LEUK_HUMAN - dbPTM
LEUK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEUK_HUMAN
UniProt AC P16150
Protein Name Leukosialin
Gene Name SPN
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell projection, microvillus . Cell projection, uropodium . Localizes to the uropodium and microvilli via its interaction with ERM proteins (EZR, RDX and MSN).
CD43 cytoplasmic tail: Nucleus . Nucleus
Protein Description Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (By similarity). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. [PubMed: 18036228 Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR]
Protein Sequence MATLLLLLGVLVVSPDALGSTTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSRGMLPVAVLVALLAVIVLVALLLLWRRRQKRRTGALVLSRGGKRNGVVDAWAGPAQVPEEGAVTVTVGGSGGDKGSGFPDGEGSSRRPTLTTFFGRRKSRQGSLAMEELKSGSGPSLKGEEEPLVASEDGAVDAPAPDEPEGGDGAAP
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
21O-linked_GlycosylationSPDALGSTTAVQTPT
CCCCCCCCCEEECCC		19.581731338
22O-linked_GlycosylationPDALGSTTAVQTPTS
CCCCCCCCEEECCCC		26.911731338
26O-linked_GlycosylationGSTTAVQTPTSGEPL
CCCCEEECCCCCCCC		23.181731338
28O-linked_GlycosylationTTAVQTPTSGEPLVS
CCEEECCCCCCCCCC		53.391731338
29O-linked_GlycosylationTAVQTPTSGEPLVST
CEEECCCCCCCCCCC		42.221731338
35O-linked_GlycosylationTSGEPLVSTSEPLSS
CCCCCCCCCCCCCCC		33.621731338
36O-linked_GlycosylationSGEPLVSTSEPLSSK
CCCCCCCCCCCCCCC		29.631731338
37O-linked_GlycosylationGEPLVSTSEPLSSKM
CCCCCCCCCCCCCCE		29.701731338
41O-linked_GlycosylationVSTSEPLSSKMYTTS
CCCCCCCCCCEEEEE		38.331731338
42O-linked_GlycosylationSTSEPLSSKMYTTSI
CCCCCCCCCEEEEEC		29.171731338
46O-linked_GlycosylationPLSSKMYTTSITSDP
CCCCCEEEEECCCCC		15.571731338
47O-linked_GlycosylationLSSKMYTTSITSDPK
CCCCEEEEECCCCCC		10.721731338
48O-linked_GlycosylationSSKMYTTSITSDPKA
CCCEEEEECCCCCCC		18.971731338
50O-linked_GlycosylationKMYTTSITSDPKADS
CEEEEECCCCCCCCC		27.181731338
51O-linked_GlycosylationMYTTSITSDPKADST
EEEEECCCCCCCCCC		50.69OGP
58O-linked_GlycosylationSDPKADSTGDQTSAL
CCCCCCCCCCCCCCC		45.371731338
69O-linked_GlycosylationTSALPPSTSINEGSP
CCCCCCCCCCCCCCC		39.121731338
85O-linked_GlycosylationWTSIGASTGSPLPEP
EEEECCCCCCCCCCC		40.94OGP
93O-linked_GlycosylationGSPLPEPTTYQEVSI
CCCCCCCCCEEEEEE		36.15OGP
94O-linked_GlycosylationSPLPEPTTYQEVSIK
CCCCCCCCEEEEEEE		33.64OGP
99O-linked_GlycosylationPTTYQEVSIKMSSVP
CCCEEEEEEEEECCC		18.751731338
103O-linked_GlycosylationQEVSIKMSSVPQETP
EEEEEEEECCCCCCC		24.151731338
109O-linked_GlycosylationMSSVPQETPHATSHP
EECCCCCCCCCCCCC		18.351731338
113O-linked_GlycosylationPQETPHATSHPAVPI
CCCCCCCCCCCCCCE		25.241731338
114O-linked_GlycosylationQETPHATSHPAVPIT
CCCCCCCCCCCCCEE		28.401731338
121O-linked_GlycosylationSHPAVPITANSLGSH
CCCCCCEECCCCCCE		17.45OGP
136O-linked_GlycosylationTVTGGTITTNSPETS
EEECCEEECCCCCCC		21.551731338
137O-linked_GlycosylationVTGGTITTNSPETSS
EECCEEECCCCCCCC		29.831731338
152O-linked_GlycosylationRTSGAPVTTAASSLE
CCCCCCCCCCHHHCC		15.06OGP
153O-linked_GlycosylationTSGAPVTTAASSLET
CCCCCCCCCHHHCCC		22.06OGP
153PhosphorylationTSGAPVTTAASSLET
CCCCCCCCCHHHCCC		22.06-
156PhosphorylationAPVTTAASSLETSRG
CCCCCCHHHCCCCCC		32.75-
170O-linked_GlycosylationGTSGPPLTMATVSLE
CCCCCCEEEEEEEEE		15.55OGP
173O-linked_GlycosylationGPPLTMATVSLETSK
CCCEEEEEEEEECCC		10.371731338
178O-linked_GlycosylationMATVSLETSKGTSGP
EEEEEEECCCCCCCC		40.821731338
211PhosphorylationPVTMTTGSLEPSSGA
CEEEEECCCCCCCCC		27.71-
215O-linked_GlycosylationTTGSLEPSSGASGPQ
EECCCCCCCCCCCCC		31.84OGP
216O-linked_GlycosylationTGSLEPSSGASGPQV
ECCCCCCCCCCCCCE		49.44OGP
230PhosphorylationVSSVKLSTMMSPTTS
EEEEEEECCCCCCCC		27.5928387310
236PhosphorylationSTMMSPTTSTNASTV
ECCCCCCCCCCCCCC		36.62-
239N-linked_GlycosylationMSPTTSTNASTVPFR
CCCCCCCCCCCCCCC		31.491731338
242PhosphorylationTTSTNASTVPFRNPD
CCCCCCCCCCCCCCC		29.7728387310
242O-linked_GlycosylationTTSTNASTVPFRNPD
