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Protein

Src kinase-associated phosphoprotein 2

Gene

SKAP2

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. B cell activation Source: UniProtKB-KW
  2. negative regulation of cell proliferation Source: Ensembl
  3. positive regulation of signal transduction Source: GOC
  4. protein complex assembly Source: ProtInc
  5. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

B-cell activation

Enzyme and pathway databases

ReactomeiREACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinkiO75563.

Names & Taxonomyi

Protein namesi
Recommended name:
Src kinase-associated phosphoprotein 2
Alternative name(s):
Pyk2/RAFTK-associated protein
Retinoic acid-induced protein 70
SKAP55 homolog
Short name:
SKAP-55HOM
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 namesi
Name:SKAP2
Synonyms:PRAP, RA70, SAPS, SCAP2, SKAP55R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:15687. SKAP2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: HPA
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162403393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Src kinase-associated phosphoprotein 2PRO_0000270179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei75 – 751Phosphotyrosine1 Publication
Modified residuei151 – 1511PhosphotyrosineBy similarity
Modified residuei197 – 1971Phosphotyrosine1 Publication
Modified residuei261 – 2611PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-261 upon T-cell activation (Probable). Dephosphorylated on Tyr-75 by PTPN22.Curated5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75563.
PaxDbiO75563.
PRIDEiO75563.

2D gel databases

OGPiO75563.

PTM databases

PhosphoSiteiO75563.

Expressioni

Tissue specificityi

Ubiquitously expressed. Present in platelets (at protein level).3 Publications

Inductioni

By retinoic acid.2 Publications

Gene expression databases

BgeeiO75563.
CleanExiHS_SKAP2.
ExpressionAtlasiO75563. baseline and differential.
GenevestigatoriO75563.

Organism-specific databases

HPAiHPA005560.
HPA024045.

Interactioni

Subunit structurei

Homodimer (By similarity). 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 (By similarity). Interacts with FYB, which is required for SKAP2 protein stability. Interacts with LAT, GRB2, PTK2B and PRAM1. May interact with FYN, HCK and LYN. Interacts with FASLG.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN22Q9Y2R23EBI-2483161,EBI-1211241

Protein-protein interaction databases

BioGridi114448. 12 interactions.
IntActiO75563. 4 interactions.
STRINGi9606.ENSP00000005587.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OMHX-ray2.90E/F/G/H71-79[»]
ProteinModelPortaliO75563.
SMRiO75563. Positions 14-221, 304-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 219104PHPROSITE-ProRule annotationAdd
BLAST
Domaini297 – 35862SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 6451HomodimerizationBy similarityAdd
BLAST

Domaini

The SH3 domain interacts with FYB and PTK2B.

Sequence similaritiesi

Belongs to the SKAP family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG46742.
GeneTreeiENSGT00390000017856.
HOGENOMiHOG000231109.
HOVERGENiHBG052827.
InParanoidiO75563.
OMAiWDCTGAL.
OrthoDBiEOG7K6PVB.
PhylomeDBiO75563.
TreeFamiTF331055.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNPSSTSSP YPLPEEIRNL LADVETFVAD ILKGENLSKK AKEKRESLIK
60 70 80 90 100
KIKDVKSIYL QEFQDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAP
110 120 130 140 150
SDGAQFPPIA AQDLPFVLKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY
160 170 180 190 200
YYGSDKDKQQ KGEFAIDGYS VRMNNTLRKD GKKDCCFEIS APDKRIYQFT
210 220 230 240 250
AASPKDAEEW VQQLKFVLQD MESDIIPEDY DERGELYDDV DHPLPISNPL
260 270 280 290 300
TSSQPIDDEI YEELPEEEED SAPVKVEEQR KMSQDSVHHT SGDKSTDYAN
310 320 330 340 350
FYQGLWDCTG AFSDELSFKR GDVIYILSKE YNRYGWWVGE MKGAIGLVPK

AYIMEMYDI
Length:359
Mass (Da):41,217
Last modified:November 1, 1998 - v1
Checksum:i65F266535A89281E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61S → C in BAA36194 (PubMed:9837776).Curated
Sequence conflicti352 – 3521Y → H in BAD96605 (Ref. 7) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti202 – 2021A → S.3 Publications
Corresponds to variant rs1129771 [ dbSNP | Ensembl ].
VAR_029812
Natural varianti253 – 2531S → T.
Corresponds to variant rs17154402 [ dbSNP | Ensembl ].
VAR_029813

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014486 mRNA. Translation: BAA36194.1.
AJ004886 mRNA. Translation: CAA06193.1.
AF072166 mRNA. Translation: AAC39924.1.
AF051323 mRNA. Translation: AAC99296.1.
AK313209 mRNA. Translation: BAG36025.1.
AK222885 mRNA. Translation: BAD96605.1.
AC003999 Genomic DNA. Translation: AAS02033.1.
AC011299 Genomic DNA. Translation: AAS07536.1.
CH236948 Genomic DNA. Translation: EAL24231.1.
CH471073 Genomic DNA. Translation: EAW93859.1.
BC002893 mRNA. Translation: AAH02893.1.
BC036044 mRNA. Translation: AAH36044.1.
CCDSiCCDS5400.1.
RefSeqiNP_003921.2. NM_003930.4.
XP_005249958.1. XM_005249901.1.
UniGeneiHs.200770.
Hs.610137.

