SEM4D_HUMAN - dbPTM
SEM4D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEM4D_HUMAN
UniProt AC Q92854
Protein Name Semaphorin-4D
Gene Name SEMA4D
Organism Homo sapiens (Human).
Sequence Length 862
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. Promotes reorganization of the actin cytoskeleton and plays a role in axonal growth cone guidance in the developing central nervous system. Regulates dendrite and axon branching and morphogenesis. Promotes the migration of cerebellar granule cells and of endothelial cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Interaction with PLXNB1 mediates activation of RHOA..
Protein Sequence MRMCTPIRGLLMALAVMFGTAMAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHEVYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLGKNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSHGKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQDFEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQTESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLKAESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVFQVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVASTQGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVPQLHSEKTMYLKSSDNRLLMSLFLFFFVLFLCLFFYNCYKGYLPRQCLKFRSALLIGKKKPKSDFCDREQSLKETLVEPGSFSQQNGEHPKPALDTGYETEQDTITSKVPTDREDSQRIDDLSARDKPFDVKCELKFADSDADGD
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
5Phosphorylation---MRMCTPIRGLLM
---CCCCHHHHHHHH		16.65-
49N-linked_GlycosylationFHEPDIYNYSALLLS
CCCCCCCCCEEEEEC		25.3120877282
49N-linked_GlycosylationFHEPDIYNYSALLLS
CCCCCCCCCEEEEEC		25.31UniProtKB CARBOHYD
74N-linked_GlycosylationREAVFAVNALNISEK
HHHHHHHCCCCCCHH		34.9719349973
74N-linked_GlycosylationREAVFAVNALNISEK
HHHHHHHCCCCCCHH		34.9719349973
77N-linked_GlycosylationVFAVNALNISEKQHE
HHHHCCCCCCHHHCE		33.07UniProtKB CARBOHYD
77N-linked_GlycosylationVFAVNALNISEKQHE
HHHHCCCCCCHHHCE		33.0720877282
81UbiquitinationNALNISEKQHEVYWK
CCCCCCHHHCEEEEE		50.60-
104UbiquitinationCAEKGKSKQTECLNY
HHHCCCCCHHHHHHH		65.80-
139N-linked_GlycosylationQPACDHLNLTSFKFL
CCCCCCCCCCCEEEC		37.5420877282
148UbiquitinationTSFKFLGKNEDGKGR
CCEEECCCCCCCCCC		60.35-
191N-linked_GlycosylationSEPIISRNSSHSPLR
CCCCCCCCCCCCCCC		40.8620877282
193PhosphorylationPIISRNSSHSPLRTE
CCCCCCCCCCCCCCC		31.3726437602
195PhosphorylationISRNSSHSPLRTEYA
CCCCCCCCCCCCCCC		27.8120068231
269AcetylationGGLRTLQKKWTSFLK
CCHHHHHHHHHHHHH		54.087484017
273PhosphorylationTLQKKWTSFLKARLI
HHHHHHHHHHHHHHH		27.7124719451
276AcetylationKKWTSFLKARLICSR
HHHHHHHHHHHHHCC		29.477484027
301PhosphorylationRDVFVLRSPGLKVPV
EEEEEECCCCCCCCE		21.1124719451
329N-linked_GlycosylationLSAVCAYNLSTAEEV
HHHHEECCCCCHHHH		14.7020877282
358PhosphorylationSHTKWVRYNGPVPKP
CCCCEEEECCCCCCC		18.1718785766
379N-linked_GlycosylationDSEARAANYTSSLNL
CHHHHHCCCCCCCCC		39.3619349973
379N-linked_GlycosylationDSEARAANYTSSLNL
CHHHHHCCCCCCCCC		39.3619349973
390PhosphorylationSLNLPDKTLQFVKDH
CCCCCCCCCHHHHCC		32.92-
419N-linked_GlycosylationRLIKKDVNYTQIVVD
CCEECCCCCEEEEEE		44.2416263699
419N-linked_GlycosylationRLIKKDVNYTQIVVD
CCEECCCCCEEEEEE		44.2416263699
505UbiquitinationAPLAFCGKHGTCEDC
ECEEECCCCCCHHHC		39.79-
547 (in isoform 2)Phosphorylation-32.5422210691
547PhosphorylationRGLIQEMSGDASVCP
CCCCHHHCCCCCCCC		32.5422461510
551PhosphorylationQEMSGDASVCPDKSK
HHHCCCCCCCCCCCC		29.0622461510
556UbiquitinationDASVCPDKSKGSYRQ
CCCCCCCCCCCCHHC		38.93-
560PhosphorylationCPDKSKGSYRQHFFK
CCCCCCCCHHCCCHH		22.3723401153
561PhosphorylationPDKSKGSYRQHFFKH
CCCCCCCHHCCCHHC		23.9822461510
575UbiquitinationHGGTAELKCSQKSNL
CCCEEEEEECCCCCH		24.2829967540
613N-linked_GlycosylationRKNLLIFNLSEGDSG
CCCEEEEECCCCCCC		35.35UniProtKB CARBOHYD
