RPTN_HUMAN - dbPTM
RPTN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPTN_HUMAN
UniProt AC Q6XPR3
Protein Name Repetin
Gene Name RPTN
Organism Homo sapiens (Human).
Sequence Length 784
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein. Reversibly binds calcium..
Protein Sequence MAQLLNSILSVIDVFHKYAKGNGDCALLCKEELKQLLLAEFGDILQRPNDPETVETILNLLDQDRDGHIDFHEYLLLVFQLVQACYHKLDNKSHGGRTSQQERGQEGAQDCKFPGNTGRQHRQRHEEERQNSHHSQPERQDGDSHHGQPERQDRDSHHGQSEKQDRDSHHSQPERQDRDSHHNQSERQDKDFSFDQSERQSQDSSSGKKVSHKSTSGQAKWQGHIFALNRCEKPIQDSHYGQSERHTQQSETLGQASHFNQTNQQKSGSYCGQSERLGQELGCGQTDRQGQSSHYGQTDRQDQSYHYGQTDRQGQSSHYSQTDRQGQSSHYSQPDRQGQSSHYGQMDRKGQCYHYDQTNRQGQGSHYSQPNRQGQSSHYGQPDTQDQSSHYGQTDRQDQSSHYGQTERQGQSSHYSQMDRQGQGSHYGQTDRQGQSSHYGQPDRQGQNSHYGQTDRQGQSSHYGQTDRQGQSSHYSQPDKQGQSSHYGKIDRQDQSYHYGQPDGQGQSSHYGQTDRQGQSFHYGQPDRQGQSSHYSQMDRQGQSSHYGQTDRQGQSSHYGQTDRQGQSYHYGQTDRQGQSSHYIQSQTGEIQGQNKYFQGTEGTRKASYVEQSGRSGRLSQQTPGQEGYQNQGQGFQSRDSQQNGHQVWEPEEDSQHHQHKLLAQIQQERPLCHKGRDWQSCSSEQGHRQAQTRQSHGEGLSHWAEEEQGHQTWDRHSHESQEGPCGTQDRRTHKDEQNHQRRDRQTHEHEQSHQRRDRQTHEDKQNRQRRDRQTHEDEQNHQR
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
53PhosphorylationQRPNDPETVETILNL
CCCCCHHHHHHHHHH		29.09-
56PhosphorylationNDPETVETILNLLDQ
CCHHHHHHHHHHHCC		26.82-
175MethylationSHHSQPERQDRDSHH
CCCCCCHHCCCCCCC		50.8416306339
180PhosphorylationPERQDRDSHHNQSER
CHHCCCCCCCCHHHH		27.7820068231
185PhosphorylationRDSHHNQSERQDKDF
CCCCCCHHHHHHCCC		39.8120068231
201PhosphorylationFDQSERQSQDSSSGK
CCHHHHHCCCCCCCC		42.02-
204PhosphorylationSERQSQDSSSGKKVS
HHHHCCCCCCCCCCC		20.83-
205PhosphorylationERQSQDSSSGKKVSH
HHHCCCCCCCCCCCC		51.94-
206PhosphorylationRQSQDSSSGKKVSHK
HHCCCCCCCCCCCCC		59.59-
233MethylationFALNRCEKPIQDSHY
EEEECCCCCCCCCCC		51.5523644510
247PhosphorylationYGQSERHTQQSETLG
CCCCHHHHHHHHHHH		34.2317525332
252PhosphorylationRHTQQSETLGQASHF
HHHHHHHHHHCHHHC		41.2417525332
262PhosphorylationQASHFNQTNQQKSGS
CHHHCCCCCCCCCCC		35.7817525332
304PhosphorylationQTDRQDQSYHYGQTD
CCCCCCCCCCCCCCC		23.3624043423
305PhosphorylationTDRQDQSYHYGQTDR
CCCCCCCCCCCCCCC		8.0724043423
307PhosphorylationRQDQSYHYGQTDRQG
CCCCCCCCCCCCCCC		11.6024043423
310PhosphorylationQSYHYGQTDRQGQSS
CCCCCCCCCCCCCCC		28.8724043423
340PhosphorylationQPDRQGQSSHYGQMD
CCCCCCCCCCCCCCC		26.3824043423
341PhosphorylationPDRQGQSSHYGQMDR
CCCCCCCCCCCCCCC		16.9124043423
343PhosphorylationRQGQSSHYGQMDRKG
CCCCCCCCCCCCCCC		15.8224043423
353PhosphorylationMDRKGQCYHYDQTNR
CCCCCCEEEEECCCC		8.7724043423
355PhosphorylationRKGQCYHYDQTNRQG
CCCCEEEEECCCCCC		5.3524043423
358PhosphorylationQCYHYDQTNRQGQGS
CEEEEECCCCCCCCC		29.4824043423
412PhosphorylationQTERQGQSSHYSQMD
CCCCCCCCCCCCCCC		26.3824043423
413PhosphorylationTERQGQSSHYSQMDR
CCCCCCCCCCCCCCC		20.6824043423
415PhosphorylationRQGQSSHYSQMDRQG
CCCCCCCCCCCCCCC		11.5324043423
416PhosphorylationQGQSSHYSQMDRQGQ
CCCCCCCCCCCCCCC		17.3824043423
436PhosphorylationQTDRQGQSSHYGQPD
CCCCCCCCCCCCCCC		26.3830576142
439PhosphorylationRQGQSSHYGQPDRQG
CCCCCCCCCCCCCCC		21.2830576142
463PhosphorylationRQGQSSHYGQTDRQG
CCCCCCCCCCCCCCC		16.9330576142
496PhosphorylationKIDRQDQSYHYGQPD
CCCCCCCCCCCCCCC		23.3622210691
523PhosphorylationRQGQSFHYGQPDRQG
CCCCEEECCCCCCCC		18.5525690035
532PhosphorylationQPDRQGQSSHYSQMD
CCCCCCCCCCCCCCC		26.3822210691
533PhosphorylationPDRQGQSSHYSQMDR
CCCCCCCCCCCCCCC		20.6824043423
535PhosphorylationRQGQSSHYSQMDRQG
CCCCCCCCCCCCCCC		11.5324043423
536PhosphorylationQGQSSHYSQMDRQGQ
CCCCCCCCCCCCCCC		17.3822210691
608PhosphorylationTEGTRKASYVEQSGR
CCCCEEEEEEECCCC		32.5224719451
609PhosphorylationEGTRKASYVEQSGRS
CCCEEEEEEECCCCC		16.9324719451
613PhosphorylationKASYVEQSGRSGRLS
EEEEEECCCCCCCCC		23.7524719451
721PhosphorylationWDRHSHESQEGPCGT
CCCCCCCCCCCCCCC		28.2727966365
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 RPTN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPTN_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 RPTN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RPTN_HUMAN !!
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 RPTN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-247; THR-252 ANDTHR-262, AND MASS SPECTROMETRY.

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