CHRD_HUMAN - dbPTM
CHRD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHRD_HUMAN
UniProt AC Q9H2X0
Protein Name Chordin
Gene Name CHRD
Organism Homo sapiens (Human).
Sequence Length 955
Subcellular Localization Secreted.
Protein Description Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes (By similarity)..
Protein Sequence MPSLPAPPAPLLLLGLLLLGSRPARGAGPEPPVLPIRSEKEPLPVRGAAGCTFGGKVYALDETWHPDLGEPFGVMRCVLCACEAPQWGRRTRGPGRVSCKNIKPECPTPACGQPRQLPGHCCQTCPQERSSSERQPSGLSFEYPRDPEHRSYSDRGEPGAEERARGDGHTDFVALLTGPRSQAVARARVSLLRSSLRFSISYRRLDRPTRIRFSDSNGSVLFEHPAAPTQDGLVCGVWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIRHRALAAETFSAILTLEGPPQQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSGGLTQVPLRLQILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAARKSCDVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRDQRTVLCHMAGLQPGGHTAVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAALPYCGHSARHDTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQGTVTAHLLGPPGTPGPRRLLKGFYGSEAQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVHIANQCEVGGLRLEAAGAEGVRALGAPDTASAAPPVVPGLPALAPAKPGGPGRPRDPNTCFFEGQQRPHGARWAPNYDPLCSLCTCQRRTVICDPVVCPPPSCPHPVQAPDQCCPVCPEKQDVRDLPGLPRSRDPGEGCYFDGDRSWRAAGTRWHPVVPPFGLIKCAVCTCKGGTGEVHCEKVQCPRLACAQPVRVNPTDCCKQCPVGSGAHPQLGDPMQADGPRGCRFAGQWFPESQSWHPSVPPFGEMSCITCRCGAGVPHCERDDCSLPLSCGSGKESRCCSRCTAHRRPAPETRTDPELEKEAEGS
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
91PhosphorylationAPQWGRRTRGPGRVS
CCCCCCCCCCCCCCC
38.3224719451
130PhosphorylationQTCPQERSSSERQPS
CCCCCCCCCCCCCCC
37.15-
131PhosphorylationTCPQERSSSERQPSG
CCCCCCCCCCCCCCC
42.30-
132PhosphorylationCPQERSSSERQPSGL
CCCCCCCCCCCCCCC
37.74-
190PhosphorylationAVARARVSLLRSSLR
HHHHHHHHHHHHHHC
19.0130576142
194PhosphorylationARVSLLRSSLRFSIS
HHHHHHHHHHCEEEE
33.4221406692
195PhosphorylationRVSLLRSSLRFSISY
HHHHHHHHHCEEEEE
19.6820068231
199PhosphorylationLRSSLRFSISYRRLD
HHHHHCEEEEEECCC
12.2830576142
217N-linked_GlycosylationRIRFSDSNGSVLFEH
EEEEECCCCCEEEEC
52.31UniProtKB CARBOHYD
245PhosphorylationWRAVPRLSLRLLRAE
HCHHCHHHHHHHHHH
16.8423532336
260PhosphorylationQLHVALVTLTHPSGE
HHEEEEEEEECCCCC
27.1325278378
262PhosphorylationHVALVTLTHPSGEVW
EEEEEEEECCCCCCC
23.5225278378
265PhosphorylationLVTLTHPSGEVWGPL
EEEEECCCCCCCHHH
39.7325278378
329 (in isoform 4)Phosphorylation-3.2726270265
330 (in isoform 4)Phosphorylation-30.6926270265
335 (in isoform 4)Phosphorylation-20.6226270265
351N-linked_GlycosylationLLRELQANVSAQEPG
HHHHHHHCCCCCCCC
18.47UniProtKB CARBOHYD
365N-linked_GlycosylationGFAEVLPNLTVQEMD
CHHHHCCCCEEEEEC
44.15UniProtKB CARBOHYD
434N-linked_GlycosylationASLTLLGNGSLIYQV
EEEEEECCCCEEEEE
36.53UniProtKB CARBOHYD
674PhosphorylationRALGAPDTASAAPPV
HHCCCCCCCCCCCCC
22.8122210691
676PhosphorylationLGAPDTASAAPPVVP
CCCCCCCCCCCCCCC
27.3622210691
942PhosphorylationHRRPAPETRTDPELE
CCCCCCCCCCCHHHH
37.5018452278
944PhosphorylationRPAPETRTDPELEKE
CCCCCCCCCHHHHHH
64.4224719451

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 CHRD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHRD_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 CHRD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD3_HUMANSMAD3physical
21988832
PAR1_HUMANF2Rphysical
21988832
HRG_HUMANHRGphysical
21988832
NR0B2_HUMANNR0B2physical
21988832
SPY2_HUMANSPRY2physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
CTSR1_HUMANCATSPER1physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

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 CHRD_HUMAN

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Related Literatures of Post-Translational Modification

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