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Reviewed, UniProtKB/Swiss-Prot Q9ULZ2 (STAP1_HUMAN)

Last modified November 3, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Signal-transducing adaptor protein 1
      Short name=STAP-1
Alternative name(s):
    Stem cell adaptor protein 1
    BCR downstream-signaling protein 1
    Docking protein BRDG1
Gene names
Name: STAP1
Synonyms: BRDG1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.1

Subcellular location

Cytoplasm Potential.

Post-translational modification

Phosphorylated on tyrosine by TEC. Ref.1 Ref.5

Sequence similarities

Contains 1 PH domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainSH2 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processintracellular protein transport Ref.1

Traceable author statement. Source: ProtInc

membrane fusion Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Signal-transducing adaptor protein 1
PRO_0000072237

Regions

Domain25 – 12197PH
Domain177 – 280104SH2

Amino acid modifications

Modified residue1681Phosphotyrosine By similarity
Modified residue1961Phosphoserine Ref.5

Secondary structure

..................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ULZ2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8C242AC5C61038E0

FASTA29534,291
        10         20         30         40         50         60 
MMAKKPPKPA PRRIFQERLK ITALPLYFEG FLLIKRSGYR EYEHYWTELR GTTLFFYTDK 

        70         80         90        100        110        120 
KSIIYVDKLD IVDLTCLTEQ NSTEKNCAKF TLVLPKEEVQ LKTENTESGE EWRGFILTVT 

       130        140        150        160        170        180 
ELSVPQNVSL LPGQVIKLHE VLEREKKRRI ETEQSTSVEK EKEPTEDYVD VLNPMPACFY 

       190        200        210        220        230        240 
TVSRKEATEM LQKNPSLGNM ILRPGSDSRN YSITIRQEID IPRIKHYKVM SVGQNYTIEL 

       250        260        270        280        290 
EKPVTLPNLF SVIDYFVKET RGNLRPFICS TDENTGQEPS MEGRSEKLKK NPHIA 

« Hide

References

« Hide 'large scale' references
[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: 10518561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION.
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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thalamus.
[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 (JUL-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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: B-cell.
[5]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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.

Cross-references

Sequence databases

AB023483 mRNA. Translation: BAA85311.1.
AK313676 mRNA. Translation: BAG36427.1.
CH471057 Genomic DNA. Translation: EAX05547.1.
BC014958 mRNA. Translation: AAH14958.1.
IPIIPI00015876.
RefSeqNP_036240.1.
UniGeneHs.435579

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1X1FNMR-A16-151[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ULZ2.

PTM databases

PhosphoSiteQ9ULZ2.

Proteomic databases

PeptideAtlasQ9ULZ2.

Genome annotation databases

EnsemblENST00000265404; ENSP00000265404; ENSG00000035720; Homo sapiens. [Genome view]
ENST00000396225; ENSP00000379527; ENSG00000035720; Homo sapiens. [Genome view]
GeneID26228.
KEGGhsa:26228.
UCSCuc003hde.2. human.

Organism-specific databases

CTD26228.
GeneCardsGC04P068108.
H-InvDBHIX0004249.
HGNCHGNC:24133. STAP1.
MIM604298. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9ULZ2.
HOVERGENQ9ULZ2.
OMAPMPACFY.

Enzyme and pathway databases

Pathway_Interaction_DBkitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).

Gene expression databases

ArrayExpressQ9ULZ2.
BgeeQ9ULZ2.
CleanExHS_STAP1.
GenevestigatorQ9ULZ2.
GermOnlineENSG00000035720. Homo sapiens.

Family and domain databases

InterProIPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR000980. SH2.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.30.505.10. SH2. 1 hit.
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio48387.
SOURCESearch...

Entry information

Entry nameSTAP1_HUMAN
AccessionPrimary (citable) accession number: Q9ULZ2
Secondary accession number(s): B2R980
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents