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Q3UND0 (SKAP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Src kinase-associated phosphoprotein 2
Alternative name(s):
Pyk2/RAFTK-associated protein
SKAP55 homolog
Short name=SKAP-HOM
Src family-associated phosphoprotein 2
Src kinase-associated phosphoprotein 55-related protein
Src-associated adapter protein with PH and SH3 domains
Gene names
Name:Skap2
Synonyms:Prap, Ra70, Saps, Scap2, Skap55r
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. Ref.1 Ref.10 Ref.11

Subunit structure

Interacts with LAT, GRB2, PTK2B and PRAM1 By similarity. Homodimer. Interacts with FYB, which is required for SKAP2 protein stability. Interacts with PTPNS1. Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3. May interact with actin. May interact with FYN, HCK and LYN. Interacts with FASLG By similarity. Ref.1 Ref.7 Ref.8 Ref.10 Ref.13 Ref.15

Subcellular location

Cytoplasm. Note: Membrane ruffles of macrophages. Perikarya and dendrites from neurons. Ref.1 Ref.9 Ref.15

Tissue specificity

Expressed in kidney, lung, liver, spleen, bone marrow and testis. Present in T-cells, B-cells, and all cells of the myelomonocytic lineage. Present in all brain regions, with highest levels in neurons from the Purkinje cell layer, hippocampal gyrus, cortex and substantia nigra (at protein level). Ref.1 Ref.9 Ref.10 Ref.11

Induction

By IL-6 in myeloid cells. Ref.1

Domain

The SH3 domain interacts with FYB and PTK2B By similarity.

Post-translational modification

Dephosphorylated on Tyr-75 by PTPN22 By similarity. Phosphorylated by FYN on Tyr-260. In case of infection with Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase yopH. Ref.1 Ref.7 Ref.10

Disruption phenotype

Mice are healthy and do not display any obvious abnormality. They have normal T-cell, platelet and macrophage function, but show reduced levels of spontaneous immunoglobulins in the serum, and defects in B-cell proliferation. Ref.11

Sequence similarities

Belongs to the SKAP family.

Contains 1 PH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processB-cell activation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.1. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3UND0-1)

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: Q3UND0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-28: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Src kinase-associated phosphoprotein 2
PRO_0000270180

Regions

Domain116 – 219104PH
Domain296 – 35762SH3
Region14 – 6451Homodimerization

Amino acid modifications

Modified residue751Phosphotyrosine Ref.12 Ref.14
Modified residue1511Phosphotyrosine Ref.14
Modified residue2601Phosphotyrosine; by FYN Ref.1 Ref.12 Ref.14

Natural variations

Alternative sequence22 – 287Missing in isoform 2.
VSP_022184

Experimental info

Mutagenesis2601Y → F: Abolishes interaction with FYN, phosphorylation by FYN, and effects on cell growth. Ref.1
Sequence conflict161E → K in BAE25817. Ref.4
Sequence conflict1041N → P AA sequence Ref.7

Secondary structure

.................................... 358
Helix Strand Turn

Details...

Sequences

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

Last modified January 9, 2007. Version 2.
Checksum: B66973A656E44E05

FASTA35840,712
        10         20         30         40         50         60 
MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK KIKDVKSVYL 

        70         80         90        100        110        120 
QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP SDGNQFPPIA AQDLPFVIKA 

       130        140        150        160        170        180 
GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD 

       190        200        210        220        230        240 
GKKDCCFEIC APDKRIYQFT AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV 

       250        260        270        280        290        300 
DHPAAVSSPQ RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF 

       310        320        330        340        350 
YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA YLMEMYDI 

« Hide

Isoform 2 [UniParc].

