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Q9UQC2

- GAB2_HUMAN

UniProt

Q9UQC2 - GAB2_HUMAN

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Protein

GRB2-associated-binding protein 2

Gene

GAB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis.2 Publications

GO - Molecular functioni

  1. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  2. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  3. transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

GO - Biological processi

  1. cell migration Source: Ensembl
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. innate immune response Source: Reactome
  4. integrin-mediated signaling pathway Source: Ensembl
  5. osteoclast differentiation Source: UniProtKB
  6. phosphatidylinositol-mediated signaling Source: UniProtKB
  7. positive regulation of cell proliferation Source: UniProtKB
  8. positive regulation of mast cell degranulation Source: UniProtKB
  9. transmembrane receptor protein tyrosine kinase signaling pathway Source: GOC
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinkiQ9UQC2.

Names & Taxonomyi

Protein namesi
Recommended name:
GRB2-associated-binding protein 2
Alternative name(s):
GRB2-associated binder 2
Growth factor receptor bound protein 2-associated protein 2
pp100
Gene namesi
Name:GAB2
Synonyms:KIAA0571
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14458. GAB2.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101S → A or E: Impaired interaction with 14-3-3 proteins and increased EGF-independent cell proliferation; when associated with A-391. 1 Publication
Mutagenesisi391 – 3911T → A or E: Impaired interaction with 14-3-3 proteins and increased EGF-independent cell proliferation; when associated with A-210. 1 Publication

Organism-specific databases

PharmGKBiPA28478.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676GRB2-associated-binding protein 2PRO_0000050285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei133 – 1331Phosphoserine1 Publication
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei141 – 1411Phosphoserine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei159 – 1591Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine1 Publication
Modified residuei210 – 2101Phosphoserine1 Publication
Modified residuei218 – 2181Phosphoserine1 Publication
Modified residuei223 – 2231Phosphoserine1 Publication
Modified residuei264 – 2641Phosphoserine1 Publication
Modified residuei265 – 2651PhosphothreonineBy similarity
Modified residuei266 – 2661PhosphotyrosineBy similarity
Modified residuei278 – 2781Phosphothreonine1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei287 – 2871Phosphothreonine1 Publication
Modified residuei293 – 2931Phosphotyrosine1 Publication
Modified residuei331 – 3311Phosphothreonine1 Publication
Modified residuei385 – 3851Phosphothreonine1 Publication
Modified residuei391 – 3911Phosphothreonine1 Publication
Modified residuei405 – 4051Phosphoserine1 Publication
Modified residuei452 – 4521PhosphotyrosineBy similarity
Modified residuei480 – 4801Phosphoserine1 Publication
Modified residuei543 – 5431Phosphoserine2 Publications
Modified residuei622 – 6221Phosphoserine1 Publication
Modified residuei623 – 6231Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residue(s) by the thrombopoietin receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B-cell antigen receptors, gp130, IL-2R and IL-3R (By similarity). Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL (By similarity). Phosphorylated upon EGF stimulation. Phosphorylated on tyrosine residues by HCK upon IL6 signaling.By similarity3 Publications
Dephosphorylated by PTPN11.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UQC2.
PaxDbiQ9UQC2.
PRIDEiQ9UQC2.

PTM databases

PhosphoSiteiQ9UQC2.

Expressioni

Gene expression databases

BgeeiQ9UQC2.
CleanExiHS_GAB2.
ExpressionAtlasiQ9UQC2. baseline and differential.
GenevestigatoriQ9UQC2.

Organism-specific databases

HPAiCAB022159.
HPA000271.

Interactioni

Subunit structurei

Interacts with SHC1; may mediate interaction with receptors (By similarity). Interacts with SYK (By similarity). Interacts with PI-3 kinase. Interacts with GRB2 (via SH3 2 domain). Interacts (phosphorylated) with PTPN11. Interacts with TNFRSF11A (via cytoplasmic domain). Interacts (phosphorylated) with 14-3-3 family proteins SFN, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ; prevents interaction with GRB2 and attenuates GAB2 signaling. Interacts with HCK.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P6299314EBI-975200,EBI-401755
PTPN11Q061244EBI-975200,EBI-297779
YWHABP319464EBI-975200,EBI-359815

Protein-protein interaction databases

BioGridi115181. 32 interactions.
DIPiDIP-36653N.
IntActiQ9UQC2. 12 interactions.
MINTiMINT-123618.
STRINGi9606.ENSP00000302452.

