BOC_HUMAN - dbPTM
BOC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BOC_HUMAN
UniProt AC Q9BWV1
Protein Name Brother of CDO
Gene Name BOC
Organism Homo sapiens (Human).
Sequence Length 1114
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Enriched at sites of cell-cell contact.
Protein Description Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells..
Protein Sequence MLRGTMTAWRGMRPEVTLACLLLATAGCFADLNEVPQVTVQPASTVQKPGGTVILGCVVEPPRMNVTWRLNGKELNGSDDALGVLITHGTLVITALNNHTVGRYQCVARMPAGAVASVPATVTLANLQDFKLDVQHVIEVDEGNTAVIACHLPESHPKAQVRYSVKQEWLEASRGNYLIMPSGNLQIVNASQEDEGMYKCAAYNPVTQEVKTSGSSDRLRVRRSTAEAARIIYPPEAQTIIVTKGQSLILECVASGIPPPRVTWAKDGSSVTGYNKTRFLLSNLLIDTTSEEDSGTYRCMADNGVGQPGAAVILYNVQVFEPPEVTMELSQLVIPWGQSAKLTCEVRGNPPPSVLWLRNAVPLISSQRLRLSRRALRVLSMGPEDEGVYQCMAENEVGSAHAVVQLRTSRPSITPRLWQDAELATGTPPVSPSKLGNPEQMLRGQPALPRPPTSVGPASPQCPGEKGQGAPAEAPIILSSPRTSKTDSYELVWRPRHEGSGRAPILYYVVKHRKVTNSSDDWTISGIPANQHRLTLTRLDPGSLYEVEMAAYNCAGEGQTAMVTFRTGRRPKPEIMASKEQQIQRDDPGASPQSSSQPDHGRLSPPEAPDRPTISTASETSVYVTWIPRGNGGFPIQSFRVEYKKLKKVGDWILATSAIPPSRLSVEITGLEKGTSYKFRVRALNMLGESEPSAPSRPYVVSGYSGRVYERPVAGPYITFTDAVNETTIMLKWMYIPASNNNTPIHGFYIYYRPTDSDNDSDYKKDMVEGDKYWHSISHLQPETSYDIKMQCFNEGGESEFSNVMICETKARKSSGQPGRLPPPTLAPPQPPLPETIERPVGTGAMVARSSDLPYLIVGVVLGSIVLIIVTFIPFCLWRAWSKQKHTTDLGFPRSALPPSCPYTMVPLGGLPGHQASGQPYLSGISGRACANGIHMNRGCPSAAVGYPGMKPQQHCPGELQQQSDTSSLLRQTHLGNGYDPQSHQITRGPKSSPDEGSFLYTLPDDSTHQLLQPHHDCCQRQEQPAAVGQSGVRRAPDSPVLEAVWDPPFHSGPPCCLGLVPVEEVDSPDSCQVSGGDWCPQHPVGAYVGQEPGMQLSPGPLVRVSFETPPLTI
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---MLRGTMTAWRGM
---CCCCCCCHHCCC
12.6229083192
7Phosphorylation-MLRGTMTAWRGMRP
-CCCCCCCHHCCCCH
23.9429083192
65N-linked_GlycosylationVVEPPRMNVTWRLNG
EECCCCCEEEEEECC
29.37UniProtKB CARBOHYD
67PhosphorylationEPPRMNVTWRLNGKE
CCCCCEEEEEECCEE
10.4025954137
76N-linked_GlycosylationRLNGKELNGSDDALG
EECCEECCCCCCCEE
49.35UniProtKB CARBOHYD
87PhosphorylationDALGVLITHGTLVIT
CCEEEEEECCEEEEE
15.3022210691
94PhosphorylationTHGTLVITALNNHTV
ECCEEEEEECCCCCC
20.0125954137
98N-linked_GlycosylationLVITALNNHTVGRYQ
EEEEECCCCCCCEEE
32.81UniProtKB CARBOHYD
189N-linked_GlycosylationSGNLQIVNASQEDEG
CCCEEECCCCHHCCC
35.19UniProtKB CARBOHYD
224PhosphorylationDRLRVRRSTAEAARI
CCEEEEHHHHHHHHE
22.7722210691
225PhosphorylationRLRVRRSTAEAARII
CEEEEHHHHHHHHEE
27.0622210691
233PhosphorylationAEAARIIYPPEAQTI
HHHHHEECCCCCCEE
15.4622210691
239PhosphorylationIYPPEAQTIIVTKGQ
ECCCCCCEEEEECCC
21.5122210691
274PhosphorylationDGSSVTGYNKTRFLL
CCCCCCCCCHHHHHE
12.24-
275N-linked_GlycosylationGSSVTGYNKTRFLLS
CCCCCCCCHHHHHEE
40.33UniProtKB CARBOHYD
372PhosphorylationSSQRLRLSRRALRVL
CHHHHHHHHHHHHHH
17.1820068231
412PhosphorylationQLRTSRPSITPRLWQ
EEECCCCCCCHHHHC
37.6724719451
454O-linked_GlycosylationALPRPPTSVGPASPQ
CCCCCCCCCCCCCCC
30.74OGP
479PhosphorylationAEAPIILSSPRTSKT
CCCCEEEECCCCCCC
28.0817081983
480PhosphorylationEAPIILSSPRTSKTD
CCCEEEECCCCCCCC
18.2417081983
483PhosphorylationIILSSPRTSKTDSYE
EEEECCCCCCCCCEE
37.65-
486PhosphorylationSSPRTSKTDSYELVW
ECCCCCCCCCEEEEE
29.91-
488PhosphorylationPRTSKTDSYELVWRP
CCCCCCCCEEEEECC
26.24-
517N-linked_GlycosylationVKHRKVTNSSDDWTI
EECCCCCCCCCCCEE
42.37UniProtKB CARBOHYD
517 (in isoform 3)Phosphorylation-42.3724043423
519 (in isoform 3)Phosphorylation-41.4824043423
520 (in isoform 3)Phosphorylation-56.1124043423
524 (in isoform 3)Phosphorylation-2.8624043423
526 (in isoform 3)Phosphorylation-26.5024043423
536 (in isoform 3)Phosphorylation-2.8824043423
538 (in isoform 3)Phosphorylation-39.9624043423
564PhosphorylationEGQTAMVTFRTGRRP
CCCEEEEEEECCCCC
8.3624719451
665PhosphorylationAIPPSRLSVEITGLE
CCCHHHEEEEEECCC
19.3230631047
669PhosphorylationSRLSVEITGLEKGTS
HHEEEEEECCCCCCC
23.3930631047
677PhosphorylationGLEKGTSYKFRVRAL
CCCCCCCEEEEEEEH
17.6230631047
693PhosphorylationMLGESEPSAPSRPYV
HCCCCCCCCCCCCEE
49.0824275569
696PhosphorylationESEPSAPSRPYVVSG
CCCCCCCCCCEEEEC
45.6724275569
699PhosphorylationPSAPSRPYVVSGYSG
CCCCCCCEEEECCCC
16.6324275569
702PhosphorylationPSRPYVVSGYSGRVY
CCCCEEEECCCCEEE
23.2124275569
704PhosphorylationRPYVVSGYSGRVYER
CCEEEECCCCEEEEC
10.6324275569
725N-linked_GlycosylationITFTDAVNETTIMLK
EECCCCCCCCEEEEE
42.49UniProtKB CARBOHYD
759N-linked_GlycosylationYRPTDSDNDSDYKKD
ECCCCCCCCCCHHHH
55.42UniProtKB CARBOHYD
968PhosphorylationQQQSDTSSLLRQTHL
HCCCCHHHHHHHHCC
33.2524719451
1109PhosphorylationLVRVSFETPPLTI--
EEEEEEECCCCCC--
28.3528348404

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 BOC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BOC_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 BOC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
12634428
CADH2_HUMANCDH2physical
12634428
LRIF1_HUMANLRIF1physical
16169070
CDON_HUMANCDONphysical
11782431
CAD15_HUMANCDH15physical
12634428
KLH24_HUMANKLHL24physical
28514442
OAF_HUMANOAFphysical
28514442
FBX2_HUMANFBXO2physical
28514442
ACOX1_HUMANACOX1physical
28514442
WDR54_HUMANWDR54physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BOC_HUMAN

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Related Literatures of Post-Translational Modification

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