SLAF7_HUMAN - dbPTM
SLAF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLAF7_HUMAN
UniProt AC Q9NQ25
Protein Name SLAM family member 7
Gene Name SLAMF7
Organism Homo sapiens (Human).
Sequence Length 335
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Isoform 1 mediates NK cell activation through a SH2D1A-independent extracellular signal-regulated ERK-mediated pathway. [PubMed: 11698418 Positively regulates NK cell functions by a mechanism dependent on phosphorylated SH2D1B. Downstream signaling implicates PLCG1, PLCG2 and PI3K]
Protein Sequence MAGSPTCLTLIYILWQLTGSAASGPVKELVGSVGGAVTFPLKSKVKQVDSIVWTFNTTPLVTIQPEGGTIIVTQNRNRERVDFPDGGYSLKLSKLKKNDSGIYYVGIYSSSLQQPSTQEYVLHVYEHLSKPKVTMGLQSNKNGTCVTNLTCCMEHGEEDVIYTWKALGQAANESHNGSILPISWRWGESDMTFICVARNPVSRNFSSPILARKLCEGAADDPDSSMVLLCLLLVPLLLSLFVLGLFLWFLKRERQEEYIEEKKRVDICRETPNICPHSGENTEYDTIPHTNRTILKEDPANTVYSTVEIPKKMENPHSLLTMPDTPRLFAYENVI
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
50PhosphorylationSKVKQVDSIVWTFNT
HHCEECCEEEEEEEC
21.8622210691
62PhosphorylationFNTTPLVTIQPEGGT
EECCCCEEEECCCCE
22.9022210691
69PhosphorylationTIQPEGGTIIVTQNR
EEECCCCEEEEECCC
20.5622210691
88PhosphorylationVDFPDGGYSLKLSKL
EECCCCCEEEEEEEC
19.1628509920
89PhosphorylationDFPDGGYSLKLSKLK
ECCCCCEEEEEEECC
23.4624719451
93PhosphorylationGGYSLKLSKLKKNDS
CCEEEEEEECCCCCC
34.0628509920
94AcetylationGYSLKLSKLKKNDSG
CEEEEEEECCCCCCC
74.827976765
98N-linked_GlycosylationKLSKLKKNDSGIYYV
EEEECCCCCCCCEEE
47.28UniProtKB CARBOHYD
129PhosphorylationLHVYEHLSKPKVTMG
HHHHHHHCCCEEEEE
49.1424719451
142N-linked_GlycosylationMGLQSNKNGTCVTNL
EEEECCCCCEEEEEE
56.08UniProtKB CARBOHYD
148N-linked_GlycosylationKNGTCVTNLTCCMEH
CCCEEEEEEEEEHHC
16.98UniProtKB CARBOHYD
172N-linked_GlycosylationKALGQAANESHNGSI
HHHHHHHHHHCCCCE
55.08UniProtKB CARBOHYD
176N-linked_GlycosylationQAANESHNGSILPIS
HHHHHHCCCCEEEEE
56.01UniProtKB CARBOHYD
183PhosphorylationNGSILPISWRWGESD
CCCEEEEEEEECCCC
14.5124719451
204N-linked_GlycosylationARNPVSRNFSSPILA
ECCCCCCCCCCHHHH
33.38UniProtKB CARBOHYD
258PhosphorylationKRERQEEYIEEKKRV
HHHHHHHHHHHHHHC
16.9323401153
271PhosphorylationRVDICRETPNICPHS
HCCCCCCCCCCCCCC
11.4130108239
278PhosphorylationTPNICPHSGENTEYD
CCCCCCCCCCCCCCC
32.7030108239
282PhosphorylationCPHSGENTEYDTIPH
CCCCCCCCCCCCCCC
31.4530108239
284PhosphorylationHSGENTEYDTIPHTN
CCCCCCCCCCCCCCC
19.1530108239
286PhosphorylationGENTEYDTIPHTNRT
CCCCCCCCCCCCCCC
35.1930108239
290PhosphorylationEYDTIPHTNRTILKE
CCCCCCCCCCCEEEC
22.5030108239
296UbiquitinationHTNRTILKEDPANTV
CCCCCEEECCCCCCE
57.11-
302PhosphorylationLKEDPANTVYSTVEI
EECCCCCCEEEEEEC
23.9528152594
304PhosphorylationEDPANTVYSTVEIPK
CCCCCCEEEEEECCC
9.1528152594
305PhosphorylationDPANTVYSTVEIPKK
CCCCCEEEEEECCCC
22.9528152594
306PhosphorylationPANTVYSTVEIPKKM
CCCCEEEEEECCCCC
12.4128152594
312UbiquitinationSTVEIPKKMENPHSL
EEEECCCCCCCCCCC
46.20-
318PhosphorylationKKMENPHSLLTMPDT
CCCCCCCCCCCCCCC
26.7428348404
321PhosphorylationENPHSLLTMPDTPRL
CCCCCCCCCCCCCCE
31.7630108239
325PhosphorylationSLLTMPDTPRLFAYE
CCCCCCCCCCEEEEE
12.3930108239
331PhosphorylationDTPRLFAYENVI---
CCCCEEEEECCC---
10.7430108239

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

Oops, there are no upstream regulatory protein records of SLAF7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAF7_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 SLAF7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLAF7_HUMANSLAMF7physical
21982860
TRIB2_HUMANTRIB2physical
21988832
MAN1_HUMANLEMD3physical
26186194
HUS1_HUMANHUS1physical
26186194
APBB1_HUMANAPBB1physical
26186194
TBC23_HUMANTBC1D23physical
26186194
PTCD2_HUMANPTCD2physical
26186194
FBX2_HUMANFBXO2physical
26186194
NAGPA_HUMANNAGPAphysical
26186194
YIF1A_HUMANYIF1Aphysical
26186194
LEG1_HUMANLGALS1physical
26186194
DGLB_HUMANDAGLBphysical
26186194
TBC23_HUMANTBC1D23physical
28514442
PTCD2_HUMANPTCD2physical
28514442
HUS1_HUMANHUS1physical
28514442
NAGPA_HUMANNAGPAphysical
28514442
FBX2_HUMANFBXO2physical
28514442
LEG1_HUMANLGALS1physical
28514442
YIF1A_HUMANYIF1Aphysical
28514442
CTNA1_HUMANCTNNA1physical
28514442
CTNB1_HUMANCTNNB1physical
28514442
APBB1_HUMANAPBB1physical
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
D09337 Elotuzumab (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLAF7_HUMAN

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Related Literatures of Post-Translational Modification

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