SLAF1_HUMAN - dbPTM
SLAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLAF1_HUMAN
UniProt AC Q13291
Protein Name Signaling lymphocytic activation molecule
Gene Name SLAMF1
Organism Homo sapiens (Human).
Sequence Length 335
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Present on the surface of B-cells and T-cells. Located at the plasma membrane contacts between neighboring T-cells (PubMed:11806999).
Isoform 3: Secreted .
Isoform 4: Cell membrane . Overexp
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. SLAMF1-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAMF1 signaling seem to exist: one depending on SH2D1A (and perhaps SH2D1B) and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates. Initially it has been proposed that association with SH2D1A prevents binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2. [PubMed: 11806999 However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1]
Protein Sequence MDPKGLLSLTFVLFLSLAFGASYGTGGRMMNCPKILRQLGSKVLLPLTYERINKSMNKSIHIVVTMAKSLENSVENKIVSLDPSEAGPPRYLGDRYKFYLENLTLGIRESRKEDEGWYLMTLEKNVSVQRFCLQLRLYEQVSTPEIKVLNKTQENGTCTLILGCTVEKGDHVAYSWSEKAGTHPLNPANSSHLLSLTLGPQHADNIYICTVSNPISNNSQTFSPWPGCRTDPSETKPWAVYAGLLGGVIMILIMVVILQLRRRGKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCTTIYVAATEPVPESVQETNSITVYASVTLPES
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
53N-linked_GlycosylationPLTYERINKSMNKSI
ECCHHHHHHHCCCCE
36.25UniProtKB CARBOHYD
57N-linked_GlycosylationERINKSMNKSIHIVV
HHHHHHCCCCEEEEE
41.85UniProtKB CARBOHYD
73PhosphorylationMAKSLENSVENKIVS
CHHHHCHHHHCCEEE
22.79-
102N-linked_GlycosylationRYKFYLENLTLGIRE
HHHHHHHHEEEEEEE
35.41UniProtKB CARBOHYD
118PhosphorylationRKEDEGWYLMTLEKN
CCCCCCEEEEEEECC
9.4628555341
121PhosphorylationDEGWYLMTLEKNVSV
CCCEEEEEEECCCCH
29.2128555341
125N-linked_GlycosylationYLMTLEKNVSVQRFC
EEEEEECCCCHHHHH
23.17UniProtKB CARBOHYD
147UbiquitinationQVSTPEIKVLNKTQE
CCCCCCEEEEEECCC
38.7225015289
150N-linked_GlycosylationTPEIKVLNKTQENGT
CCCEEEEEECCCCCE
48.60UniProtKB CARBOHYD
153UbiquitinationIKVLNKTQENGTCTL
EEEEEECCCCCEEEE
43.7125015289
155N-linked_GlycosylationVLNKTQENGTCTLIL
EEEECCCCCEEEEEE
41.05UniProtKB CARBOHYD
189N-linked_GlycosylationTHPLNPANSSHLLSL
CCCCCCCCCCCEEEE
45.35UniProtKB CARBOHYD
217N-linked_GlycosylationTVSNPISNNSQTFSP
EECCCCCCCCCCCCC
53.55UniProtKB CARBOHYD
256UbiquitinationIMILIMVVILQLRRR
HHHHHHHHHHHHHHC
1.6825015289
262UbiquitinationVVILQLRRRGKTNHY
HHHHHHHHCCCCCCC
61.3625015289
266PhosphorylationQLRRRGKTNHYQTTV
HHHHCCCCCCCEEEE
30.0129978859
269PhosphorylationRRGKTNHYQTTVEKK
HCCCCCCCEEEEEEC
15.0429978859
271PhosphorylationGKTNHYQTTVEKKSL
CCCCCCEEEEEECEE
26.1630622161
272PhosphorylationKTNHYQTTVEKKSLT
CCCCCEEEEEECEEE
15.9030622161
277PhosphorylationQTTVEKKSLTIYAQV
EEEEEECEEEEEEEE
41.6430108239
279PhosphorylationTVEKKSLTIYAQVQK
EEEECEEEEEEEECC
21.0230108239
281PhosphorylationEKKSLTIYAQVQKPG
EECEEEEEEEECCCC
5.9211806999
286UbiquitinationTIYAQVQKPGPLQKK
EEEEEECCCCCHHHH
53.7525015289
292UbiquitinationQKPGPLQKKLDSFPA
CCCCCHHHHHCCCCC
64.0925015289
307PhosphorylationQDPCTTIYVAATEPV
CCCCCEEEEEECCCC
5.0711806999
327PhosphorylationETNSITVYASVTLPE
CCCCEEEEEEEECCC
5.6311806999

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
281YPhosphorylationKinaseFYNP06241
Uniprot
307YPhosphorylationKinaseFYNP06241
Uniprot
307YPhosphorylationKinaseLCKP06239
PSP
327YPhosphorylationKinaseFYNP06241
Uniprot
327YPhosphorylationKinaseLYNP07948
PSP
-KUbiquitinationE3 ubiquitin ligaseMARCHF9Q86YJ5
PMID:19457934

