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Q13480

- GAB1_HUMAN

UniProt

Q13480 - GAB1_HUMAN

Protein

GRB2-associated-binding protein 1

Gene

GAB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (07 Feb 2006)
      Previous versions | rss
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    Functioni

    Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR).

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. SH3/SH2 adaptor activity Source: ProtInc
    3. signal transducer activity Source: Ensembl

    GO - Biological processi

    1. activation of JUN kinase activity Source: Ensembl
    2. cell proliferation Source: ProtInc
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. epidermis development Source: Ensembl
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. fibroblast growth factor receptor signaling pathway Source: Reactome
    7. heart development Source: Ensembl
    8. innate immune response Source: Reactome
    9. insulin receptor signaling pathway Source: Reactome
    10. interleukin-6-mediated signaling pathway Source: Ensembl
    11. labyrinthine layer development Source: Ensembl
    12. neurotrophin TRK receptor signaling pathway Source: Reactome
    13. phosphatidylinositol-mediated signaling Source: Reactome
    14. platelet-derived growth factor receptor signaling pathway Source: Ensembl
    15. regulation of cell migration Source: Ensembl
    16. response to oxidative stress Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_115852. Signaling by constitutively active EGFR.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_121398. Signaling by FGFR mutants.
    REACT_12578. GAB1 signalosome.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21270. PI-3K cascade.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinkiQ13480.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GRB2-associated-binding protein 1
    Alternative name(s):
    GRB2-associated binder 1
    Growth factor receptor bound protein 2-associated protein 1
    Gene namesi
    Name:GAB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4066. GAB1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28477.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 694693GRB2-associated-binding protein 1PRO_0000050282Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei627 – 6271Phosphotyrosine2 Publications
    Modified residuei659 – 6591Phosphotyrosine2 Publications

    Post-translational modificationi

    Phosphorylated in response to FGFR1 activation. Phosphorylated on tyrosine residue(s) by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Tyrosine phosphorylation of GAB1 mediates interaction with several proteins that contain SH2 domains. Phosphorylated on tyrosine residues by HCK upon IL6 signaling.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13480.
    PaxDbiQ13480.
    PRIDEiQ13480.

    PTM databases

    PhosphoSiteiQ13480.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13480.
    BgeeiQ13480.
    CleanExiHS_GAB1.
    GenevestigatoriQ13480.

    Interactioni

    Subunit structurei

    Interacts with GRB2 and with other SH2-containing proteins. Interacts with phosphorylated LAT2. Interacts with PTPRJ. Identified in a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1. Interacts (phosphorylated) with PTPN11. Interacts with HCK.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLKP514513EBI-517684,EBI-2105445
    CRKP461082EBI-517684,EBI-886
    CRKLP461094EBI-517684,EBI-910
    FESP073322EBI-517684,EBI-1055635
    GRB2P629935EBI-517684,EBI-401755
    INPPL1O153572EBI-517684,EBI-1384248
    LCKP0623910EBI-517684,EBI-1348
    LYNP079487EBI-517684,EBI-79452
    NCK1P163333EBI-517684,EBI-389883
    NCK2O436395EBI-517684,EBI-713635
    PIK3R1P2798633EBI-517684,EBI-79464
    PIK3R2O0045923EBI-517684,EBI-346930
    PIK3R3Q9256936EBI-517684,EBI-79893
    PLCG1P1917436EBI-517684,EBI-79387
    PLCG2P1688515EBI-517684,EBI-617403
    PTK6Q138826EBI-517684,EBI-1383632
    PTPN11Q0612439EBI-517684,EBI-297779
    PTPRJQ129132EBI-517684,EBI-2264500
    PXNP490232EBI-517684,EBI-702209
    RASA1P2093625EBI-517684,EBI-1026476
    SH2D1BO147968EBI-517684,EBI-3923013
    SH2D2AQ9NP316EBI-517684,EBI-490630
    SHC1P293539EBI-517684,EBI-78835
    SLA2Q9H6Q34EBI-517684,EBI-1222854
    SOCS3O145434EBI-517684,EBI-714146
    SOCS6O145449EBI-517684,EBI-3929549
    SRCP1293112EBI-517684,EBI-621482
    STAP1Q9ULZ23EBI-517684,EBI-6083058
    SYKP434054EBI-517684,EBI-78302
    TECP426802EBI-517684,EBI-1383480
    VAV1P154982EBI-517684,EBI-625518
    VAV2P527352EBI-517684,EBI-297549
    VAV3Q9UKW46EBI-517684,EBI-297568
    YES1P079477EBI-517684,EBI-515331

