PCD12_HUMAN - dbPTM
PCD12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCD12_HUMAN
UniProt AC Q9NPG4
Protein Name Protocadherin-12 {ECO:0000305}
Gene Name PCDH12 {ECO:0000312|HGNC:HGNC:8657}
Organism Homo sapiens (Human).
Sequence Length 1184
Subcellular Localization Protocadherin-12: Cell membrane
Single-pass type I membrane protein . Cell junction .
Protocadherin-12, secreted form: Secreted . The secreted form is produced following cleavage by ADAM10.
Protein Description Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions (By similarity). Acts as a regulator of cell migration, probably via increasing cell-cell adhesion. [PubMed: 21402705 Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions (By similarity Unable to bind to catenins, weakly associates with the cytoskeleton (By similarity]
Protein Sequence MMQLLQLLLGLLGPGGYLFLLGDCQEVTTLTVKYQVSEEVPSGTVIGKLSQELGREERRRQAGAAFQVLQLPQALPIQVDSEEGLLSTGRRLDREQLCRQWDPCLVSFDVLATGDLALIHVEIQVLDINDHQPRFPKGEQELEISESASLRTRIPLDRALDPDTGPNTLHTYTLSPSEHFALDVIVGPDETKHAELIVVKELDREIHSFFDLVLTAYDNGNPPKSGTSLVKVNVLDSNDNSPAFAESSLALEIQEDAAPGTLLIKLTATDPDQGPNGEVEFFLSKHMPPEVLDTFSIDAKTGQVILRRPLDYEKNPAYEVDVQARDLGPNPIPAHCKVLIKVLDVNDNIPSIHVTWASQPSLVSEALPKDSFIALVMADDLDSGHNGLVHCWLSQELGHFRLKRTNGNTYMLLTNATLDREQWPKYTLTLLAQDQGLQPLSAKKQLSIQISDINDNAPVFEKSRYEVSTRENNLPSLHLITIKAHDADLGINGKVSYRIQDSPVAHLVAIDSNTGEVTAQRSLNYEEMAGFEFQVIAEDSGQPMLASSVSVWVSLLDANDNAPEVVQPVLSDGKASLSVLVNASTGHLLVPIETPNGLGPAGTDTPPLATHSSRPFLLTTIVARDADSGANGEPLYSIRSGNEAHLFILNPHTGQLFVNVTNASSLIGSEWELEIVVEDQGSPPLQTRALLRVMFVTSVDHLRDSARKPGALSMSMLTVICLAVLLGIFGLILALFMSICRTEKKDNRAYNCREAESTYRQQPKRPQKHIQKADIHLVPVLRGQAGEPCEVGQSHKDVDKEAMMEAGWDPCLQAPFHLTPTLYRTLRNQGNQGAPAESREVLQDTVNLLFNHPRQRNASRENLNLPEPQPATGQPRSRPLKVAGSPTGRLAGDQGSEEAPQRPPASSATLRRQRHLNGKVSPEKESGPRQILRSLVRLSVAAFAERNPVEELTVDSPPVQQISQLLSLLHQGQFQPKPNHRGNKYLAKPGGSRSAIPDTDGPSARAGGQTDPEQEEGPLDPEEDLSVKQLLEEELSSLLDPSTGLALDRLSAPDPAWMARLSLPLTTNYRDNVISPDAAATEEPRTFQTFGKAEAPELSPTGTRLASTFVSEMSSLLEMLLEQRSSMPVEAASEALRRLSVCGRTLSLDLATSAASGMKVQGDPGGKTGTEGKSRGSSSSSRCL
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
34PhosphorylationVTTLTVKYQVSEEVP
EEEEEEEEEEECCCC		15.1522817900
147PhosphorylationQELEISESASLRTRI
CEEEECCCCCCCCCC		19.1624905233
149PhosphorylationLEISESASLRTRIPL
EEECCCCCCCCCCCC		27.8824905233
294PhosphorylationMPPEVLDTFSIDAKT
CCHHHHCEEEEECCC		18.3425690035
296PhosphorylationPEVLDTFSIDAKTGQ
HHHHCEEEEECCCCC		22.9625690035
415N-linked_GlycosylationNTYMLLTNATLDREQ
CEEEEEEECEECHHH		30.78UniProtKB CARBOHYD
522PhosphorylationGEVTAQRSLNYEEMA
CCEEEEEECCHHHHC		14.6429759185
525PhosphorylationTAQRSLNYEEMAGFE
EEEEECCHHHHCCCE		20.6829759185
582N-linked_GlycosylationASLSVLVNASTGHLL
EEEEEEEECCCCCEE		24.82UniProtKB CARBOHYD
603O-linked_GlycosylationNGLGPAGTDTPPLAT
CCCCCCCCCCCCCCC		38.51OGP
619PhosphorylationSSRPFLLTTIVARDA
CCCCEEEEEEEEECC		19.3422210691
620PhosphorylationSRPFLLTTIVARDAD
