PRD10_HUMAN - dbPTM
PRD10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRD10_HUMAN
UniProt AC Q9NQV6
Protein Name PR domain zinc finger protein 10
Gene Name PRDM10
Organism Homo sapiens (Human).
Sequence Length 1147
Subcellular Localization Nucleus.
Protein Description May be involved in transcriptional regulation..
Protein Sequence MDSKDESSHVWPTSAEHEQNAAQVHFVPDTGTVAQIVYTDDQVRPPQQVVYTADGASYTSVDGPEHTLVYIHPVEAAQTLFTDPGQVAYVQQDATAQQASLPVHNQVLPSIESVDGSDPLATLQTPLGRLEAKEEEDEDEDEDTEEDEEEDGEDTDLDDWEPDPPRPFDPHDLWCEECNNAHASVCPKHGPLHPIPNRPVLTRARASLPLVLYIDRFLGGVFSKRRIPKRTQFGPVEGPLVRGSELKDCYIHLKVSLDKGDRKERDLHEDLWFELSDETLCNWMMFVRPAQNHLEQNLVAYQYGHHVYYTTIKNVEPKQELKVWYAASYAEFVNQKIHDISEEERKVLREQEKNWPCYECNRRFISSEQLQQHLNSHDEKLDVFSRTRGRGRGRGKRRFGPGRRPGRPPKFIRLEITSENGEKSDDGTQDLLHFPTKEQFDEAEPATLNGLDQPEQTTIPIPQLPQETQSSLEHEPETHTLHLQPQHEESVVPTQSTLTADDMRRAKRIRLELQNAALQHLFIRKSFRPFKCLQCGKAFREKDKLDQHLRFHGREGNCPLTCDLCNKGFISSTSLESHMKLHSDQKTYSCIFCPESFDRLDLLKDHVAIHINDGYFTCPTCKKRFPDFIQVKKHVRSFHSEKIYQCTECDKAFCRPDKLRLHMLRHSDRKDFLCSTCGKQFKRKDKLREHMQRMHNPEREAKKADRISRSKTFKPRITSTDYDSFTFKCRLCMMGFRRRGMLVNHLSKRHPDMKIEEVPELTLPIIKPNRDYFCQYCDKVYKSASKRKAHILKNHPGAELPPSIRKLRPAGPGEPDPMLSTHTQLTGTIATPPVCCPHCSKQYSSKTKMVQHIRKKHPEFAQLSNTIHTPLTTAVISATPAVLTTDSATGETVVTTDLLTQAMTELSQTLTTDYRTPQGDYQRIQYIPVSQSASGLQQPQHIQLQVVQVASATSPHQSQQSTVDVGQLHDPQPYPQHAIQVQHIQVSGQPLSPSAQQAQQGLSPSHIQGSSSTQGQALQQQQQQQQNSSVQHTYLPSAWNSFRGYSSEIQMMTLPPGQFVITDSGVATPVTTGQVKAVTSGHYVLSESQSELEEKQTSALSGGVQVEPPAHSDSLDPQTNSQQQTTQYIITTTTNGNGSSEVHITKP
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
331PhosphorylationWYAASYAEFVNQKIH
HHHHHHHHHHHHHHH		41.7320068231
338PhosphorylationEFVNQKIHDISEEER
HHHHHHHHCCCHHHH		33.1319651622
341PhosphorylationNQKIHDISEEERKVL
HHHHHCCCHHHHHHH		45.0428348404
342PhosphorylationQKIHDISEEERKVLR
HHHHCCCHHHHHHHH		65.3017525332
380SumoylationHLNSHDEKLDVFSRT
HHHHCHHHHCHHHCC		56.9228112733
417PhosphorylationKFIRLEITSENGEKS
CEEEEEEECCCCCCC		22.1722115753
418PhosphorylationFIRLEITSENGEKSD
EEEEEEECCCCCCCC		34.4225159151
424PhosphorylationTSENGEKSDDGTQDL
ECCCCCCCCCCCCCC		36.3117525332
428PhosphorylationGEKSDDGTQDLLHFP
CCCCCCCCCCCCCCC		26.3817525332
436PhosphorylationQDLLHFPTKEQFDEA
CCCCCCCCHHHCCCC		46.3925850435
494PhosphorylationHEESVVPTQSTLTAD
CCCCCCCCCCCCCHH		24.4426657352
497PhosphorylationSVVPTQSTLTADDMR
CCCCCCCCCCHHHHH		20.5026657352
526PhosphorylationQHLFIRKSFRPFKCL
HHHHHHHHCCCEEEC		19.3528555341
577PhosphorylationISSTSLESHMKLHSD
CCCCCHHHHHHHCCC		33.8920068231
637PhosphorylationQVKKHVRSFHSEKIY
HHHHHHHHCCCCCEE		26.6521712546
640PhosphorylationKHVRSFHSEKIYQCT
HHHHHCCCCCEEECC		38.2829214152
658AcetylationKAFCRPDKLRLHMLR
CCCCCHHHHHHHCCC		37.8823749302
667PhosphorylationRLHMLRHSDRKDFLC
HHHCCCCCCCCHHHH		32.45-
677UbiquitinationKDFLCSTCGKQFKRK
CHHHHHCCCHHHHHH		3.5429967540
681UbiquitinationCSTCGKQFKRKDKLR
HHCCCHHHHHHHHHH		10.6129967540
708PhosphorylationAKKADRISRSKTFKP
HHHHHHCCCCCCCCC		31.25-
718PhosphorylationKTFKPRITSTDYDSF
CCCCCCCCCCCCCCC		27.1829978859
719PhosphorylationTFKPRITSTDYDSFT
CCCCCCCCCCCCCCE		19.5329978859
720PhosphorylationFKPRITSTDYDSFTF
CCCCCCCCCCCCCEE		29.9029978859
724PhosphorylationITSTDYDSFTFKCRL
CCCCCCCCCEEEECH		21.6929978859
763UbiquitinationEEVPELTLPIIKPNR
CCCCCCCCCCCCCCC		4.4829967540
767UbiquitinationELTLPIIKPNRDYFC
CCCCCCCCCCCHHHH		36.6429967540
803PhosphorylationPGAELPPSIRKLRPA
CCCCCCCCHHCCCCC		32.8425159151
885PhosphorylationATPAVLTTDSATGET
CCCCEEECCCCCCCE		24.6422798277
916PhosphorylationTLTTDYRTPQGDYQR
HHCCCCCCCCCCCCE		17.4629052541
921PhosphorylationYRTPQGDYQRIQYIP
CCCCCCCCCEEEEEE		13.4029052541
930O-linked_GlycosylationRIQYIPVSQSASGLQ
EEEEEECCCCCCCCC		17.0529351928
932O-linked_GlycosylationQYIPVSQSASGLQQP
EEEECCCCCCCCCCC		19.5229351928
1002PhosphorylationAQQAQQGLSPSHIQG
HHHHHCCCCHHHCCC		6.2217525332
1062O-linked_GlycosylationPPGQFVITDSGVATP
CCCCEEEECCCCCCC		20.8629351928
1064O-linked_GlycosylationGQFVITDSGVATPVT
CCEEEECCCCCCCCC		26.9029351928
1071O-linked_GlycosylationSGVATPVTTGQVKAV
CCCCCCCCCCCEEEE		26.8129351928
1072O-linked_GlycosylationGVATPVTTGQVKAVT
CCCCCCCCCCEEEEE		26.3329351928
1086PhosphorylationTSGHYVLSESQSELE
ECCEEEECCCHHHHH		25.7623312004
1088PhosphorylationGHYVLSESQSELEEK
CEEEECCCHHHHHHH		35.3125849741
1090PhosphorylationYVLSESQSELEEKQT
EEECCCHHHHHHHHH		54.1227251275
1101PhosphorylationEKQTSALSGGVQVEP
HHHHHHHCCCCCCCC		32.9717525332
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 PRD10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRD10_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 PRD10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PRD10_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 PRD10_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 SER-424; THR-428 ANDSER-1088, AND MASS SPECTROMETRY.

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