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAF1_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 SLAF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH21A_HUMANSH2D1Aphysical
11806999
PTN11_HUMANPTPN11physical
11806999
FGR_HUMANFGRphysical
10229804
SHIP1_HUMANINPP5Dphysical
10229804
PTPRC_HUMANPTPRCphysical
10229804
PTN11_HUMANPTPN11physical
11689425
SH21B_HUMANSH2D1Bphysical
22974441
SLAF1_HUMANSLAMF1physical
21982860
S39AB_HUMANSLC39A11physical
26186194
AT1A3_HUMANATP1A3physical
26186194
AT12A_HUMANATP12Aphysical
26186194
AT2B2_HUMANATP2B2physical
26186194
AT2B3_HUMANATP2B3physical
26186194
NF1_HUMANNF1physical
26186194
HEAT1_HUMANHEATR1physical
26186194
PYRG2_HUMANCTPS2physical
26186194
INT4_HUMANINTS4physical
26186194
NU188_HUMANNUP188physical
26186194
QCR2_HUMANUQCRC2physical
26186194
GLPK2_HUMANGK2physical
26186194
GLPK_HUMANGKphysical
26186194
ELYS_HUMANAHCTF1physical
26186194
INT2_HUMANINTS2physical
26186194
BIG1_HUMANARFGEF1physical
26186194
BIG2_HUMANARFGEF2physical
26186194
LTN1_HUMANLTN1physical
26186194
MD2L2_HUMANMAD2L2physical
26186194
LEG1_HUMANLGALS1physical
26186194
HEAT6_HUMANHEATR6physical
26186194
ANTR1_HUMANANTXR1physical
26186194
HUS1_HUMANHUS1physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
URB2_HUMANURB2physical
26186194
OCLN_HUMANOCLNphysical
26186194
TOM40_HUMANTOMM40physical
26186194
UFSP2_HUMANUFSP2physical
26186194
AN13A_HUMANANKRD13Aphysical
26186194
VPS52_HUMANVPS52physical
26186194
INT12_HUMANINTS12physical
26186194
RAB3B_HUMANRAB3Bphysical
26186194
S27A6_HUMANSLC27A6physical
26186194
ARF5_HUMANARF5physical
26186194
RAB18_HUMANRAB18physical
26186194
CHPT1_HUMANCHPT1physical
26186194
INT1_HUMANINTS1physical
26186194
RAB5A_HUMANRAB5Aphysical
26186194
ORNT1_HUMANSLC25A15physical
26186194
TAM41_HUMANTAMM41physical
26186194
ZN292_HUMANZNF292physical
26186194
INT7_HUMANINTS7physical
26186194
COT2_HUMANNR2F2physical
26186194
ERAP1_HUMANERAP1physical
26186194
MTCH1_HUMANMTCH1physical
26186194
MYADM_HUMANMYADMphysical
26186194
SGPP1_HUMANSGPP1physical
26186194
GATB_HUMANGATBphysical
26186194
PTCD2_HUMANPTCD2physical
26186194
STML1_HUMANSTOML1physical
26186194
XRCC3_HUMANXRCC3physical
26186194
EAA3_HUMANSLC1A1physical
26186194
CNTP3_HUMANCNTNAP3physical
28514442
GPR98_HUMANGPR98physical
28514442
RTCA_HUMANRTCAphysical
28514442
KBRS1_HUMANNKIRAS1physical
28514442
FUT11_HUMANFUT11physical
28514442
GT253_HUMANCERCAMphysical
28514442
ATS2_HUMANADAMTS2physical
28514442
ITA7_HUMANITGA7physical
28514442
CBPE_HUMANCPEphysical
28514442
D2HDH_HUMAND2HGDHphysical
28514442
GLT18_HUMANGALNT18physical
28514442
CHLE_HUMANBCHEphysical
28514442
LIFR_HUMANLIFRphysical
28514442
ANAG_HUMANNAGLUphysical
28514442
TXD15_HUMANTXNDC15physical
28514442
LARG1_HUMANLARGEphysical
28514442
TBB3_HUMANTUBB3physical
28514442
PYC_HUMANPCphysical
28514442
EPHA3_HUMANEPHA3physical
28514442
PLXA2_HUMANPLXNA2physical
28514442
AT12A_HUMANATP12Aphysical
28514442
MOXD1_HUMANMOXD1physical
28514442
CBWD1_HUMANCBWD1physical
28514442
FAT1_HUMANFAT1physical
28514442
LAMB2_HUMANLAMB2physical
28514442
T132A_HUMANTMEM132Aphysical
28514442
CELR1_HUMANCELSR1physical
28514442
GALNS_HUMANGALNSphysical
28514442
CSTN1_HUMANCLSTN1physical
28514442
SIA10_HUMANST3GAL6physical
28514442
I17RA_HUMANIL17RAphysical
28514442
OS9_HUMANOS9physical
28514442
DUSTY_HUMANDSTYKphysical
28514442
SE1L1_HUMANSEL1Lphysical
28514442
ATG2B_HUMANATG2Bphysical
28514442
PCSK5_HUMANPCSK5physical
28514442
ARSK_HUMANARSKphysical
28514442
LAMA3_HUMANLAMA3physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
FAKD3_HUMANFASTKD3physical
28514442
ACHA5_HUMANCHRNA5physical
28514442
GFPT2_HUMANGFPT2physical
28514442
NAGAB_HUMANNAGAphysical
28514442
BMP7_HUMANBMP7physical
28514442
CAHD1_HUMANCACHD1physical
28514442
ANR46_HUMANANKRD46physical
28514442
THUM3_HUMANTHUMPD3physical
28514442
IGF1R_HUMANIGF1Rphysical
28514442
FRAS1_HUMANFRAS1physical
28514442
ADAM9_HUMANADAM9physical
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 SLAF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-281, AND MASSSPECTROMETRY.

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