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Q9UGK3 (STAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal-transducing adaptor protein 2

Short name=STAP-2
Alternative name(s):
Breast tumor kinase substrate
Short name=BRK substrate
Gene names
Name:STAP2
Synonyms:BKS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate of protein kinase PTK6. May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity. Ref.1

Subunit structure

Interacts with PTK6 and CSF1R. Ref.1 Ref.6

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Widely expressed. Ref.1 Ref.5

Post-translational modification

Phosphorylated on tyrosine. Tyr-250 may be important for interaction with kinases. Phosphorylated by PTK6 at Tyr-250 modulates PTK6-mediated STAT3 activation. Tyr-22 and Tyr-322 appears to be phosphorylated by SRC. Ref.5 Ref.6

Sequence similarities

Contains 1 PH domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
SH2 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16365431. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKBKBO149207EBI-1553984,EBI-81266
MYD88Q998363EBI-1553984,EBI-447677

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UGK3-1)

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.
Isoform 2 (identifier: Q9UGK3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     356-356: K → KPVEKGFHHVAQAGLELLTSSDPPTSASQSAGITGVSHHTWPHLSSL
Note: Alu insert from position 358 to 403.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Signal-transducing adaptor protein 2
PRO_0000072239

Regions

Domain18 – 130113PH
Domain133 – 248116SH2
Coiled coil382 – 40221 Potential
Compositional bias271 – 35989Pro-rich

Amino acid modifications

Modified residue221Phosphotyrosine; by SRC Probable
Modified residue2501Phosphotyrosine; by PTK6 Ref.5 Ref.6
Modified residue3101Phosphotyrosine Probable
Modified residue3221Phosphotyrosine; by SRC Probable

Natural variations

Alternative sequence3561K → KPVEKGFHHVAQAGLELLTS SDPPTSASQSAGITGVSHHT WPHLSSL in isoform 2.
VSP_041403
Natural variant931D → N. Ref.1 Ref.2 Ref.4
Corresponds to variant rs7247504 [ dbSNP | Ensembl ].
VAR_055239

Experimental info

Mutagenesis221Y → F: Small decrease in tyrosine phosphorylation. Ref.5
Mutagenesis2501Y → F: Loss of tyrosine phosphorylation. Ref.5
Mutagenesis3101Y → F: Decrease in tyrosine phosphorylation. Ref.5
Mutagenesis3221Y → F: Decrease in tyrosine phosphorylation. Ref.5

Secondary structure

................ 403
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: A5E809B3F233EFD0

FASTA40344,894
        10         20         30         40         50         60 
MASALRPPRV PKPKGVLPSH YYESFLEKKG PCDRDYKKFW AGLQGLTIYF YNSNRDFQHV 

        70         80         90        100        110        120 
EKLNLGAFEK LTDEIPWGSS RDPGTHFSLI LRDQEIKFKV ETLECREMWK GFILTVVELR 

       130        140        150        160        170        180 
VPTDLTLLPG HLYMMSEVLA KEEARRALET PSCFLKVSRL EAQLLLERYP ECGNLLLRPS 

       190        200        210        220        230        240 
GDGADGVSVT TRQMHNGTHV VRHYKVKREG PKYVIDVEQP FSCTSLDAVV NYFVSHTKKA 

       250        260        270        280        290        300 
LVPFLLDEDY EKVLGYVEAD KENGENVWVA PSAPGPGPAP CTGGPKPLSP ASSQDKLPPL 

       310        320        330        340        350        360 
PPLPNQEENY VTPIGDGPAV DYENQDVASS SWPVILKPKK LPKPPAKLPK PPVGPKPEPK 

       370        380        390        400 
VFNGGLGRKL PVSSAQPLFP TAGLADMTAE LQKKLEKRRA LEH 

« Hide

Isoform 2 [UniParc].

Checksum: 31A9048F7B0E750F
Show »

FASTA44949,649

References

« Hide 'large scale' references
[1]"A novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRK."
Mitchell P.J., Sara E.A., Crompton M.R.
Oncogene 19:4273-4282(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PTK6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ASN-93.
Tissue: Mammary gland.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASN-93.
Tissue: Colon mucosa.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 1), VARIANT ASN-93.
Tissue: Placenta.
[5]"STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation in acute-phase response through its YXXQ motif."
Minoguchi M., Minoguchi S., Aki D., Joo A., Yamamoto T., Yumioka T., Matsuda T., Yoshimura A.
J. Biol. Chem. 278:11182-11189(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-22; TYR-250; TYR-310 AND TYR-322, MUTAGENESIS OF TYR-22; TYR-250; TYR-310 AND TYR-322.
[6]"STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation."
Ikeda O., Miyasaka Y., Sekine Y., Mizushima A., Muromoto R., Nanbo A., Yoshimura A., Matsuda T.
Biochem. Biophys. Res. Commun. 384:71-75(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-250 BY PTK6, INTERACTION WITH PTK6.
[7]"Solution structure of the human STAP2 SH2 domain."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 137-247.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245719 mRNA. Translation: CAB65105.1.
AK000241 mRNA. Translation: BAA91028.1.
AC008616 Genomic DNA. No translation available.
BC000795 mRNA. Translation: AAH00795.1.
CCDSCCDS12128.1. [Q9UGK3-2]
CCDS45926.1. [Q9UGK3-1]
RefSeqNP_001013863.1. NM_001013841.1. [Q9UGK3-1]
NP_060190.2. NM_017720.2. [Q9UGK3-2]
UniGeneHs.194385.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EL8NMR-A137-247[»]
ProteinModelPortalQ9UGK3.
SMRQ9UGK3. Positions 21-247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120759. 10 interactions.
IntActQ9UGK3. 5 interactions.
MINTMINT-1213508.
STRING9606.ENSP00000317912.

PTM databases

PhosphoSiteQ9UGK3.

Polymorphism databases

DMDM229462752.

Proteomic databases

MaxQBQ9UGK3.
PaxDbQ9UGK3.
PRIDEQ9UGK3.

Protocols and materials databases

DNASU55620.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000594605; ENSP00000471052; ENSG00000178078. [Q9UGK3-1]
ENST00000600324; ENSP00000468927; ENSG00000178078. [Q9UGK3-2]
GeneID55620.
KEGGhsa:55620.
UCSCuc002mab.3. human. [Q9UGK3-1]
uc002mac.3. human. [Q9UGK3-2]

Organism-specific databases

CTD55620.
GeneCardsGC19M004324.
H-InvDBHIX0018702.
HGNCHGNC:30430. STAP2.
HPAHPA002375.
HPA027761.
MIM607881. gene.
neXtProtNX_Q9UGK3.
PharmGKBPA162404971.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43046.
HOGENOMHOG000063725.
HOVERGENHBG108516.
OMAPGHLYMM.
PhylomeDBQ9UGK3.
TreeFamTF332087.

Enzyme and pathway databases

SignaLinkQ9UGK3.

Gene expression databases

ArrayExpressQ9UGK3.
BgeeQ9UGK3.
CleanExHS_STAP2.
GenevestigatorQ9UGK3.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR001849. Pleckstrin_homology.
IPR000980. SH2.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UGK3.
GeneWikiSTAP2.
GenomeRNAi55620.
NextBio60220.
PROQ9UGK3.
SOURCESearch...

Entry information

Entry nameSTAP2_HUMAN
AccessionPrimary (citable) accession number: Q9UGK3
Secondary accession number(s): A6NKK3, Q9NXI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM