SKAP1_HUMAN - dbPTM
SKAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKAP1_HUMAN
UniProt AC Q86WV1
Protein Name Src kinase-associated phosphoprotein 1
Gene Name SKAP1
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization Cytoplasm. Nucleus. Cell membrane. Upon T-cell stimulation, translocates to lipid rafts at the cell membrane.
Protein Description Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway. Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells..
Protein Sequence MQAAALPEEIRWLLEDAEEFLAEGLRNENLSAVARDHRDHILRGFQQIKARYYWDFQPQGGDIGQDSSDDNHSGTLGLSLTSDAPFLSDYQDEGMEDIVKGAQELDNVIKQGYLEKKSKDHSFFGSEWQKRWCVVSRGLFYYYANEKSKQPKGTFLIKGYGVRMAPHLRRDSKKESCFELTSQDRRSYEFTATSPAEARDWVDQISFLLKDLSSLTIPYEEDEEEEEKEETYDDIDGFDSPSCGSQCRPTILPGSVGIKEPTEEKEEEDIYEVLPDEEHDLEEDESGTRRKGVDYASYYQGLWDCHGDQPDELSFQRGDLIRILSKEYNMYGWWVGELNSLVGIVPKEYLTTAFEVEER
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
90PhosphorylationDAPFLSDYQDEGMED
CCCCCCCCCCCCHHH
17.94-
110UbiquitinationQELDNVIKQGYLEKK
HHHHHHHHHCHHCHH
33.13-
110AcetylationQELDNVIKQGYLEKK
HHHHHHHHHCHHCHH
33.137226439
141PhosphorylationVVSRGLFYYYANEKS
EEECCEEEECCCCCC
10.70-
142PhosphorylationVSRGLFYYYANEKSK
EECCEEEECCCCCCC
6.7025147952
143PhosphorylationSRGLFYYYANEKSKQ
ECCEEEECCCCCCCC
7.50-
152AcetylationNEKSKQPKGTFLIKG
CCCCCCCCCEEEEEE
69.0028734743
173AcetylationPHLRRDSKKESCFEL
CHHCCCCCCCCCEEC
65.9228734751
174AcetylationHLRRDSKKESCFELT
HHCCCCCCCCCEECC
59.8328734759
176PhosphorylationRRDSKKESCFELTSQ
CCCCCCCCCEECCCC
32.7428972365
181PhosphorylationKESCFELTSQDRRSY
CCCCEECCCCCCCEE
19.6928972365
219PhosphorylationLSSLTIPYEEDEEEE
HHHCCCCCCCCCCHH
28.2711909961
232PhosphorylationEEEKEETYDDIDGFD
HHHHHHHCCCCCCCC
18.2011909961
240PhosphorylationDDIDGFDSPSCGSQC
CCCCCCCCCCCCCCC
19.2226074081
242PhosphorylationIDGFDSPSCGSQCRP
CCCCCCCCCCCCCCC
34.7526074081
245PhosphorylationFDSPSCGSQCRPTIL
CCCCCCCCCCCCCCC
30.3626074081
250PhosphorylationCGSQCRPTILPGSVG
CCCCCCCCCCCCCCC
18.7826074081
255PhosphorylationRPTILPGSVGIKEPT
CCCCCCCCCCCCCCC
18.4126074081
259UbiquitinationLPGSVGIKEPTEEKE
CCCCCCCCCCCCCCC
52.27-
262PhosphorylationSVGIKEPTEEKEEED
CCCCCCCCCCCCHHH
58.8428796482
271PhosphorylationEKEEEDIYEVLPDEE
CCCHHHHHHHCCCCC
16.5912171928
295PhosphorylationTRRKGVDYASYYQGL
CCCCCCCHHHHHCCC
8.6116461356
298PhosphorylationKGVDYASYYQGLWDC
CCCCHHHHHCCCCCC
7.5216461356
299PhosphorylationGVDYASYYQGLWDCH
CCCHHHHHCCCCCCC
8.1325147952
314PhosphorylationGDQPDELSFQRGDLI
CCCCCCCCCCCCHHH
19.7924719451
325PhosphorylationGDLIRILSKEYNMYG
CHHHHHHHHHCCCCC
22.5228122231

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