    Protein-protein interaction databases

    BioGridi108824. 21 interactions.
    IntActiQ13480. 59 interactions.
    MINTiMINT-140909.
    STRINGi9606.ENSP00000262995.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13480.
    SMRiQ13480. Positions 26-111.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 116112PHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi449 – 54092Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG80382.
    HOGENOMiHOG000236270.
    HOVERGENiHBG051685.
    KOiK09593.
    OMAiQIPRTFP.
    OrthoDBiEOG7T4MJJ.
    PhylomeDBiQ13480.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13480-1) [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

    MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN    50
    DHAKKPIRII DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS 100
    EEEMNKWVRC ICDICGFNPT EEDPVKPPGS SLQAPADLPL AINTAPPSTQ 150
    ADSSSATLPP PYQLINVPPH LETLGIQEDP QDYLLLINCQ SKKPEPTRTH 200
    ADSAKSTSSE TDCNDNVPSH KNPASSQSKH GMNGFFQQQM IYDSPPSRAP 250
    SASVDSSLYN LPRSYSHDVL PKVSPSSTEA DGELYVFNTP SGTSSVETQM 300
    RHVSISYDIP PTPGNTYQIP RTFPEGTLGQ TSKLDTIPDI PPPRPPKPHP 350
    AHDRSPVETC SIPRTASDTD SSYCIPTAGM SPSRSNTIST VDLNKLRKDA 400
    SSQDCYDIPR AFPSDRSSSL EGFHNHFKVK NVLTVGSVSS EELDENYVPM 450
    NPNSPPRQHS SSFTEPIQEA NYVPMTPGTF DFSSFGMQVP PPAHMGFRSS 500
    PKTPPRRPVP VADCEPPPVD RNLKPDRKVK PAPLEIKPLP EWEELQAPVR 550
    SPITRSFARD SSRFPMSPRP DSVHSTTSSS DSHDSEENYV PMNPNLSSED 600
    PNLFGSNSLD GGSSPMIKPK GDKQVEYLDL DLDSGKSTPP RKQKSSGSGS 650
    SVADERVDYV VVDQQKTLAL KSTREAWTDG RQSTESETPA KSVK 694
    Length:694
    Mass (Da):76,616
    Last modified:February 7, 2006 - v2
    Checksum:iE0FAC78772B6677B
    GO
    Isoform 2 (identifier: Q13480-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         528-528: K → KGQSPKILRLKPHGLERTDSQTIGDFATRRK

    Note: Contains a phosphoserine at position 547.

    Show »
    Length:724
    Mass (Da):80,005
    Checksum:iEAA4573B9E5A25B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti204 – 2041A → G in AAC50380. (PubMed:8596638)Curated
    Sequence conflicti213 – 2131C → S in AAC50380. (PubMed:8596638)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831Y → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036132
    Natural varianti311 – 3111P → L.1 Publication
    Corresponds to variant rs28925904 [ dbSNP | Ensembl ].
    VAR_025261
    Natural varianti377 – 3771T → I.
    Corresponds to variant rs2229879 [ dbSNP | Ensembl ].
    VAR_053096
    Natural varianti387 – 3871T → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036133

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei528 – 5281K → KGQSPKILRLKPHGLERTDS QTIGDFATRRK in isoform 2. 1 PublicationVSP_017137

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43885 mRNA. Translation: AAC50380.1.
    DQ021880 Genomic DNA. Translation: AAY26398.1.
    AK289767 mRNA. Translation: BAF82456.1.
    AC097658 Genomic DNA. No translation available.
    AC104685 Genomic DNA. Translation: AAY40964.1.
    CH471056 Genomic DNA. Translation: EAX05072.1.
    BC064848 mRNA. Translation: AAH64848.1.
    CCDSiCCDS3759.1. [Q13480-1]
    CCDS3760.1. [Q13480-2]
    PIRiS68442.
    RefSeqiNP_002030.2. NM_002039.3. [Q13480-1]
    NP_997006.1. NM_207123.2. [Q13480-2]
    UniGeneiHs.618456.
    Hs.80720.