Genome annotation databases

EnsembliENST00000345317; ENSP00000005587; ENSG00000005020.
GeneIDi8935.
KEGGihsa:8935.
UCSCiuc003syc.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014486 mRNA. Translation: BAA36194.1.
AJ004886 mRNA. Translation: CAA06193.1.
AF072166 mRNA. Translation: AAC39924.1.
AF051323 mRNA. Translation: AAC99296.1.
AK313209 mRNA. Translation: BAG36025.1.
AK222885 mRNA. Translation: BAD96605.1.
AC003999 Genomic DNA. Translation: AAS02033.1.
AC011299 Genomic DNA. Translation: AAS07536.1.
CH236948 Genomic DNA. Translation: EAL24231.1.
CH471073 Genomic DNA. Translation: EAW93859.1.
BC002893 mRNA. Translation: AAH02893.1.
BC036044 mRNA. Translation: AAH36044.1.
CCDSiCCDS5400.1.
RefSeqiNP_003921.2. NM_003930.4.
XP_005249958.1. XM_005249901.1.
UniGeneiHs.200770.
Hs.610137.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OMHX-ray2.90E/F/G/H71-79[»]
ProteinModelPortaliO75563.
SMRiO75563. Positions 14-221, 304-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114448. 12 interactions.
IntActiO75563. 4 interactions.
STRINGi9606.ENSP00000005587.

PTM databases

PhosphoSiteiO75563.

2D gel databases

OGPiO75563.

Proteomic databases

MaxQBiO75563.
PaxDbiO75563.
PRIDEiO75563.

Protocols and materials databases

DNASUi8935.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345317; ENSP00000005587; ENSG00000005020.
GeneIDi8935.
KEGGihsa:8935.
UCSCiuc003syc.3. human.

Organism-specific databases

CTDi8935.
GeneCardsiGC07M026706.
H-InvDBHIX0025350.
HGNCiHGNC:15687. SKAP2.
HPAiHPA005560.
HPA024045.
MIMi605215. gene.
neXtProtiNX_O75563.
PharmGKBiPA162403393.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG46742.
GeneTreeiENSGT00390000017856.
HOGENOMiHOG000231109.
HOVERGENiHBG052827.
InParanoidiO75563.
OMAiWDCTGAL.
OrthoDBiEOG7K6PVB.
PhylomeDBiO75563.
TreeFamiTF331055.

Enzyme and pathway databases

ReactomeiREACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinkiO75563.

Miscellaneous databases

ChiTaRSiSKAP2. human.
GeneWikiiSKAP2.
GenomeRNAii8935.
NextBioi33596.
PROiO75563.
SOURCEiSearch...

Gene expression databases

BgeeiO75563.
CleanExiHS_SKAP2.
ExpressionAtlasiO75563. baseline and differential.
GenevestigatoriO75563.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN, FUNCTION, VARIANT SER-202.
    Tissue: Testis.
  2. "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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH FYB, VARIANT SER-202.
    Tissue: Leukocyte.
  3. "FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells."
    Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.
    Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FYB, PHOSPHORYLATION.
    Tissue: Lymphocyte.
  4. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PTK2B, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION.
    Tissue: Hippocampus.
  5. "Src-associated adaptor protein with PH and SH3 domain."
    Lee J.-S., Suh K.S., Burr J.G.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
    Tissue: Pancreas.
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  8. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Testis.
  12. "Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
    Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
    J. Biol. Chem. 275:33427-33434(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH FYB; LAT AND GRB2, TISSUE SPECIFICITY.
  13. "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells."
    Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F., Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.
    J. Biol. Chem. 276:22375-22381(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, INTERACTION WITH PRAM1.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND TYR-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
    Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
    J. Biol. Chem. 286:30526-30534(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 71-79 IN COMPLEX WITH PTPN22, PHOSPHORYLATION AT TYR-75.

Entry informationi

Entry nameiSKAP2_HUMAN
AccessioniPrimary (citable) accession number: O75563
Secondary accession number(s): A4D173
, Q53GP6, Q75MK6, Q75MZ4, Q9UBZ3, Q9UED8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: March 4, 2015
This is version 120 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 7
    Human chromosome 7: 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

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.