219YPhosphorylationKinaseFYNP06241
PhosphoELM
232YPhosphorylationKinaseFYNP06241
PSP
271YPhosphorylationKinaseFYNP06241
Uniprot
295YPhosphorylationKinaseFYNP06241
Uniprot
298YPhosphorylationKinaseFYNP06241
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKAP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SKAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTPRC_HUMANPTPRCphysical
11909961
SKAP1_HUMANSKAP1physical
12171928
GRB2_HUMANGRB2physical
12171928
A4_HUMANAPPphysical
21832049
BLCAP_HUMANBLCAPphysical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
PRAM_HUMANPRAM1physical
25416956
F102A_HUMANFAM102Aphysical
25416956
AP3M1_HUMANAP3M1physical
26186194
MYO9B_HUMANMYO9Bphysical
26186194
MYO9A_HUMANMYO9Aphysical
26186194
RPA2_HUMANPOLR1Bphysical
26186194
REXO5_HUMANLOC81691physical
26186194
EMAL3_HUMANEML3physical
26186194
WRN_HUMANWRNphysical
26186194
ASPM_HUMANASPMphysical
26186194
JPH1_HUMANJPH1physical
26186194
RPA1_HUMANPOLR1Aphysical
26186194
RPC1_HUMANPOLR3Aphysical
26186194
RECQ4_HUMANRECQL4physical
26186194
HPS3_HUMANHPS3physical
26186194
Z324A_HUMANZNF324physical
26186194
TASOR_HUMANFAM208Aphysical
26186194
UXT_HUMANUXTphysical
26186194
CNDD3_HUMANNCAPD3physical
26186194
MYCB2_HUMANMYCBP2physical
26186194
CUL2_HUMANCUL2physical
26186194
PI51A_HUMANPIP5K1Aphysical
26186194
NEK1_HUMANNEK1physical
26186194
PKHH3_HUMANPLEKHH3physical
26186194
PHLB3_HUMANPHLDB3physical
26186194
PK3C3_HUMANPIK3C3physical
26186194
SEC63_HUMANSEC63physical
26186194
SKAP2_HUMANSKAP2physical
26186194
TF3C1_HUMANGTF3C1physical
26186194
RMP_HUMANURI1physical
26186194
P85B_HUMANPIK3R2physical
26186194
P55G_HUMANPIK3R3physical
26186194
RPOM_HUMANPOLRMTphysical
26186194
PLD2_HUMANPLD2physical
26186194
UCKL1_HUMANUCKL1physical
26186194
PR14L_HUMANPRR14Lphysical
26186194
KSR1_HUMANKSR1physical
26186194
BCD1_HUMANZNHIT6physical
26186194
PDRG1_HUMANPDRG1physical
26186194
SETX_HUMANSETXphysical
26186194
NFL_HUMANNEFLphysical
26186194
ALMS1_HUMANALMS1physical
26186194
APBP2_HUMANAPPBP2physical
26186194
UTP15_HUMANUTP15physical
26186194
SENP5_HUMANSENP5physical
26186194
CNDH2_HUMANNCAPH2physical
26186194
PAX3_HUMANPAX3physical
26186194
TBL2_HUMANTBL2physical
26186194
ZNHI2_HUMANZNHIT2physical
26186194
ZN644_HUMANZNF644physical
26186194
SUCHY_HUMANSUGCTphysical
26186194
PKN3_HUMANPKN3physical
26186194
TTF2_HUMANTTF2physical
26186194
PPHLN_HUMANPPHLN1physical
26186194
NPHP4_HUMANNPHP4physical
26186194
MTMR1_HUMANMTMR1physical
26186194
PKN2_HUMANPKN2physical
26186194
CU002_HUMANC21orf2physical
26186194
DPOLA_HUMANPOLA1physical
26186194
RPC2_HUMANPOLR3Bphysical