CCCEEEEEEEEECCC		17.2722210691
637PhosphorylationANGEPLYSIRSGNEA
CCCCCCEEEECCCCE		21.1424719451
659N-linked_GlycosylationHTGQLFVNVTNASSL
CCCCEEEEECCHHHH		27.79UniProtKB CARBOHYD
662N-linked_GlycosylationQLFVNVTNASSLIGS
CEEEEECCHHHHCCC		33.28UniProtKB CARBOHYD
697PhosphorylationLLRVMFVTSVDHLRD
HHHHHHHHCHHHHHH		16.2722210691
698PhosphorylationLRVMFVTSVDHLRDS
HHHHHHHCHHHHHHC		21.9022210691
705PhosphorylationSVDHLRDSARKPGAL
CHHHHHHCCCCCCCC		24.4422210691
713PhosphorylationARKPGALSMSMLTVI
CCCCCCCCHHHHHHH		14.3122210691
859PhosphorylationHPRQRNASRENLNLP
CHHHHCCCCCCCCCC		43.6126657352
885PhosphorylationRPLKVAGSPTGRLAG
CCCEECCCCCCCCCC		15.0024275569
896PhosphorylationRLAGDQGSEEAPQRP
CCCCCCCCCCCCCCC		26.9923312004
906PhosphorylationAPQRPPASSATLRRQ
CCCCCCCCHHHHHHH		26.6923312004
907PhosphorylationPQRPPASSATLRRQR
CCCCCCCHHHHHHHH		27.6423312004
909PhosphorylationRPPASSATLRRQRHL
CCCCCHHHHHHHHHH		23.8123312004
921PhosphorylationRHLNGKVSPEKESGP
HHHCCCCCCCCCCCH		30.7229083192
992PhosphorylationYLAKPGGSRSAIPDT
EECCCCCCCCCCCCC		29.04-
1062PhosphorylationPAWMARLSLPLTTNY
HHHHHHHCCCCCCCC		23.5314702039
1099PhosphorylationKAEAPELSPTGTRLA
CCCCCCCCCCCHHHH		20.8224275569
1133PhosphorylationSMPVEAASEALRRLS
CCCHHHHHHHHHHHC		30.37-
1140PhosphorylationSEALRRLSVCGRTLS
HHHHHHHCCCCCEEE		17.3528857561
1145PhosphorylationRLSVCGRTLSLDLAT
HHCCCCCEEEEEHHH		13.14-
1147PhosphorylationSVCGRTLSLDLATSA
CCCCCEEEEEHHHHH		21.15-
1152PhosphorylationTLSLDLATSAASGMK
EEEEEHHHHHHCCCE		26.62-
1168PhosphorylationQGDPGGKTGTEGKSR
ECCCCCCCCCCCCCC		53.24-
1170PhosphorylationDPGGKTGTEGKSRGS
CCCCCCCCCCCCCCC		46.96-
1179PhosphorylationGKSRGSSSSSRCL--
CCCCCCCCCCCCC--		33.75-
1179O-linked_GlycosylationGKSRGSSSSSRCL--
CCCCCCCCCCCCC--		33.7531492838
1180O-linked_GlycosylationKSRGSSSSSRCL---
CCCCCCCCCCCC---		24.6131492838
1181O-linked_GlycosylationSRGSSSSSRCL----
CCCCCCCCCCC----		29.0331492838
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 PCD12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCD12_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 PCD12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCD10_HUMANPCDH10physical
28514442
PCD17_HUMANPCDH17physical
28514442
CLIC3_HUMANCLIC3physical
28514442
PCDGB_HUMANPCDHGA11physical
28514442
DCBD1_HUMANDCBLD1physical
28514442
CDON_HUMANCDONphysical
28514442
PTPRS_HUMANPTPRSphysical
28514442
PCDGK_HUMANPCDHGC3physical
28514442
TMTC4_HUMANTMTC4physical
28514442
LTBP1_HUMANLTBP1physical
28514442
CD166_HUMANALCAMphysical
28514442
CELR2_HUMANCELSR2physical
28514442
RL23_HUMANRPL23physical
28514442
EFNB1_HUMANEFNB1physical
28514442
CELR1_HUMANCELSR1physical
28514442
PCDH7_HUMANPCDH7physical
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 PCD12_HUMAN

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Related Literatures of Post-Translational Modification

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