Structurei

Secondary structure

1
676
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi515 – 5173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VWFX-ray1.58B508-522[»]
2W0ZX-ray1.70B350-358[»]
ProteinModelPortaliQ9UQC2.
SMRiQ9UQC2. Positions 27-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UQC2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 117112PHPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi351 – 3588SH3-binding
Motifi510 – 51910SH3-binding

Domaini

The SH3-binding motifs mediate interaction with SHC1 and GRB2.By similarity
The PH domain mediates phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate binding.By similarity

Sequence similaritiesi

Belongs to the GAB family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG83177.
GeneTreeiENSGT00510000046662.
HOGENOMiHOG000236270.
HOVERGENiHBG051685.
InParanoidiQ9UQC2.
KOiK08091.
OMAiMQPTLST.
OrthoDBiEOG7T4MJJ.
PhylomeDBiQ9UQC2.
TreeFamiTF329487.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UQC2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSGGGDVVCT GWLRKSPPEK KLRRYAWKKR WFILRSGRMS GDPDVLEYYK
60 70 80 90 100
NDHSKKPLRI INLNFCEQVD AGLTFNKKEL QDSFVFDIKT SERTFYLVAE
110 120 130 140 150
TEEDMNKWVQ SICQICGFNQ AEESTDSLRN VSSAGHGPRS SPAELSSSSQ
160 170 180 190 200
HLLRERKSSA PSHSSQPTLF TFEPPVSNHM QPTLSTSAPQ EYLYLHQCIS
210 220 230 240 250
RRAENARSAS FSQGTRASFL MRSDTAVQKL AQGNGHCVNG ISGQVHGFYS
260 270 280 290 300
LPKPSRHNTE FRDSTYDLPR SLASHGHTKG SLTGSETDNE DVYTFKTPSN
310 320 330 340 350
TLCREFGDLL VDNMDVPATP LSAYQIPRTF TLDKNHNAMT VATPGDSAIA
360 370 380 390 400
PPPRPPKPSQ AETPRWGSPQ QRPPISENSR SVAATIPRRN TLPAMDNSRL
410 420 430 440 450
HRASSCETYE YPQRGGESAG RSAESMSDGV GSFLPGKMIV GRSDSTNSED
460 470 480 490 500
NYVPMNPGSS TLLAMERAGD NSQSVYIPMS PGAHHFDSLG YPSTTLPVHR
510 520 530 540 550
GPSRGSEIQP PPVNRNLKPD RKAKPTPLDL RNNTVIDELP FKSPITKSWS
560 570 580 590 600
RANHTFNSSS SQYCRPISTQ SITSTDSGDS EENYVPMQNP VSASPVPSGT
610 620 630 640 650
NSPAPKKSTG SVDYLALDFQ PSSPSPHRKP STSSVTSDEK VDYVQVDKEK
660 670
TQALQNTMQE WTDVRQSSEP SKGAKL
Length:676
Mass (Da):74,458
Last modified:May 1, 2000 - v1
Checksum:i107623FD07D884C9
GO
Isoform 2 (identifier: Q9UQC2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:638
Mass (Da):69,968
Checksum:iEA3BCC63C00BBAF0
GO

Sequence cautioni

The sequence BAA25497.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201P → L.
Corresponds to variant rs2279374 [ dbSNP | Ensembl ].
VAR_053097
Natural varianti344 – 3441P → L.
Corresponds to variant rs2279374 [ dbSNP | Ensembl ].
VAR_020407

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 2. 2 PublicationsVSP_038520Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018413 mRNA. Translation: BAA76737.1.
AB011143 mRNA. Translation: BAA25497.2. Different initiation.
AP002985 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75057.1.
CH471076 Genomic DNA. Translation: EAW75058.1.
BC131711 mRNA. Translation: AAI31712.1.
BC152459 mRNA. Translation: AAI52460.1.
CCDSiCCDS8259.1. [Q9UQC2-1]
CCDS8260.1. [Q9UQC2-2]
RefSeqiNP_036428.1. NM_012296.3. [Q9UQC2-2]
NP_536739.1. NM_080491.2. [Q9UQC2-1]
XP_006718816.1. XM_006718753.1. [Q9UQC2-2]
UniGeneiHs.429434.

