GO:0051028)
Nls-bearing protein import into nucleus
(GO:0006607)
Nuclear envelope
(GO:0005635)
Nuclear export
(GO:0051168)
Nuclear inclusion body
(GO:0042405)
Nuclear membrane
(GO:0031965)
Nuclear pore
(GO:0005643)
Nuclear pore cytoplasmic filaments
(GO:0044614)
Nuclear pore nuclear basket
(GO:0044615)
Nucleocytoplasmic transport
(GO:0006913)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Peptidyl-prolyl cis-trans isomerase activity
(GO:0003755)
Positive regulation of glucokinase activity
(GO:0033133)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein peptidyl-prolyl isomerization
(GO:0000413)
Protein transport
(GO:0015031)
Regulation of gluconeogenesis
(GO:0006111)
Rna binding
(GO:0003723)
Small gtpase binding
(GO:0031267)
Sumo ligase activity
(GO:0061665)
Sumo ligase complex
(GO:0106068)
Sumo transferase activity
(GO:0019789)
Transferase activity
(GO:0016740)

Other Information

Proteins

E3 SUMO-protein ligase RanBP2

Genular Protein ID: 4261103665

Symbol: RBP2_MOUSE

Name: E3 SUMO-protein ligase RanBP2

UniProtKB Accession Codes:

Q9ERU9 E9QM01 Q61992 Q8C9K9

Database IDs:

Citations:

PubMed ID: 11353387

Title: Genomic organization, expression, and localization of murine Ran-binding protein 2 (RanBP2) gene.

PubMed ID: 11353387

DOI: 10.1007/s003350010291

PubMed ID: 19468303

Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

PubMed ID: 19468303

DOI: 10.1371/journal.pbio.1000112

PubMed ID: 16141072

Title: The transcriptional landscape of the mammalian genome.

PubMed ID: 16141072

DOI: 10.1126/science.1112014

PubMed ID: 8603673

Title: Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex.

PubMed ID: 8603673

PubMed ID: 16332688

Title: Parkin ubiquitinates and promotes the degradation of RanBP2.

PubMed ID: 16332688

DOI: 10.1074/jbc.m504994200

PubMed ID: 16452087

Title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

PubMed ID: 16452087

DOI: 10.1074/mcp.t500041-mcp200

PubMed ID: 17242355

Title: Large-scale phosphorylation analysis of mouse liver.

PubMed ID: 17242355

DOI: 10.1073/pnas.0609836104

PubMed ID: 19144319

Title: The phagosomal proteome in interferon-gamma-activated macrophages.

PubMed ID: 19144319

DOI: 10.1016/j.immuni.2008.11.006

PubMed ID: 19131326

Title: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.

PubMed ID: 19131326

DOI: 10.1074/mcp.m800451-mcp200

PubMed ID: 21183079

Title: A tissue-specific atlas of mouse protein phosphorylation and expression.

PubMed ID: 21183079

DOI: 10.1016/j.cell.2010.12.001

PubMed ID: 23641069

Title: Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport.

PubMed ID: 23641069

DOI: 10.1242/jcs.124172

PubMed ID: 23806337

Title: SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.

PubMed ID: 23806337

DOI: 10.1016/j.molcel.2013.06.001

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 35771867

Title: An Rtn4/Nogo-A-interacting micropeptide modulates synaptic plasticity with age.

PubMed ID: 35771867

DOI: 10.1371/journal.pone.0269404

Sequence Information:

Length: 3053
Mass: 341121
Checksum: 62FD4249DEE466AE
Sequence:

MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP 
KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER 
AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDIHVNIR LVELYRSNKR 
LKDAVAHCHE ADRNTALRSS LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA 
NLMLLTLSTR DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK 
MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR LSQSGHMLLN 
LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF LGNDDIGNLD GQVPDPDDLA 
RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL PAIRKWLKQL FHHLPQETSR LETNAPESIC 
ILDLEVFLLG VIYTSHLQLK EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH 
RKALPGTSAK LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG 
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA HITFAILDAV 
NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIR 
ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM QELEDYSEGG TLYKNGCWRS ADSELKHSTP 
SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR 
WPAEPYGQDP APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT GILSPRGDDY 
FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF GKSNFVQPMQ GEVIRPPLTT 
PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VAQPPSTAYS NSESLLGLLT SDKPLQGDGY 
SGLKPISGQA SGSRNTFSFG SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA 
SELANKSHET DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG 
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP NAGSDRSFVW 
HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK ALGTNTSTAP NHTLRIVKES 
ATQDNKDICK ADGGNLNFEF QIVKKEGPYW NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL 
LGPPLVENGF APKTGLENAQ DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS 
SFVQTSFKFG QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK 
EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG FEGMFAKKEG 
QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS ETSRSPKSGF EGLFPKKEGE 
WECAVCSVQN ESSSLKCVAC EASKPTHKPH EAPSAFTVGS KSQSNESAGS QVGTEFKSNF 
PEKNFKVGIS EQKFKFGHVD QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ 
EKGNQEKKSE KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK 
KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF EPVVQMPEKV 
ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL KNEVNGKLRM LMRREQVLKV 
CANHWITTTM NLKPLSGSDR AWMWLASDFS DGDAKLEQLA AKFKTPELAE EFKQKFEECQ 
RLLLDIPLQT PHKLVDTGRA AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA 
PSASDTTAKQ NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES 
TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV VPLPDLVEVS 
SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY DNKQVRIVMR RDQVLKLCAN 
HRITPDMTLQ TMKGTERVWV WTACDFADGE RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ 
EKDSLITPHV SHLSTPRESP CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE 
TTPKAVVSPP KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS 
RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT PEKAQEKSKP 
EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR PGYVSEEEED DEDYEMAVKK 
LNGKLYLDDS EKPLEENLAD NDKECVIVWE KKPTVEERAK ADTLKLPPTF FCGVCSDTDE 
DNGNGEDFQS ELRKVCEAQK SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS 
SPVSGTMDKP VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK 
DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV EVKSGEEDEE 
VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI LMRRDQVFKV CANHVITKAM 
ELKPLNVSNN ALVWTASDYA DGEAKVEQLA VRFKTKEMTE SFKKKFEECQ QNIIKLQNGH 
TSLAAELSKD TNPVVFFDVC ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS 
IFHRVVPDFI CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ 
FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC GQL

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: Ranbp2

Associated with

Other Information

Genomic organization, expression, and localization of murine Ran-binding protein 2 (RanBP2) gene. PubMed ID: 11353387

Lineage-specific biology revealed by a finished genome assembly of the mouse. PubMed ID: 19468303

The transcriptional landscape of the mammalian genome. PubMed ID: 16141072

Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex. PubMed ID: 8603673

Parkin ubiquitinates and promotes the degradation of RanBP2. PubMed ID: 16332688

Comprehensive identification of phosphorylation sites in postsynaptic density preparations. PubMed ID: 16452087

Large-scale phosphorylation analysis of mouse liver. PubMed ID: 17242355

The phagosomal proteome in interferon-gamma-activated macrophages. PubMed ID: 19144319

Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. PubMed ID: 19131326

A tissue-specific atlas of mouse protein phosphorylation and expression. PubMed ID: 21183079

Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport. PubMed ID: 23641069

SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. PubMed ID: 23806337

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

An Rtn4/Nogo-A-interacting micropeptide modulates synaptic plasticity with age. PubMed ID: 35771867