    Genome annotation databases

    EnsembliENST00000262994; ENSP00000262994; ENSG00000109458. [Q13480-1]
    ENST00000262995; ENSP00000262995; ENSG00000109458. [Q13480-2]
    GeneIDi2549.
    KEGGihsa:2549.
    UCSCiuc003ijd.3. human. [Q13480-2]
    uc003ije.3. human. [Q13480-1]

    Polymorphism databases

    DMDMi90180201.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43885 mRNA. Translation: AAC50380.1 .
    DQ021880 Genomic DNA. Translation: AAY26398.1 .
    AK289767 mRNA. Translation: BAF82456.1 .
    AC097658 Genomic DNA. No translation available.
    AC104685 Genomic DNA. Translation: AAY40964.1 .
    CH471056 Genomic DNA. Translation: EAX05072.1 .
    BC064848 mRNA. Translation: AAH64848.1 .
    CCDSi CCDS3759.1. [Q13480-1 ]
    CCDS3760.1. [Q13480-2 ]
    PIRi S68442.
    RefSeqi NP_002030.2. NM_002039.3. [Q13480-1 ]
    NP_997006.1. NM_207123.2. [Q13480-2 ]
    UniGenei Hs.618456.
    Hs.80720.

    3D structure databases

    ProteinModelPortali Q13480.
    SMRi Q13480. Positions 26-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108824. 21 interactions.
    IntActi Q13480. 59 interactions.
    MINTi MINT-140909.
    STRINGi 9606.ENSP00000262995.

    PTM databases

    PhosphoSitei Q13480.

    Polymorphism databases

    DMDMi 90180201.

    Proteomic databases

    MaxQBi Q13480.
    PaxDbi Q13480.
    PRIDEi Q13480.

    Protocols and materials databases

    DNASUi 2549.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262994 ; ENSP00000262994 ; ENSG00000109458 . [Q13480-1 ]
    ENST00000262995 ; ENSP00000262995 ; ENSG00000109458 . [Q13480-2 ]
    GeneIDi 2549.
    KEGGi hsa:2549.
    UCSCi uc003ijd.3. human. [Q13480-2 ]
    uc003ije.3. human. [Q13480-1 ]

    Organism-specific databases

    CTDi 2549.
    GeneCardsi GC04P144257.
    H-InvDB HIX0004529.
    HGNCi HGNC:4066. GAB1.
    MIMi 604439. gene.
    neXtProti NX_Q13480.
    PharmGKBi PA28477.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80382.
    HOGENOMi HOG000236270.
    HOVERGENi HBG051685.
    KOi K09593.
    OMAi QIPRTFP.
    OrthoDBi EOG7T4MJJ.
    PhylomeDBi Q13480.
    TreeFami TF329487.

    Enzyme and pathway databases

    Reactomei REACT_115852. Signaling by constitutively active EGFR.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_121398. Signaling by FGFR mutants.
    REACT_12578. GAB1 signalosome.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21270. PI-3K cascade.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinki Q13480.

    Miscellaneous databases

    GeneWikii GAB1.
    GenomeRNAii 2549.
    NextBioi 10055.
    PROi Q13480.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13480.
    Bgeei Q13480.
    CleanExi HS_GAB1.
    Genevestigatori Q13480.

    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

    1. "A Grb2-associated docking protein in EGF- and insulin-receptor signalling."
      Holgado-Madruga M., Emlet D.R., Moscatello D.K., Godwin A.K., Wong A.J.
      Nature 379:560-564(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-311.
    3. "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.
      , 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] (ISOFORM 1).
      Tissue: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Testis.
    7. Cited for: INTERACTION WITH LAT2.
    8. "Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
      Palka H.L., Park M., Tonks N.K.
      J. Biol. Chem. 278:5728-5735(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPRJ.
    9. "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.
    10. "Cellular signaling by fibroblast growth factor receptors."
      Eswarakumar V.P., Lax I., Schlessinger J.
      Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN FGFR1 SIGNALING; SUBUNIT AND PHOSPHORYLATION.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-659, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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 TYR-627, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-83 AND ASN-387.

    Entry informationi

    Entry nameiGAB1_HUMAN
    AccessioniPrimary (citable) accession number: Q13480
    Secondary accession number(s): A8K152, Q4W5G2, Q6P1W2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3