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Q9UGK3

- STAP2_HUMAN

UniProt

Q9UGK3 - STAP2_HUMAN

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Protein

Signal-transducing adaptor protein 2

Gene
STAP2, BKS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9UGK3.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal-transducing adaptor protein 2
Short name:
STAP-2
Alternative name(s):
Breast tumor kinase substrate
Short name:
BRK substrate
Gene namesi
Name:STAP2
Synonyms:BKS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:30430. STAP2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221Y → F: Small decrease in tyrosine phosphorylation. 1 Publication
Mutagenesisi250 – 2501Y → F: Loss of tyrosine phosphorylation. 1 Publication
Mutagenesisi310 – 3101Y → F: Decrease in tyrosine phosphorylation. 1 Publication
Mutagenesisi322 – 3221Y → F: Decrease in tyrosine phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA162404971.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Signal-transducing adaptor protein 2PRO_0000072239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphotyrosine; by SRC Inferred
Modified residuei250 – 2501Phosphotyrosine; by PTK62 Publications
Modified residuei310 – 3101Phosphotyrosine Inferred
Modified residuei322 – 3221Phosphotyrosine; by SRC Inferred

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UGK3.
PaxDbiQ9UGK3.
PRIDEiQ9UGK3.

PTM databases

PhosphoSiteiQ9UGK3.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

ArrayExpressiQ9UGK3.
BgeeiQ9UGK3.
CleanExiHS_STAP2.
GenevestigatoriQ9UGK3.

Organism-specific databases

HPAiHPA002375.
HPA027761.

Interactioni

Subunit structurei

Interacts with PTK6 and CSF1R.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKBO149207EBI-1553984,EBI-81266
MYD88Q998363EBI-1553984,EBI-447677

Protein-protein interaction databases

BioGridi120759. 10 interactions.
IntActiQ9UGK3. 5 interactions.
MINTiMINT-1213508.
STRINGi9606.ENSP00000317912.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi148 – 1503
Helixi159 – 16810
Beta strandi174 – 1796
Beta strandi182 – 19110
Beta strandi202 – 2043
Beta strandi215 – 2195
Helixi226 – 23611
Beta strandi237 – 2393

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EL8NMR-A137-247[»]
ProteinModelPortaliQ9UGK3.
SMRiQ9UGK3. Positions 21-247.

Miscellaneous databases

EvolutionaryTraceiQ9UGK3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 130113PHAdd
BLAST
Domaini133 – 248116SH2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili382 – 40221 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi271 – 35989Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 SH2 domain.

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiNOG43046.
HOGENOMiHOG000063725.
HOVERGENiHBG108516.
OMAiPGHLYMM.
PhylomeDBiQ9UGK3.
TreeFamiTF332087.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR001849. PH_domain.
IPR000980. SH2.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UGK3-1) [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

MASALRPPRV PKPKGVLPSH YYESFLEKKG PCDRDYKKFW AGLQGLTIYF    50
YNSNRDFQHV EKLNLGAFEK LTDEIPWGSS RDPGTHFSLI LRDQEIKFKV 100
ETLECREMWK GFILTVVELR VPTDLTLLPG HLYMMSEVLA KEEARRALET 150
PSCFLKVSRL EAQLLLERYP ECGNLLLRPS GDGADGVSVT TRQMHNGTHV 200
VRHYKVKREG PKYVIDVEQP FSCTSLDAVV NYFVSHTKKA LVPFLLDEDY 250
EKVLGYVEAD KENGENVWVA PSAPGPGPAP CTGGPKPLSP ASSQDKLPPL 300
PPLPNQEENY VTPIGDGPAV DYENQDVASS SWPVILKPKK LPKPPAKLPK 350
PPVGPKPEPK VFNGGLGRKL PVSSAQPLFP TAGLADMTAE LQKKLEKRRA 400
LEH 403
Length:403
Mass (Da):44,894
Last modified:May 5, 2009 - v2
Checksum:iA5E809B3F233EFD0
GO
Isoform 2 (identifier: Q9UGK3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     356-356: K → KPVEKGFHHVAQAGLELLTSSDPPTSASQSAGITGVSHHTWPHLSSL

Note: Alu insert from position 358 to 403.

