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Q9ULZ2

- STAP1_HUMAN

UniProt

Q9ULZ2 - STAP1_HUMAN

Protein

Signal-transducing adaptor protein 1

Gene

STAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    In BCR signaling, appears to function as a docking protein acting downstream of TEC and participates in a positive feedback loop by increasing the activity of TEC.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. intracellular protein transport Source: ProtInc
    2. membrane fusion Source: ProtInc
    3. positive regulation of signal transduction Source: GOC
    4. signal transduction Source: ProtInc
    5. transmembrane receptor protein tyrosine kinase signaling pathway Source: Ensembl

    Enzyme and pathway databases

    SignaLinkiQ9ULZ2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal-transducing adaptor protein 1
    Short name:
    STAP-1
    Alternative name(s):
    BCR downstream-signaling protein 1
    Docking protein BRDG1
    Stem cell adaptor protein 1
    Gene namesi
    Name:STAP1
    Synonyms:BRDG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:24133. STAP1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. mitochondrion Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. protein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162404948.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Signal-transducing adaptor protein 1PRO_0000072237Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei168 – 1681PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine by TEC. Phosphorylated on tyrosine by KIT By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULZ2.
    PaxDbiQ9ULZ2.
    PeptideAtlasiQ9ULZ2.
    PRIDEiQ9ULZ2.

    PTM databases

    PhosphoSiteiQ9ULZ2.

    Expressioni

    Gene expression databases

    BgeeiQ9ULZ2.
    CleanExiHS_STAP1.
    GenevestigatoriQ9ULZ2.

    Organism-specific databases

    HPAiHPA038529.

    Interactioni

    Subunit structurei

    Interacts with KIT and CSF1R By similarity. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth-dependent manner.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102752EBI-6083058,EBI-608057
    GAB1Q134803EBI-6083058,EBI-517684
    KITP107213EBI-6083058,EBI-1379503
    METP085813EBI-6083058,EBI-1039152
    SH3KBP1Q96B974EBI-6083058,EBI-346595

    Protein-protein interaction databases

    BioGridi117619. 6 interactions.
    IntActiQ9ULZ2. 6 interactions.
    MINTiMINT-8098930.
    STRINGi9606.ENSP00000265404.

    Structurei

    Secondary structure

    1
    295
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 243
    Beta strandi26 – 3510
    Beta strandi43 – 508
    Beta strandi53 – 586
    Beta strandi66 – 683
    Beta strandi76 – 794
    Beta strandi89 – 935
    Beta strandi99 – 1024
    Helixi106 – 12116
    Helixi132 – 14918
    Helixi184 – 19310
    Helixi195 – 1973
    Beta strandi199 – 2046
    Beta strandi208 – 21710
    Beta strandi219 – 2213
    Beta strandi223 – 23210
    Beta strandi235 – 2384
    Beta strandi240 – 2423
    Beta strandi244 – 2485
    Helixi249 – 25911
    Turni260 – 2623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X1FNMR-A16-151[»]
    3MAZX-ray1.90A167-285[»]
    ProteinModelPortaliQ9ULZ2.
    SMRiQ9ULZ2. Positions 16-156, 171-268.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ULZ2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 12197PHPROSITE-ProRule annotationsAdd
    BLAST
    Domaini177 – 280104SH2PROSITE-ProRule annotationsAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotations
    Contains 1 SH2 domain.PROSITE-ProRule annotations

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG47666.
    HOGENOMiHOG000234375.
    HOVERGENiHBG062262.
    InParanoidiQ9ULZ2.
    OMAiPMPACFY.
    OrthoDBiEOG79KPFP.
    PhylomeDBiQ9ULZ2.
    TreeFamiTF332087.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000980. SH2.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    Q9ULZ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLIKRSGYR EYEHYWTELR    50
    GTTLFFYTDK KSIIYVDKLD IVDLTCLTEQ NSTEKNCAKF TLVLPKEEVQ 100
    LKTENTESGE EWRGFILTVT ELSVPQNVSL LPGQVIKLHE VLEREKKRRI 150
    ETEQSTSVEK EKEPTEDYVD VLNPMPACFY TVSRKEATEM LQKNPSLGNM 200
    ILRPGSDSRN YSITIRQEID IPRIKHYKVM SVGQNYTIEL EKPVTLPNLF 250
    SVIDYFVKET RGNLRPFICS TDENTGQEPS MEGRSEKLKK NPHIA 295
    Length:295
    Mass (Da):34,291
    Last modified:May 1, 2000 - v1
    Checksum:i8C242AC5C61038E0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023483 mRNA. Translation: BAA85311.1.
    AK313676 mRNA. Translation: BAG36427.1.
    CH471057 Genomic DNA. Translation: EAX05547.1.
    BC014958 mRNA. Translation: AAH14958.1.
    CCDSiCCDS3515.1.
    RefSeqiNP_036240.1. NM_012108.2.
    XP_006714238.1. XM_006714175.1.
    UniGeneiHs.435579.

    Genome annotation databases

    EnsembliENST00000265404; ENSP00000265404; ENSG00000035720.
    ENST00000396225; ENSP00000379527; ENSG00000035720.
    GeneIDi26228.
    KEGGihsa:26228.
    UCSCiuc003hde.4. human.

    Polymorphism databases

    DMDMi62511239.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023483 mRNA. Translation: BAA85311.1 .
    AK313676 mRNA. Translation: BAG36427.1 .
    CH471057 Genomic DNA. Translation: EAX05547.1 .
    BC014958 mRNA. Translation: AAH14958.1 .
    CCDSi CCDS3515.1.
    RefSeqi NP_036240.1. NM_012108.2.
    XP_006714238.1. XM_006714175.1.
    UniGenei Hs.435579.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X1F NMR - A 16-151 [» ]
    3MAZ X-ray 1.90 A 167-285 [» ]
    ProteinModelPortali Q9ULZ2.
    SMRi Q9ULZ2. Positions 16-156, 171-268.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117619. 6 interactions.
    IntActi Q9ULZ2. 6 interactions.
    MINTi MINT-8098930.
    STRINGi 9606.ENSP00000265404.

    PTM databases

    PhosphoSitei Q9ULZ2.

    Polymorphism databases

    DMDMi 62511239.

    Proteomic databases

    MaxQBi Q9ULZ2.
    PaxDbi Q9ULZ2.
    PeptideAtlasi Q9ULZ2.
    PRIDEi Q9ULZ2.

    Protocols and materials databases

    DNASUi 26228.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265404 ; ENSP00000265404 ; ENSG00000035720 .
    ENST00000396225 ; ENSP00000379527 ; ENSG00000035720 .
    GeneIDi 26228.
    KEGGi hsa:26228.
    UCSCi uc003hde.4. human.

    Organism-specific databases

    CTDi 26228.
    GeneCardsi GC04P068424.
    HGNCi HGNC:24133. STAP1.
    HPAi HPA038529.
    MIMi 604298. gene.
    neXtProti NX_Q9ULZ2.
    PharmGKBi PA162404948.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47666.
    HOGENOMi HOG000234375.
    HOVERGENi HBG062262.
    InParanoidi Q9ULZ2.
    OMAi PMPACFY.
    OrthoDBi EOG79KPFP.
    PhylomeDBi Q9ULZ2.
    TreeFami TF332087.

    Enzyme and pathway databases

    SignaLinki Q9ULZ2.

    Miscellaneous databases

    EvolutionaryTracei Q9ULZ2.
    GeneWikii STAP1.
    GenomeRNAii 26228.
    NextBioi 48387.
    PROi Q9ULZ2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ULZ2.
    CleanExi HS_STAP1.
    Genevestigatori Q9ULZ2.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000980. SH2.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase."
      Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A., Yamashita Y., Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.
      Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION BY TEC.
      Tissue: Hematopoietic.
    2. "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].
      Tissue: Thalamus.
    3. 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].
      Tissue: B-cell.
    5. "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
      Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
      Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH URI1, SUBCELLULAR LOCATION.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Solution structure of the PH domain of human docking protein BRDG1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 16-151.

    Entry informationi

    Entry nameiSTAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULZ2
    Secondary accession number(s): B2R980
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 112 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 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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