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Protein

Signal-transducing adaptor protein 1

Gene

STAP1

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

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

  • phospholipid binding Source: BHF-UCL
  • phosphotyrosine binding Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL
  • SH3/SH2 adaptor activity Source: BHF-UCL
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

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
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24133. STAP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162404948.

Polymorphism and mutation databases

BioMutaiSTAP1.
DMDMi62511239.

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.
ExpressionAtlasiQ9ULZ2. baseline and differential.
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
Q5JPT65EBI-6083058,EBI-10244213
ARP102752EBI-6083058,EBI-608057
FAM134CQ86VR23EBI-6083058,EBI-10192441
GAB1Q134803EBI-6083058,EBI-517684
KITP107213EBI-6083058,EBI-1379503
METP085813EBI-6083058,EBI-1039152
SH3KBP1Q96B974EBI-6083058,EBI-346595

Protein-protein interaction databases

BioGridi117619. 12 interactions.
IntActiQ9ULZ2. 8 interactions.
MINTiMINT-8098930.
STRINGi9606.ENSP00000265404.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 annotationAdd
BLAST
Domaini177 – 280104SH2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG47666.
GeneTreeiENSGT00530000063841.
HOGENOMiHOG000234375.
HOVERGENiHBG062262.
InParanoidiQ9ULZ2.
OMAiALPLYFE.
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]

Sequencei

Sequence statusi: Complete.

Q9ULZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLIKRSGYR EYEHYWTELR
60 70 80 90 100
GTTLFFYTDK KSIIYVDKLD IVDLTCLTEQ NSTEKNCAKF TLVLPKEEVQ
110 120 130 140 150
LKTENTESGE EWRGFILTVT ELSVPQNVSL LPGQVIKLHE VLEREKKRRI
160 170 180 190 200
ETEQSTSVEK EKEPTEDYVD VLNPMPACFY TVSRKEATEM LQKNPSLGNM
210 220 230 240 250
ILRPGSDSRN YSITIRQEID IPRIKHYKVM SVGQNYTIEL EKPVTLPNLF
260 270 280 290
SVIDYFVKET RGNLRPFICS TDENTGQEPS MEGRSEKLKK NPHIA
Length:295
Mass (Da):34,291
Last modified:May 1, 2000 - v1
Checksum:i8C242AC5C61038E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006714175.2.
UniGeneiHs.435579.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006714175.2.
UniGeneiHs.435579.

3D structure databases

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

Protein-protein interaction databases

BioGridi117619. 12 interactions.
IntActiQ9ULZ2. 8 interactions.
MINTiMINT-8098930.
STRINGi9606.ENSP00000265404.

PTM databases

PhosphoSiteiQ9ULZ2.

Polymorphism and mutation databases

BioMutaiSTAP1.
DMDMi62511239.

Proteomic databases

MaxQBiQ9ULZ2.
PaxDbiQ9ULZ2.
PeptideAtlasiQ9ULZ2.
PRIDEiQ9ULZ2.

Protocols and materials databases

DNASUi26228.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26228.
GeneCardsiGC04P068424.
HGNCiHGNC:24133. STAP1.
HPAiHPA038529.
MIMi604298. gene.
neXtProtiNX_Q9ULZ2.
PharmGKBiPA162404948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47666.
GeneTreeiENSGT00530000063841.
HOGENOMiHOG000234375.
HOVERGENiHBG062262.
InParanoidiQ9ULZ2.
OMAiALPLYFE.
OrthoDBiEOG79KPFP.
PhylomeDBiQ9ULZ2.
TreeFamiTF332087.

Enzyme and pathway databases

SignaLinkiQ9ULZ2.

Miscellaneous databases

EvolutionaryTraceiQ9ULZ2.
GeneWikiiSTAP1.
GenomeRNAii26228.
NextBioi48387.
PROiQ9ULZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULZ2.
CleanExiHS_STAP1.
ExpressionAtlasiQ9ULZ2. baseline and differential.
GenevestigatoriQ9ULZ2.

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...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.