26186194
RPAB5_HUMANPOLR2Lphysical
26186194
CP110_HUMANCCP110physical
26186194
SETD5_HUMANSETD5physical
26186194
ELP3_HUMANELP3physical
26186194
DOCK7_HUMANDOCK7physical
26186194
UBP54_HUMANUSP54physical
26186194
RPA49_HUMANPOLR1Ephysical
26186194
TRM44_HUMANTRMT44physical
26186194
NEK4_HUMANNEK4physical
26186194
ATX2_HUMANATXN2physical
26186194
MTMR5_HUMANSBF1physical
26186194
GTPB6_HUMANGTPBP6physical
26186194
TRM1_HUMANTRMT1physical
26186194
RPA34_HUMANCD3EAPphysical
26186194
PER1_HUMANPER1physical
26186194
SPT6H_HUMANSUPT6Hphysical
26186194
MCM8_HUMANMCM8physical
26186194
RTEL1_HUMANRTEL1physical
26186194
TIGD5_HUMANTIGD5physical
26186194
PUSL1_HUMANPUSL1physical
26186194
KLDC3_HUMANKLHDC3physical
26186194
SKAP2_HUMANSKAP2physical
28514442
PAX3_HUMANPAX3physical
28514442
NEK1_HUMANNEK1physical
28514442
PKN3_HUMANPKN3physical
28514442
SUCHY_HUMANSUGCTphysical
28514442
PK3C3_HUMANPIK3C3physical
28514442
CU002_HUMANC21orf2physical
28514442
NPHP4_HUMANNPHP4physical
28514442
KSR1_HUMANKSR1physical
28514442
RECQ4_HUMANRECQL4physical
28514442
RPA49_HUMANPOLR1Ephysical
28514442
CP110_HUMANCCP110physical
28514442
KLDC3_HUMANKLHDC3physical
28514442
MTMR5_HUMANSBF1physical
28514442
ZN644_HUMANZNF644physical
28514442
RPA1_HUMANPOLR1Aphysical
28514442
SETD5_HUMANSETD5physical
28514442
TASOR_HUMANFAM208Aphysical
28514442
WRN_HUMANWRNphysical
28514442
RPA2_HUMANPOLR1Bphysical
28514442
MYCB2_HUMANMYCBP2physical
28514442
REXO5_HUMANLOC81691physical
28514442
RPC1_HUMANPOLR3Aphysical
28514442
APBP2_HUMANAPPBP2physical
28514442
ZNHI2_HUMANZNHIT2physical
28514442
PPHLN_HUMANPPHLN1physical
28514442
TIGD5_HUMANTIGD5physical
28514442
UBP54_HUMANUSP54physical
28514442
ASPM_HUMANASPMphysical
28514442
SPT6H_HUMANSUPT6Hphysical
28514442
Z324A_HUMANZNF324physical
28514442
PHLB3_HUMANPHLDB3physical
28514442
PKHH3_HUMANPLEKHH3physical
28514442
RMP_HUMANURI1physical
28514442
TTF2_HUMANTTF2physical
28514442
EMAL3_HUMANEML3physical
28514442
ALMS1_HUMANALMS1physical
28514442
MTMR1_HUMANMTMR1physical
28514442
PR14L_HUMANPRR14Lphysical
28514442
JPH1_HUMANJPH1physical
28514442
MYO9B_HUMANMYO9Bphysical
28514442
RTEL1_HUMANRTEL1physical
28514442
BCD1_HUMANZNHIT6physical
28514442
MYO9A_HUMANMYO9Aphysical
28514442
P85B_HUMANPIK3R2physical
28514442
RPAB5_HUMANPOLR2Lphysical
28514442
NEK4_HUMANNEK4physical
28514442
MA7D1_HUMANMAP7D1physical
28514442
FYB1_HUMANFYBphysical
29127148

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKAP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-142, AND MASSSPECTROMETRY.

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