Checksum: A6C08305272498D8
Show »

FASTA35139,950

References

« Hide 'large scale' references
[1]"Adaptor protein SKAP55R is associated with myeloid differentiation and growth arrest."
Curtis D.J., Jane S.M., Hilton D.J., Dougherty L., Bodine D.M., Begley C.G.
Exp. Hematol. 28:1250-1259(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN, PHOSPHORYLATION AT TYR-260, MUTAGENESIS OF TYR-260, FUNCTION.
Tissue: Testis.
[2]"Mouse Saps, Src-associated adaptor protein with PH and SH3 domain."
Lee J.-S., Suh K.S., Burr J.G.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[3]"RA70, retinoic acid responsive gene, is expressed specifically in spermatocyte in mouse testis."
Momoi T., Urase K., Mukasa T., Fujita E., Kouroku Y., Miho Y., Soyama A., Momoi M.Y.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Lymph node.
[5]"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] (ISOFORMS 1 AND 2).
[6]"SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55."
Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.
FEBS Lett. 435:55-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Tissue: T-cell.
[7]"The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages."
Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.
Cell. Microbiol. 2:401-414(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 93-114; 129-139 AND 147-158, PHOSPHORYLATION, INTERACTION WITH FYB, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1, IDENTIFICATION IN A COMPLEX WITH FYB AND LILRB3.
[8]"SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages."
Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E., Schraven B., Neel B.G.
Curr. Biol. 9:927-930(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPNS1, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1.
[9]"Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation."
Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H., Avraham S., Yasuda M., Matsumoto M.
J. Biol. Chem. 278:42225-42233(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Macrophage colony-stimulating factor receptor induces tyrosine phosphorylation of SKAP55R adaptor and its association with actin."
Bourette R.P., Therier J., Mouchiroud G.
Cell. Signal. 17:941-949(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH ACTIN, FUNCTION.
[11]"Regulation of in vitro and in vivo immune functions by the cytosolic adaptor protein SKAP-HOM."
Togni M., Swanson K.D., Reimann S., Kliche S., Pearce A.C., Simeoni L., Reinhold D., Wienands J., Neel B.G., Schraven B., Gerber A.
Mol. Cell. Biol. 25:8052-8063(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[12]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75 AND TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-IX-V and other agonists."
Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K., Ruggeri Z.M., Schraven B., Neel B.G., Koretzky G., Shattil S.J.
Blood 109:1018-1025(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FYB.
[14]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-151 AND TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[15]"The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch."
Swanson K.D., Tang Y., Ceccarelli D.F., Poy F., Sliwa J.P., Neel B.G., Eck M.J.
Mol. Cell 32:564-575(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-222, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF051324 mRNA. Translation: AAC99297.1.
AB014485 mRNA. Translation: BAA77253.1.
AK076000 mRNA. Translation: BAC36111.1.
AK144289 mRNA. Translation: BAE25817.1.
BC003711 mRNA. Translation: AAH03711.1.
RefSeqNP_061243.1. NM_018773.2.
UniGeneMm.221479.
Mm.392558.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5EX-ray2.60A/B14-222[»]
1U5FX-ray1.90A111-248[»]
1U5GX-ray2.10A/B/C/D103-222[»]
2OTXX-ray2.60A/B14-222[»]
ProteinModelPortalQ3UND0.
SMRQ3UND0. Positions 14-222, 299-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207619. 1 interaction.
IntActQ3UND0. 1 interaction.
MINTMINT-263820.

Proteomic databases

PaxDbQ3UND0.
PRIDEQ3UND0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000078214; ENSMUSP00000077342; ENSMUSG00000059182. [Q3UND0-1]
GeneID54353.
KEGGmmu:54353.
UCSCuc009bxv.1. mouse. [Q3UND0-1]
uc009bxw.1. mouse. [Q3UND0-2]

Organism-specific databases

CTD8935.
MGIMGI:1889206. Skap2.

Phylogenomic databases

eggNOGNOG46742.
GeneTreeENSGT00390000017856.
HOGENOMHOG000231109.
HOVERGENHBG052827.
InParanoidQ3UND0.
OMAWDCTGAL.
OrthoDBEOG7K6PVB.
PhylomeDBQ3UND0.
TreeFamTF331055.

Gene expression databases

BgeeQ3UND0.
CleanExMM_SKAP2.
GenevestigatorQ3UND0.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ3UND0.
NextBio311138.
PROQ3UND0.
SOURCESearch...

Entry information

Entry nameSKAP2_MOUSE
AccessionPrimary (citable) accession number: Q3UND0
Secondary accession number(s): Q8BK74, Q9Z2K4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot