SLAP1_HUMAN - dbPTM
SLAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLAP1_HUMAN
UniProt AC Q13239
Protein Name Src-like-adapter
Gene Name SLA
Organism Homo sapiens (Human).
Sequence Length 276
Subcellular Localization Cytoplasm. Endosome. Colocalizes with endosomes..
Protein Description Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. Involved in the negative regulation of positive selection and mitosis of T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins..
Protein Sequence MGNSMKSTPAPAERPLPNPEGLDSDFLAVLSDYPSPDISPPIFRRGEKLRVISDEGGWWKAISLSTGRESYIPGICVARVYHGWLFEGLGRDKAEELLQLPDTKVGSFMIRESETKKGFYSLSVRHRQVKHYRIFRLPNNWYYISPRLTFQCLEDLVNHYSEVADGLCCVLTTPCLTQSTAAPAVRASSSPVTLRQKTVDWRRVSRLQEDPEGTENPLGVDESLFSYGLRESIASYLSLTSEDNTSFDRKKKSISLMYGGSKRKSSFFSSPPYFED
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
2Myristoylation------MGNSMKSTP
------CCCCCCCCC		34.61-
8 (in isoform 4)Phosphorylation-20.25-
8 (in isoform 3)Phosphorylation-20.25-
9UbiquitinationGNSMKSTPAPAERPL
CCCCCCCCCCCCCCC		43.25-
15UbiquitinationTPAPAERPLPNPEGL
CCCCCCCCCCCCCCC		43.61-
18PhosphorylationPAERPLPNPEGLDSD
CCCCCCCCCCCCCCC		55.7424719451
18 (in isoform 5)Phosphorylation-55.7424719451
31 (in isoform 5)Phosphorylation-28.62-
31PhosphorylationSDFLAVLSDYPSPDI
CCHHHHHCCCCCCCC		28.62-
60UbiquitinationSDEGGWWKAISLSTG
ECCCCEEEEEECCCC		29.3622505724
77UbiquitinationSYIPGICVARVYHGW
CCCCCEEEEEEECCH		3.44-
77UbiquitinationSYIPGICVARVYHGW
CCCCCEEEEEEECCH		3.4422505724
93UbiquitinationFEGLGRDKAEELLQL
HCCCCCHHHHHHHCC		57.2322505724
100UbiquitinationKAEELLQLPDTKVGS
HHHHHHCCCCCCCEE		4.1222505724
104UbiquitinationLLQLPDTKVGSFMIR
HHCCCCCCCEEEEEE		52.5622505724
107PhosphorylationLPDTKVGSFMIRESE
CCCCCCEEEEEEECC		18.0323401153
110UbiquitinationTKVGSFMIRESETKK
CCCEEEEEEECCCCC		4.10-
110UbiquitinationTKVGSFMIRESETKK
CCCEEEEEEECCCCC		4.1022505724
117UbiquitinationIRESETKKGFYSLSV
EEECCCCCCEEEEEE		62.77-
120PhosphorylationSETKKGFYSLSVRHR
CCCCCCEEEEEEEEC		19.8527642862
121UbiquitinationETKKGFYSLSVRHRQ
CCCCCEEEEEEEECC		16.3522505724
121UbiquitinationETKKGFYSLSVRHRQ
CCCCCEEEEEEEECC		16.35-
123PhosphorylationKKGFYSLSVRHRQVK
CCCEEEEEEEECCCC		15.9124719451
133UbiquitinationHRQVKHYRIFRLPNN
ECCCCEEEEEECCCC		22.6822505724
143PhosphorylationRLPNNWYYISPRLTF
ECCCCEEEECHHHHH		6.1226074081
144UbiquitinationLPNNWYYISPRLTFQ
CCCCEEEECHHHHHH		2.4122505724
145PhosphorylationPNNWYYISPRLTFQC
CCCEEEECHHHHHHH		6.4526074081
154UbiquitinationRLTFQCLEDLVNHYS
HHHHHHHHHHHHHHH		57.8529967540
156UbiquitinationTFQCLEDLVNHYSEV
HHHHHHHHHHHHHHH		2.8022505724
170UbiquitinationVADGLCCVLTTPCLT
HCCCEEEEEECCCCC		5.33-
172PhosphorylationDGLCCVLTTPCLTQS
CCEEEEEECCCCCCC		14.3226074081
173PhosphorylationGLCCVLTTPCLTQST
CEEEEEECCCCCCCC		14.0826074081
177PhosphorylationVLTTPCLTQSTAAPA
EEECCCCCCCCCCCC		27.4726074081
179PhosphorylationTTPCLTQSTAAPAVR
ECCCCCCCCCCCCCC		18.1226074081
180PhosphorylationTPCLTQSTAAPAVRA
CCCCCCCCCCCCCCC		19.6126074081
188PhosphorylationAAPAVRASSSPVTLR
CCCCCCCCCCCEEEE		22.3026657352
189PhosphorylationAPAVRASSSPVTLRQ
CCCCCCCCCCEEEEE		37.3628122231
190PhosphorylationPAVRASSSPVTLRQK
CCCCCCCCCEEEEEC		22.3923401153
193PhosphorylationRASSSPVTLRQKTVD
CCCCCCEEEEECCCC		21.4328450419
197UbiquitinationSPVTLRQKTVDWRRV
CCEEEEECCCCHHHH		44.04-
198PhosphorylationPVTLRQKTVDWRRVS
CEEEEECCCCHHHHH		18.5026074081
205PhosphorylationTVDWRRVSRLQEDPE
CCCHHHHHHHCCCCC		26.0126074081
214PhosphorylationLQEDPEGTENPLGVD
HCCCCCCCCCCCCCC		30.8126074081