CCCCCCCCCCCCCCC		29.77OGP
285PhosphorylationRRRQKRRTGALVLSR
HHHHHHHCCEEEECC		30.7323403867
291PhosphorylationRTGALVLSRGGKRNG
HCCEEEECCCCCCCC		22.7723401153
316O-linked_GlycosylationVPEEGAVTVTVGGSG
CCCCCCEEEEECCCC		15.21OGP
316PhosphorylationVPEEGAVTVTVGGSG
CCCCCCEEEEECCCC		15.2128122231
318PhosphorylationEEGAVTVTVGGSGGD
CCCCEEEEECCCCCC		12.2230108239
322PhosphorylationVTVTVGGSGGDKGSG
EEEEECCCCCCCCCC		33.4028122231
328PhosphorylationGSGGDKGSGFPDGEG
CCCCCCCCCCCCCCC		42.8923882029
336PhosphorylationGFPDGEGSSRRPTLT
CCCCCCCCCCCCEEE		19.1723401153
337O-linked_GlycosylationFPDGEGSSRRPTLTT
CCCCCCCCCCCEEEH		43.0729351928
337PhosphorylationFPDGEGSSRRPTLTT
CCCCCCCCCCCEEEH		43.0723401153
341PhosphorylationEGSSRRPTLTTFFGR
CCCCCCCEEEHHHCC		34.6223401153
341O-linked_GlycosylationEGSSRRPTLTTFFGR
CCCCCCCEEEHHHCC		34.62OGP
343PhosphorylationSSRRPTLTTFFGRRK
CCCCCEEEHHHCCCC		24.8423882029
344PhosphorylationSRRPTLTTFFGRRKS
CCCCEEEHHHCCCCC		21.7823882029
351PhosphorylationTFFGRRKSRQGSLAM
HHHCCCCCCCCCCCH		28.2023401153
355PhosphorylationRRKSRQGSLAMEELK
CCCCCCCCCCHHHHH		12.4828674151
362UbiquitinationSLAMEELKSGSGPSL
CCCHHHHHCCCCCCC		56.93-
363PhosphorylationLAMEELKSGSGPSLK
CCHHHHHCCCCCCCC		51.3021082442
365PhosphorylationMEELKSGSGPSLKGE
HHHHHCCCCCCCCCC		55.4021082442
368PhosphorylationLKSGSGPSLKGEEEP
HHCCCCCCCCCCCCC		46.3623401153
379PhosphorylationEEEPLVASEDGAVDA
CCCCCEECCCCCCCC		28.8330576142
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
351SPhosphorylationKinasePRKCAP17252
GPS
355SPhosphorylationKinasePRKCQQ04759
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXO7Q9Y3I1
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
355SPhosphorylation

18088087
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 LEUK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EZRI_HUMANEZRphysical
9616160
MOES_HUMANMSNphysical
9616160
MOES_HUMANMSNphysical
9472040
DAXX_HUMANDAXXphysical
11773067
S39AB_HUMANSLC39A11physical
26186194
SAAL1_HUMANSAAL1physical
26186194
EI2BG_HUMANEIF2B3physical
26186194
EI2BE_HUMANEIF2B5physical
26186194
EI2BD_HUMANEIF2B4physical
26186194
EI2BB_HUMANEIF2B2physical
26186194
EI2BG_HUMANEIF2B3physical
28514442
S39AB_HUMANSLC39A11physical
28514442
JIP4_HUMANSPAG9physical
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 LEUK_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Amino acid sequence of human plasma galactoglycoprotein: identitywith the extracellular region of CD43 (sialophorin).";
Schmid K., Hediger M.A., Brossmer R., Collins J.H., Haupt H.,Marti T., Offner G.D., Schaller J., Takagaki K., Walsh M.T.,Schwick H.G., Rose F.S., Remold-O'Donnell E.;
Proc. Natl. Acad. Sci. U.S.A. 89:663-667(1992).
Cited for: PROTEIN SEQUENCE OF 20-245, AND GLYCOSYLATION AT THR-21; THR-22;THR-26; THR-28; SER-29; SER-35; THR-36; SER-37; SER-41; SER-42;THR-46; THR-47; SER-48; THR-50; THR-58; THR-69; SER-99; SER-103;THR-109; THR-113; SER-114; THR-136; THR-137; THR-173; THR-178 ANDASN-239.
O-linked Glycosylation
ReferencePubMed
"Amino acid sequence of human plasma galactoglycoprotein: identitywith the extracellular region of CD43 (sialophorin).";
Schmid K., Hediger M.A., Brossmer R., Collins J.H., Haupt H.,Marti T., Offner G.D., Schaller J., Takagaki K., Walsh M.T.,Schwick H.G., Rose F.S., Remold-O'Donnell E.;
Proc. Natl. Acad. Sci. U.S.A. 89:663-667(1992).
Cited for: PROTEIN SEQUENCE OF 20-245, AND GLYCOSYLATION AT THR-21; THR-22;THR-26; THR-28; SER-29; SER-35; THR-36; SER-37; SER-41; SER-42;THR-46; THR-47; SER-48; THR-50; THR-58; THR-69; SER-99; SER-103;THR-109; THR-113; SER-114; THR-136; THR-137; THR-173; THR-178 ANDASN-239.
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-291 AND SER-368, ANDMASS SPECTROMETRY.
"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-355, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory