Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P46060 (RAGP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ran GTPase-activating protein 1

Short name=RanGAP1
Gene names
Name:RANGAP1
Synonyms:KIAA1835, SD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.

Subunit structure

Homodimer. Forms a tight complex in association with RANBP2/NUP358 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2. Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2/NUP358. The SUMO1/RANGAP1/UBC9/NUP358 complex associates with nuclear pore complexes. Interacts with TRAF6. Ref.9 Ref.11

Subcellular location

Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Note: Cytoplasmic during interphase. Targeted to the nuclear rim after sumoylation. During mitosis, associates with mitotic spindles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation. Ref.8 Ref.9

Tissue specificity

Highly expressed in brain, thymus and testis. Ref.7

Post-translational modification

Phosphorylated occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBC9, on nuclear pore complex (NPC) diassembly and during mitosis. Ref.9

Sumoylated with SUMO1. Sumoylation is necessary for targeting to the nuclear envelope (NE), and for association with mitotic spindles and kinetochores during mitosis. Also required for interaction with RANBP2 and is mediated by UBC9. Ref.8 Ref.16

Sequence similarities

Belongs to the RNA1 family.

Contains 6 LRR (leucine-rich) repeats.

Sequence caution

The sequence BAB47464.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SUMO1P631654EBI-396091,EBI-80140
UBE2IP632794EBI-396091,EBI-80168

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 587586Ran GTPase-activating protein 1
PRO_0000056737

Regions

Repeat48 – 7124LRR 1
Repeat111 – 13424LRR 2
Repeat207 – 23024LRR 3
Repeat235 – 25824LRR 4
Repeat292 – 31928LRR 5
Repeat320 – 34324LRR 6
Motif523 – 5264SUMO conjugation
Compositional bias359 – 39941Asp/Glu-rich (highly acidic)
Compositional bias359 – 39739Asp/Glu-rich (highly acidic)

Sites

Site5621Hydrophobic interaction with UBC9 By similarity
Site5651Hydrophobic interaction with UBC9 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.16
Modified residue3581Phosphoserine Ref.12
Modified residue4091Phosphothreonine; by CDK2 Ref.9
Modified residue4281Phosphoserine Ref.9 Ref.12 Ref.14 Ref.17
Modified residue4351Phosphoserine Ref.14
Modified residue4361Phosphothreonine Ref.14
Modified residue4421Phosphoserine Ref.9 Ref.10 Ref.12 Ref.14 Ref.17 Ref.19
Modified residue5241N6-acetyllysine; alternate Ref.15
Cross-link8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.16
Cross-link524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate Ref.16

Natural variations

Natural variant1331E → Q.
Corresponds to variant rs2229752 [ dbSNP | Ensembl ].
VAR_029240

Experimental info

Mutagenesis5241K → R: No association with mitotic spindles during mitosis. Ref.8

Secondary structure

......................... 587
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46060 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3C18068AAC06B98F

FASTA58763,542
        10         20         30         40         50         60 
MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS LEALRLEGNT 

        70         80         90        100        110        120 
VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL ISLGEGLITA GAQLVELDLS 

       130        140        150        160        170        180 
DNAFGPDGVQ GFEALLKSSA CFTLQELKLN NCGMGIGGGK ILAAALTECH RKSSAQGKPL 

       190        200        210        220        230        240 
ALKVFVAGRN RLENDGATAL AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV 

       250        260        270        280        290        300 
INLNDNTFTE KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL 

       310        320        330        340        350        360 
SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM AKVLASLSDD 

       370        380        390        400        410        420 
EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ RGQGEKSATP SRKILDPNTG 

       430        440        450        460        470        480 
EPAPVLSSPP PADVSTFLAF PSPEKLLRLG PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF 

       490        500        510        520        530        540 
KDEATVRMAV QDAVDALMQK AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM 

       550        560        570        580 
ALNHMVQQDY FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV 