223PhosphorylationNPLGVDESLFSYGLR
CCCCCCHHHHHHCHH		30.1926074081
225UbiquitinationLGVDESLFSYGLRES
CCCCHHHHHHCHHHH		8.02-
225UbiquitinationLGVDESLFSYGLRES
CCCCHHHHHHCHHHH		8.0222505724
226PhosphorylationGVDESLFSYGLRESI
CCCHHHHHHCHHHHH		24.4728122231
229PhosphorylationESLFSYGLRESIASY
HHHHHHCHHHHHHHH		4.1124719451
230PhosphorylationSLFSYGLRESIASYL
HHHHHCHHHHHHHHH		31.1127251275
235UbiquitinationGLRESIASYLSLTSE
CHHHHHHHHHHCCCC		25.57-
235UbiquitinationGLRESIASYLSLTSE
CHHHHHHHHHHCCCC		25.5729967540
235PhosphorylationGLRESIASYLSLTSE
CHHHHHHHHHHCCCC		25.57-
237UbiquitinationRESIASYLSLTSEDN
HHHHHHHHHCCCCCC		2.91-
237UbiquitinationRESIASYLSLTSEDN
HHHHHHHHHCCCCCC		2.9122505724
238PhosphorylationESIASYLSLTSEDNT
HHHHHHHHCCCCCCC		22.74-
240PhosphorylationIASYLSLTSEDNTSF
HHHHHHCCCCCCCCC		27.05-
252UbiquitinationTSFDRKKKSISLMYG
CCCCHHCCEEEEEEC		56.9322505724
252AcetylationTSFDRKKKSISLMYG
CCCCHHCCEEEEEEC		56.9318585177
253PhosphorylationSFDRKKKSISLMYGG
CCCHHCCEEEEEECC		26.7028857561
255PhosphorylationDRKKKSISLMYGGSK
CHHCCEEEEEECCCC		17.7427251275
258PhosphorylationKKSISLMYGGSKRKS
CCEEEEEECCCCCCC		24.5118083107
261PhosphorylationISLMYGGSKRKSSFF
EEEEECCCCCCCCCC		25.5624247654
262UbiquitinationSLMYGGSKRKSSFFS
EEEECCCCCCCCCCC		68.0929967540
262AcetylationSLMYGGSKRKSSFFS
EEEECCCCCCCCCCC		68.0918585185
264UbiquitinationMYGGSKRKSSFFSSP
EECCCCCCCCCCCCC		54.9422505724
265PhosphorylationYGGSKRKSSFFSSPP
ECCCCCCCCCCCCCC		36.0926074081
266PhosphorylationGGSKRKSSFFSSPPY
CCCCCCCCCCCCCCC		33.0926074081
269UbiquitinationKRKSSFFSSPPYFED
CCCCCCCCCCCCCCC		39.6722505724
269PhosphorylationKRKSSFFSSPPYFED
CCCCCCCCCCCCCCC		39.6728122231
270PhosphorylationRKSSFFSSPPYFED-
CCCCCCCCCCCCCC-		25.4126074081
273PhosphorylationSFFSSPPYFED----
CCCCCCCCCCC----		24.0019605366
279UbiquitinationPYFED----------
CCCCC----------		29967540
281UbiquitinationFED------------
CCC------------		22505724
292Ubiquitination-----------------------
-----------------------		22505724
293Phosphorylation------------------------
------------------------		27251275
301Phosphorylation--------------------------------
--------------------------------		27251275
302Ubiquitination---------------------------------
---------------------------------		29967540
304Ubiquitination-----------------------------------
-----------------------------------		22505724
306Phosphorylation-------------------------------------
-------------------------------------		24719451
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
120YPhosphorylationKinaseKITP10721
PSP
258YPhosphorylationKinaseKITP10721
PSP
273YPhosphorylationKinaseKITP10721
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAP1_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 SLAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZAP70_HUMANZAP70physical
10449770
CD3Z_HUMANCD247physical
10449770
KSYK_HUMANSYKphysical
10449770
LAT_HUMANLATphysical
10449770
EPHA2_HUMANEPHA2physical
7543898
VAV_HUMANVAV1physical
10662792
PGFRB_HUMANPDGFRBphysical
18193084
CBL_HUMANCBLphysical
18193084
FLT3_HUMANFLT3physical
23300935
EPHA2_HUMANEPHA2physical
24457997
UBE4A_HUMANUBE4Aphysical
24457997
NCOA2_HUMANNCOA2physical
28514442
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 SLAP1_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 SER-255, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASSSPECTROMETRY.

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