Show »
Length:449
Mass (Da):49,649
Checksum:i31A9048F7B0E750F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931D → N.3 Publications
Corresponds to variant rs7247504 [ dbSNP | Ensembl ].
VAR_055239

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei356 – 3561K → KPVEKGFHHVAQAGLELLTS SDPPTSASQSAGITGVSHHT WPHLSSL in isoform 2. VSP_041403

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ245719 mRNA. Translation: CAB65105.1.
AK000241 mRNA. Translation: BAA91028.1.
AC008616 Genomic DNA. No translation available.
BC000795 mRNA. Translation: AAH00795.1.
CCDSiCCDS12128.1. [Q9UGK3-2]
CCDS45926.1. [Q9UGK3-1]
RefSeqiNP_001013863.1. NM_001013841.1. [Q9UGK3-1]
NP_060190.2. NM_017720.2. [Q9UGK3-2]
UniGeneiHs.194385.

Genome annotation databases

EnsembliENST00000594605; ENSP00000471052; ENSG00000178078. [Q9UGK3-1]
ENST00000600324; ENSP00000468927; ENSG00000178078. [Q9UGK3-2]
GeneIDi55620.
KEGGihsa:55620.
UCSCiuc002mab.3. human. [Q9UGK3-1]
uc002mac.3. human. [Q9UGK3-2]

Polymorphism databases

DMDMi229462752.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ245719 mRNA. Translation: CAB65105.1 .
AK000241 mRNA. Translation: BAA91028.1 .
AC008616 Genomic DNA. No translation available.
BC000795 mRNA. Translation: AAH00795.1 .
CCDSi CCDS12128.1. [Q9UGK3-2 ]
CCDS45926.1. [Q9UGK3-1 ]
RefSeqi NP_001013863.1. NM_001013841.1. [Q9UGK3-1 ]
NP_060190.2. NM_017720.2. [Q9UGK3-2 ]
UniGenei Hs.194385.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EL8 NMR - A 137-247 [» ]
ProteinModelPortali Q9UGK3.
SMRi Q9UGK3. Positions 21-247.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120759. 10 interactions.
IntActi Q9UGK3. 5 interactions.
MINTi MINT-1213508.
STRINGi 9606.ENSP00000317912.

PTM databases

PhosphoSitei Q9UGK3.

Polymorphism databases

DMDMi 229462752.

Proteomic databases

MaxQBi Q9UGK3.
PaxDbi Q9UGK3.
PRIDEi Q9UGK3.

Protocols and materials databases

DNASUi 55620.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000594605 ; ENSP00000471052 ; ENSG00000178078 . [Q9UGK3-1 ]
ENST00000600324 ; ENSP00000468927 ; ENSG00000178078 . [Q9UGK3-2 ]
GeneIDi 55620.
KEGGi hsa:55620.
UCSCi uc002mab.3. human. [Q9UGK3-1 ]
uc002mac.3. human. [Q9UGK3-2 ]

Organism-specific databases

CTDi 55620.
GeneCardsi GC19M004324.
H-InvDB HIX0018702.
HGNCi HGNC:30430. STAP2.
HPAi HPA002375.
HPA027761.
MIMi 607881. gene.
neXtProti NX_Q9UGK3.
PharmGKBi PA162404971.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43046.
HOGENOMi HOG000063725.
HOVERGENi HBG108516.
OMAi PGHLYMM.
PhylomeDBi Q9UGK3.
TreeFami TF332087.

Enzyme and pathway databases

SignaLinki Q9UGK3.

Miscellaneous databases

EvolutionaryTracei Q9UGK3.
GeneWikii STAP2.
GenomeRNAii 55620.
NextBioi 60220.
PROi Q9UGK3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UGK3.
Bgeei Q9UGK3.
CleanExi HS_STAP2.
Genevestigatori Q9UGK3.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR001849. PH_domain.
IPR000980. SH2.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiSTAP2_HUMAN
AccessioniPrimary (citable) accession number: Q9UGK3
Secondary accession number(s): A6NKK3, Q9NXI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 5, 2009
Last modified: September 3, 2014
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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