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

Q8N6T3 (ARFG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribosylation factor GTPase-activating protein 1

Short name=ARF GAP 1
Alternative name(s):
ADP-ribosylation factor 1 GTPase-activating protein
Short name=ARF1 GAP
ARF1-directed GTPase-activating protein
Gene names
Name:ARFGAP1
Synonyms:ARF1GAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine By similarity.

Subunit structure

Interacts with ARF1. Interacts with the COPI coat proteins, KDELR1 and TMED2. The interaction with TMED2 inhibits the GAP activity By similarity.

Subcellular location

Cytoplasm By similarity. Golgi apparatus By similarity. Note: Associates with the Golgi complex By similarity.

Domain

The region downstream of Arf-GAP domain is essential to GAP activity in vivo. This region may be required for its targeting to Golgi membranes By similarity.

Sequence similarities

Contains 1 Arf-GAP domain.

Sequence caution

The sequence BAB55009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB55113.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB70901.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCOPI coating of Golgi vesicle

Traceable author statement. Source: Reactome

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

positive regulation of GTPase activity

Inferred from direct assay PubMed 22423108. Source: GOC

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of ARF GTPase activity

Inferred from electronic annotation. Source: InterPro

retrograde vesicle-mediated transport, Golgi to ER

Traceable author statement. Source: Reactome

   Cellular_componentGolgi-associated vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionARF GTPase activator activity

Inferred from electronic annotation. Source: InterPro

GTPase activator activity

Inferred from direct assay PubMed 22423108. Source: MGI

protein binding

Inferred from physical interaction PubMed 22363216. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S0076EBI-6288865,EBI-5323863

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N6T3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N6T3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     239-239: K → KFWGHKQQPEP
     279-280: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8N6T3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     279-406: VQGVGSKGWR...TDDGWDNQNW → CQRRLCCHQS...AVWTTSKTAT
Isoform 4 (identifier: Q8N6T3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVS → MLSSESSWSLRRITILAGPCRRSTTAEPRPSLGI
     35-147: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406ADP-ribosylation factor GTPase-activating protein 1
PRO_0000074190

Regions

Domain7 – 124118Arf-GAP
Zinc finger22 – 4524C4-type

Amino acid modifications

Modified residue1351Phosphothreonine Ref.8 Ref.11
Modified residue1891Phosphothreonine Ref.7 Ref.9 Ref.11
Modified residue2311N6-acetyllysine Ref.10
Modified residue3041Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 3434MASPR…PQWVS → MLSSESSWSLRRITILAGPC RRSTTAEPRPSLGI in isoform 4.
VSP_055379
Alternative sequence35 – 147113Missing in isoform 4.
VSP_055380
Alternative sequence2391K → KFWGHKQQPEP in isoform 2.
VSP_000298
Alternative sequence279 – 406128VQGVG…DNQNW → CQRRLCCHQSHCSAGHLGRA FCPVSWHEALCGQTGREEQA SLLPPKHVVGALEVCARGCP RCHVPHTPGTAAEWPGRLCL SRESVVRDGGTSPPFFRGKQ RAPWTAPRRATVIRTAVWTT SKTAT in isoform 3.
VSP_021818
Alternative sequence279 – 2802Missing in isoform 2.
VSP_000299
Natural variant1841V → M.
Corresponds to variant rs2273499 [ dbSNP | Ensembl ].
VAR_015187

Experimental info

Sequence conflict2741Q → R in BAB55009. Ref.1

Secondary structure

......................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: CAE41828DE660621

FASTA40644,668
        10         20         30         40         50         60 
MASPRTRKVL KEVRVQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR 

        70         80         90        100        110        120 
SVTMDKWKDI ELEKMKAGGN AKFREFLESQ EDYDPCWSLQ EKYNSRAAAL FRDKVVALAE 

       130        140        150        160        170        180 
GREWSLESSP AQNWTPPQPR TLPSMVHRVS GQPQSVTASS DKAFEDWLND DLGSYQGAQG 

       190        200        210        220        230        240 
NRYVGFGNTP PPQKKEDDFL NNAMSSLYSG WSSFTTGASR FASAAKEGAT KFGSQASQKA 

       250        260        270        280        290        300 
SELGHSLNEN VLKPAQEKVK EGKIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAEG 

       310        320        330        340        350        360 
PLDSPSEGHS YQNSGLDHFQ NSNIDQSFWE TFGSAEPTKT RKSPSSDSWT CADTSTERRS 

       370        380        390        400 
SDSWEVWGSA STNRNSNSDG GEGGEGTKKA VPPAVPTDDG WDNQNW 

« Hide

Isoform 2 [UniParc].

Checksum: BD081C6CE6CF0A18
Show »

FASTA41445,676
Isoform 3 [UniParc].

Checksum: 0C695741E21D0F6F
Show »

FASTA40344,467
Isoform 4 [UniParc].

Checksum: C0EEFC7461FF6CB3
Show »

FASTA29331,476

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Tissue: Thymus.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 2 AND 3).
Tissue: Brain and Fetal brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-406 (ISOFORM 1).
Tissue: Testis.
[6]"HRI NTT human fetal brain cDNA project."
Ueki N.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-406 (ISOFORM 1).
Tissue: Fetal brain.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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 THR-135 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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 THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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 THR-135 AND THR-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"Crystal structure of the ARFGAP domain of human ARFGAP1."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-128 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001629 mRNA. Translation: BAA91796.1.
AK027268 mRNA. Translation: BAB55009.1. Different initiation.
AK027441 mRNA. Translation: BAB55113.1. Different initiation.
AK303454 mRNA. Translation: BAH13964.1.
AL121827 Genomic DNA. Translation: CAX12645.1.
CH471077 Genomic DNA. Translation: EAW75292.1.
CH471077 Genomic DNA. Translation: EAW75294.1.
BC000786 mRNA. Translation: AAH00786.1.
BC006085 mRNA. Translation: AAH06085.1.
BC011876 mRNA. Translation: AAH11876.1.
BC028233 mRNA. Translation: AAH28233.1.
AL137744 mRNA. Translation: CAB70901.1. Sequence problems.
AB015340 mRNA. Translation: BAA88117.1.
CCDSCCDS13515.1. [Q8N6T3-1]
CCDS13516.1. [Q8N6T3-2]
CCDS63326.1. [Q8N6T3-3]
PIRT46298.
RefSeqNP_001268411.1. NM_001281482.1. [Q8N6T3-3]
NP_001268412.1. NM_001281483.1.
NP_001268413.1. NM_001281484.1.
NP_060679.1. NM_018209.3. [Q8N6T3-1]
NP_783202.1. NM_175609.2. [Q8N6T3-2]
UniGeneHs.25584.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWDX-ray2.40A/B1-128[»]
3O47X-ray2.80A/B1-140[»]
ProteinModelPortalQ8N6T3.
SMRQ8N6T3. Positions 3-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120856. 24 interactions.
IntActQ8N6T3. 19 interactions.
MINTMINT-1409968.
STRING9606.ENSP00000314615.

PTM databases

PhosphoSiteQ8N6T3.

Polymorphism databases

DMDM27923731.

Proteomic databases

MaxQBQ8N6T3.
PaxDbQ8N6T3.
PRIDEQ8N6T3.

Protocols and materials databases

DNASU55738.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353546; ENSP00000314615; ENSG00000101199. [Q8N6T3-2]
ENST00000370275; ENSP00000359298; ENSG00000101199. [Q8N6T3-3]
ENST00000370283; ENSP00000359306; ENSG00000101199. [Q8N6T3-1]
ENST00000519273; ENSP00000443716; ENSG00000101199.
GeneID55738.
KEGGhsa:55738.
UCSCuc002yel.3. human. [Q8N6T3-2]
uc002yem.3. human. [Q8N6T3-1]

Organism-specific databases

CTD55738.
GeneCardsGC20P061904.
H-InvDBHIX0174713.
HGNCHGNC:15852. ARFGAP1.
HPAHPA051019.
HPA056273.
MIM608377. gene.
neXtProtNX_Q8N6T3.
PharmGKBPA164741246.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOVERGENHBG050562.
KOK12492.
OMASDSWENW.
OrthoDBEOG7C8GH3.
PhylomeDBQ8N6T3.
TreeFamTF105931.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ8N6T3.
BgeeQ8N6T3.
CleanExHS_ARFGAP1.
GenevestigatorQ8N6T3.

Family and domain databases

InterProIPR001164. ArfGAP.
[Graphical view]
PfamPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00105. ArfGap. 1 hit.
[Graphical view]
PROSITEPS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARFGAP1. human.
EvolutionaryTraceQ8N6T3.
GeneWikiARFGAP1.
GenomeRNAi55738.
NextBio60684.
PROQ8N6T3.
SOURCESearch...

Entry information

Entry nameARFG1_HUMAN
AccessionPrimary (citable) accession number: Q8N6T3
Secondary accession number(s): B7Z8H8 expand/collapse secondary AC list , B7ZBI3, E1P5I9, Q6PK71, Q96KC4, Q96T02, Q9NSU3, Q9NVF6, Q9UIL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: July 9, 2014
This is version 123 of the entry and version 2 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 20

Human chromosome 20: entries, gene names and cross-references to MIM