« Hide

References

« Hide 'large scale' references
[1]"Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport."
Bischoff F.R., Krebber H., Kempf T., Hermes I., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 92:1749-1753(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Kidney.
[7]"Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1."
Krebber H., Ponstingl H.
Gene 180:7-11(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524.
[9]"RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification."
Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.
J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF6.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-435; THR-436 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-8 AND LYS-524, ACETYLATION AT ALA-2.
Tissue: Cervix carcinoma.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
Reverter D., Lima C.D.
Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 418-587 IN COMPLEX WITH SUMO1; RANBP2 AND UBE2I.
[21]"SUMO protease SENP1 induces isomerization of the scissile peptide bond."
Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 432-587 IN COMPLEX WITH SUMO1 AND SENP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82260 mRNA. Translation: CAA57714.1.
AB058738 mRNA. Translation: BAB47464.1. Different initiation.
CR456557 mRNA. Translation: CAG30443.1.
AL035681 Genomic DNA. Translation: CAB63073.1.
BC014044 mRNA. Translation: AAH14044.1.
BC041396 mRNA. Translation: AAH41396.1.
CCDSCCDS14012.1.
PIRJC5300.
RefSeqNP_001265580.1. NM_001278651.1.
NP_002874.1. NM_002883.3.
XP_006724352.1. XM_006724289.1.
UniGeneHs.183800.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5SX-ray3.01C418-587[»]
2GRNX-ray1.80B419-587[»]
2GROX-ray1.70B419-587[»]
2GRPX-ray2.05B419-587[»]
2GRQX-ray1.70B419-587[»]
2GRRX-ray1.30B419-587[»]
2IO2X-ray2.90C418-587[»]
2IO3X-ray3.20C418-587[»]
2IY0X-ray2.77C432-587[»]
3UINX-ray2.60C419-587[»]
3UIOX-ray2.60C419-587[»]
3UIPX-ray2.29C419-587[»]
ProteinModelPortalP46060.
SMRP46060. Positions 21-349, 431-587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111840. 75 interactions.
DIPDIP-29079N.
IntActP46060. 17 interactions.
MINTMINT-3016328.
STRING9606.ENSP00000348577.

PTM databases

PhosphoSiteP46060.

Polymorphism databases

DMDM1172922.

Proteomic databases

MaxQBP46060.
PaxDbP46060.
PRIDEP46060.

Protocols and materials databases

DNASU5905.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356244; ENSP00000348577; ENSG00000100401.
ENST00000405486; ENSP00000385866; ENSG00000100401.
ENST00000455915; ENSP00000401470; ENSG00000100401.
GeneID5905.
KEGGhsa:5905.
UCSCuc003azs.3. human.

Organism-specific databases

CTD5905.
GeneCardsGC22M041641.
HGNCHGNC:9854. RANGAP1.
HPACAB004293.
HPA050110.
MIM602362. gene.
neXtProtNX_P46060.
PharmGKBPA34216.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5238.
HOGENOMHOG000195026.
HOVERGENHBG017720.
InParanoidP46060.
KOK14319.
OMASFNSNAF.
OrthoDBEOG70W3DV.
PhylomeDBP46060.
TreeFamTF318283.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP46060.
BgeeP46060.
CleanExHS_RANGAP1.
GenevestigatorP46060.

Family and domain databases

Gene3D1.25.40.200. 1 hit.
InterProIPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view]
PANTHERPTHR24113. PTHR24113. 1 hit.
PfamPF07834. RanGAP1_C. 1 hit.
[Graphical view]
SUPFAMSSF69099. SSF69099. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRANGAP1. human.
EvolutionaryTraceP46060.
GeneWikiRANGAP1.
GenomeRNAi5905.
NextBio22968.
PROP46060.
SOURCESearch...

Entry information

Entry nameRAGP1_HUMAN
AccessionPrimary (citable) accession number: P46060
Secondary accession number(s): Q96JJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM