ZC12A_HUMAN - dbPTM
ZC12A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZC12A_HUMAN
UniProt AC Q5D1E8
Protein Name Endoribonuclease ZC3H12A {ECO:0000305}
Gene Name ZC3H12A {ECO:0000312|HGNC:HGNC:26259}
Organism Homo sapiens (Human).
Sequence Length 599
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, P-body . Rough endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasmic granule . Predominantly localized in the cytoplasm. Colocalizes with GW182 on many granule-like structures,
Protein Description Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. [PubMed: 19909337 Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation]
Protein Sequence MSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE
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
31PhosphorylationDSHSRQGTPRPGQEL
CCCCCCCCCCCCHHH		14.0528555341
57SumoylationMKVDFFRKLGYSSTE
HHHHHHHHCCCCHHH		40.90-
57UbiquitinationMKVDFFRKLGYSSTE
HHHHHHHHCCCCHHH		40.9022505724
57SumoylationMKVDFFRKLGYSSTE
HHHHHHHHCCCCHHH		40.90-
77UbiquitinationQKLGVQADTNTVLGE
HHHCCCCCCCCHHHH		24.3330230243
87UbiquitinationTVLGELVKHGTATER
CHHHHHHHHCCCCHH		49.2829967540
98PhosphorylationATERERQTSPDPCPQ
CCHHHHCCCCCCCCC		48.7425159151
99PhosphorylationTERERQTSPDPCPQL
CHHHHCCCCCCCCCC		20.9725159151
117UbiquitinationPRGGGTPKAPNLEPP
CCCCCCCCCCCCCCC		76.0629967540
181PhosphorylationDITVFVPSWRKEQPR
CEEEEECCCCCCCCC		33.9226091039
211PhosphorylationKKKILVFTPSRRVGG
HCCEEEECCCCCCCC		16.9321815630
294UbiquitinationSLDNFLRKKPLTLEH
CHHHHHHCCCCCCCC		61.9729967540
295UbiquitinationLDNFLRKKPLTLEHR
HHHHHHCCCCCCCCC		38.5329967540
344PhosphorylationLRANALLSPPRAPSK
HHHHHHCCCCCCCCC		33.4425867546
350PhosphorylationLSPPRAPSKDKNGRR
CCCCCCCCCCCCCCC		53.1323312004
351UbiquitinationSPPRAPSKDKNGRRP
CCCCCCCCCCCCCCC		72.2130230243
359PhosphorylationDKNGRRPSPSSQSSS
CCCCCCCCCCCCCHH		35.2925849741
361PhosphorylationNGRRPSPSSQSSSLL
CCCCCCCCCCCHHCC		45.4023186163
362PhosphorylationGRRPSPSSQSSSLLT
CCCCCCCCCCHHCCC		37.1523186163
364PhosphorylationRPSPSSQSSSLLTES
CCCCCCCCHHCCCCC		24.6830576142
365PhosphorylationPSPSSQSSSLLTESE
CCCCCCCHHCCCCCE		19.8523186163
366PhosphorylationSPSSQSSSLLTESEQ
CCCCCCHHCCCCCEE		32.4223186163
371PhosphorylationSSSLLTESEQCSLDG
CHHCCCCCEEECCCC		27.9423186163
375PhosphorylationLTESEQCSLDGKKLG
CCCCEEECCCCCCCC		29.2330576142
379AcetylationEQCSLDGKKLGAQAS
EEECCCCCCCCCCCC		44.4826051181
379UbiquitinationEQCSLDGKKLGAQAS
EEECCCCCCCCCCCC		44.4829967540
386PhosphorylationKKLGAQASPGSRQEG
CCCCCCCCCCCCCCC		20.0825159151
389PhosphorylationGAQASPGSRQEGLTQ
CCCCCCCCCCCCCCC		33.8928985074
395PhosphorylationGSRQEGLTQTYAPSG
CCCCCCCCCCCCCCC		29.7124670416
397PhosphorylationRQEGLTQTYAPSGRS
CCCCCCCCCCCCCCC		19.2024043423
398PhosphorylationQEGLTQTYAPSGRSL
CCCCCCCCCCCCCCC		13.4924043423
401PhosphorylationLTQTYAPSGRSLAPS
CCCCCCCCCCCCCCC		38.3724043423
408PhosphorylationSGRSLAPSGGSGSSF
CCCCCCCCCCCCCCC		50.6230576142
411PhosphorylationSLAPSGGSGSSFGPT
CCCCCCCCCCCCCCC		38.7430576142
438PhosphorylationVSQDCLDSGIGSLES
CCHHHHHCCCCCHHH		21.25-
442PhosphorylationCLDSGIGSLESQMSE
HHHCCCCCHHHHHHH		27.35-
468PhosphorylationPGPPRAPYTGYSPYG
CCCCCCCCCCCCCCC		16.2926552605
469PhosphorylationGPPRAPYTGYSPYGS
CCCCCCCCCCCCCCC		28.6928348404
471PhosphorylationPRAPYTGYSPYGSEL
CCCCCCCCCCCCCCC		9.9326552605
472PhosphorylationRAPYTGYSPYGSELP
CCCCCCCCCCCCCCC		17.0026552605
474PhosphorylationPYTGYSPYGSELPAT
CCCCCCCCCCCCCHH		27.6128348404
476PhosphorylationTGYSPYGSELPATAA
CCCCCCCCCCCHHHH		30.0730087585
481PhosphorylationYGSELPATAAFSAFG
CCCCCCHHHHHHHHH		19.3126552605
485PhosphorylationLPATAAFSAFGRAMG
CCHHHHHHHHHHHHC		20.2626552605
497PhosphorylationAMGAGHFSVPADYPP
HHCCCCCCCCCCCCC		22.8627251275
516PhosphorylationFPPREYWSEPYPLPP
CCCHHHCCCCCCCCC		28.0027251275
535PhosphorylationLQEPPVQSPGAGRSP
CCCCCCCCCCCCCCC		26.0724719451
548PhosphorylationSPWGRAGSLAKEQAS
CCCCCHHHHHHHHHH		24.9524719451
551UbiquitinationGRAGSLAKEQASVYT
CCHHHHHHHHHHHHH		56.50-
591PhosphorylationQLAAEILSYKSQHPS
HHHHHHHHHHHCCCC		35.8529759185
592PhosphorylationLAAEILSYKSQHPSE
HHHHHHHHHHCCCCC		15.9429759185
598PhosphorylationSYKSQHPSE------
HHHHCCCCC------		54.5429759185
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 ZC12A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
438SPhosphorylation

-
438Subiquitylation

-
442SPhosphorylation

-
442Subiquitylation

-
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 ZC12A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
21115689
NEMO_HUMANIKBKGphysical
24270572
UBC_HUMANUBCphysical
24270572
UBP10_HUMANUSP10physical
24270572
P4HA3_HUMANP4HA3physical
25416956
ZC12A_HUMANZC3H12Aphysical
23355615
ZC12A_HUMANZC3H12Aphysical
19909337
IL1B_HUMANIL1Bphysical
19909337
ZC12D_HUMANZC3H12Dphysical
26134560
TANK_HUMANTANKphysical
25861989
HIF1A_HUMANHIF1Aphysical
24048733
CEBPB_HUMANCEBPBphysical
28328949
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 ZC12A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASSSPECTROMETRY.

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