Genome annotation databases

EnsembliENST00000340149; ENSP00000343959; ENSG00000033327. [Q9UQC2-2]
ENST00000361507; ENSP00000354952; ENSG00000033327. [Q9UQC2-1]
GeneIDi9846.
KEGGihsa:9846.
UCSCiuc001ozg.3. human. [Q9UQC2-1]

Polymorphism databases

DMDMi46396035.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018413 mRNA. Translation: BAA76737.1 .
AB011143 mRNA. Translation: BAA25497.2 . Different initiation.
AP002985 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75057.1 .
CH471076 Genomic DNA. Translation: EAW75058.1 .
BC131711 mRNA. Translation: AAI31712.1 .
BC152459 mRNA. Translation: AAI52460.1 .
CCDSi CCDS8259.1. [Q9UQC2-1 ]
CCDS8260.1. [Q9UQC2-2 ]
RefSeqi NP_036428.1. NM_012296.3. [Q9UQC2-2 ]
NP_536739.1. NM_080491.2. [Q9UQC2-1 ]
XP_006718816.1. XM_006718753.1. [Q9UQC2-2 ]
UniGenei Hs.429434.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VWF X-ray 1.58 B 508-522 [» ]
2W0Z X-ray 1.70 B 350-358 [» ]
ProteinModelPortali Q9UQC2.
SMRi Q9UQC2. Positions 27-112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115181. 32 interactions.
DIPi DIP-36653N.
IntActi Q9UQC2. 12 interactions.
MINTi MINT-123618.
STRINGi 9606.ENSP00000302452.

PTM databases

PhosphoSitei Q9UQC2.

Polymorphism databases

DMDMi 46396035.

Proteomic databases

MaxQBi Q9UQC2.
PaxDbi Q9UQC2.
PRIDEi Q9UQC2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340149 ; ENSP00000343959 ; ENSG00000033327 . [Q9UQC2-2 ]
ENST00000361507 ; ENSP00000354952 ; ENSG00000033327 . [Q9UQC2-1 ]
GeneIDi 9846.
KEGGi hsa:9846.
UCSCi uc001ozg.3. human. [Q9UQC2-1 ]

Organism-specific databases

CTDi 9846.
GeneCardsi GC11M077926.
HGNCi HGNC:14458. GAB2.
HPAi CAB022159.
HPA000271.
MIMi 606203. gene.
neXtProti NX_Q9UQC2.
PharmGKBi PA28478.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83177.
GeneTreei ENSGT00510000046662.
HOGENOMi HOG000236270.
HOVERGENi HBG051685.
InParanoidi Q9UQC2.
KOi K08091.
OMAi MQPTLST.
OrthoDBi EOG7T4MJJ.
PhylomeDBi Q9UQC2.
TreeFami TF329487.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinki Q9UQC2.

Miscellaneous databases

ChiTaRSi GAB2. human.
EvolutionaryTracei Q9UQC2.
GeneWikii GAB2.
GenomeRNAii 9846.
NextBioi 37106.
PROi Q9UQC2.
SOURCEi Search...

Gene expression databases

Bgeei Q9UQC2.
CleanExi HS_GAB2.
ExpressionAtlasi Q9UQC2. baseline and differential.
Genevestigatori Q9UQC2.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
PROSITEi PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors."
    Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T., Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.
    Blood 93:1809-1816(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTPN11.
    Tissue: Myeloma.
  2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] (ISOFORMS 1 AND 2).
  7. "Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells."
    Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.
    J. Biol. Chem. 279:21658-21665(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY HCK, INTERACTION WITH HCK; CRKL PTPN11 AND GRB2.
  8. "The molecular scaffold Gab2 is a crucial component of RANK signaling and osteoclastogenesis."
    Wada T., Nakashima T., Oliveira-dos-Santos A.J., Gasser J., Hara H., Schett G., Penninger J.M.
    Nat. Med. 11:394-399(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TNFRSF11A.
  9. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
    Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
    EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR; GRB2; PTPN11; PI-3 KINASE; SFN; SHC1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ, MUTAGENESIS OF SER-210 AND THR-391, PHOSPHORYLATION AT SER-133; SER-140; SER-141; SER-148; SER-149; SER-159; SER-164; SER-210; SER-218; SER-223; SER-264; THR-278; SER-281; THR-287; TYR-293; THR-331; THR-385; THR-391; SER-405; SER-480; SER-543; SER-622 AND SER-623.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Distinct binding modes of two epitopes in Gab2 that interact with the SH3C domain of Grb2."
    Harkiolaki M., Tsirka T., Lewitzky M., Simister P.C., Joshi D., Bird L.E., Jones E.Y., O'Reilly N., Feller S.M.
    Structure 17:809-822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 350-358 IN COMPLEX WITH GRB2, X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 508-522 IN COMPLEX WITH GRB2.

Entry informationi

Entry nameiGAB2_HUMAN
AccessioniPrimary (citable) accession number: Q9UQC2
Secondary accession number(s): A2RRM2
, A6NEW9, A7MD36, O60317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3