632N-linked_GlycosylationLSEERVKNKTVFQVV
CCHHHCCCCCHHHHH		42.23UniProtKB CARBOHYD
657O-linked_GlycosylationPKPVVAPTLSVVQTE
CCCEECCEEEEEEEC		23.1755835813
663O-linked_GlycosylationPTLSVVQTEGSRIAT
CEEEEEEECCCHHEE		30.6155825041
666O-linked_GlycosylationSVVQTEGSRIATKVL
EEEEECCCHHEEEEE		17.8055825047
670O-linked_GlycosylationTEGSRIATKVLVAST
ECCCHHEEEEEEEEC		21.2255825053
680O-linked_GlycosylationLVASTQGSSPPTPAV
EEEECCCCCCCCCCC		29.83OGP
690O-linked_GlycosylationPTPAVQATSSGAITL
CCCCCEECCCCCEEC		13.31OGP
696O-linked_GlycosylationATSSGAITLPPKPAP
ECCCCCEECCCCCCC		32.45OGP
704PhosphorylationLPPKPAPTGTSCEPK
CCCCCCCCCCCCCCE		56.0226074081
706PhosphorylationPKPAPTGTSCEPKIV
CCCCCCCCCCCCEEE		32.4526074081
707PhosphorylationKPAPTGTSCEPKIVI
CCCCCCCCCCCEEEE		20.1626074081
716O-linked_GlycosylationEPKIVINTVPQLHSE
CCEEEEECCCCCCCC		23.5755825607
722PhosphorylationNTVPQLHSEKTMYLK
ECCCCCCCCCEEEEC		49.75-
722O-linked_GlycosylationNTVPQLHSEKTMYLK
ECCCCCCCCCEEEEC		49.7555825613
725 (in isoform 2)Phosphorylation-13.6529083192
727PhosphorylationLHSEKTMYLKSSDNR
CCCCCEEEECCCHHH		19.06-
732 (in isoform 2)Phosphorylation-51.8929083192
734 (in isoform 2)Phosphorylation-33.9029083192
769PhosphorylationRQCLKFRSALLIGKK
HHHHHHHHHHHHCCC		26.80-
775UbiquitinationRSALLIGKKKPKSDF
HHHHHHCCCCCCCCC		51.1033845483
780PhosphorylationIGKKKPKSDFCDREQ
HCCCCCCCCCCCHHH		44.4326552605
788PhosphorylationDFCDREQSLKETLVE
CCCCHHHHHHHHHCC		36.3323898821
790UbiquitinationCDREQSLKETLVEPG
CCHHHHHHHHHCCCC		54.6329967540
792PhosphorylationREQSLKETLVEPGSF
HHHHHHHHHCCCCCH		34.2228464451
798PhosphorylationETLVEPGSFSQQNGE
HHHCCCCCHHHCCCC		32.2325849741
800PhosphorylationLVEPGSFSQQNGEHP
HCCCCCHHHCCCCCC		32.3328796482
808UbiquitinationQQNGEHPKPALDTGY
HCCCCCCCCCCCCCC		44.8429967540
813PhosphorylationHPKPALDTGYETEQD
CCCCCCCCCCCCCCC		42.3828796482
815PhosphorylationKPALDTGYETEQDTI
CCCCCCCCCCCCCCC		23.0528796482
817PhosphorylationALDTGYETEQDTITS
CCCCCCCCCCCCCCC		30.3828796482
821PhosphorylationGYETEQDTITSKVPT
CCCCCCCCCCCCCCC		26.3328796482
823PhosphorylationETEQDTITSKVPTDR
CCCCCCCCCCCCCCH		25.2928796482
824PhosphorylationTEQDTITSKVPTDRE
CCCCCCCCCCCCCHH		28.0128796482
825UbiquitinationEQDTITSKVPTDRED
CCCCCCCCCCCCHHH		43.5129967540
828PhosphorylationTITSKVPTDREDSQR
CCCCCCCCCHHHHHC		51.1530108239
833PhosphorylationVPTDREDSQRIDDLS
CCCCHHHHHCHHHCH		19.3323401153
840PhosphorylationSQRIDDLSARDKPFD
HHCHHHCHHCCCCCC		28.4028060719
857PhosphorylationCELKFADSDADGD--
EEEEECCCCCCCC--		31.1330576142
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 SEM4D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEM4D_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 SEM4D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD72_HUMANCD72physical
12882840
PTPRC_HUMANPTPRCphysical
8955171
SEM4D_HUMANSEMA4Dphysical
1530858
PLXB1_HUMANPLXNB1physical
11937491
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 SEM4D_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis of semaphorin-plexin signalling.";
Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H.,Mitchell K.J., Siebold C., Jones E.Y.;
Nature 467:1118-1122(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 22-677 IN COMPLEX WITHPLXNB1, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF100-LYS-GLY-101; 181-PHE-LEU-182; PHE-244; PHE-246 AND LYS-395,GLYCOSYLATION AT ASN-49; ASN-77; ASN-139; ASN-191; ASN-329 ANDASN-419, AND DISULFIDE BONDS.
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-74; ASN-77;ASN-379 AND ASN-419, AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-419, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND MASSSPECTROMETRY.

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