ZRAB3_MOUSE - dbPTM
ZRAB3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZRAB3_MOUSE
UniProt AC Q6NZP1
Protein Name DNA annealing helicase and endonuclease ZRANB3
Gene Name Zranb3
Organism Mus musculus (Mouse).
Sequence Length 1069
Subcellular Localization Nucleus. Chromosome. Following DNA damage, recruited to sites of DNA damage and stalled replication forks by polyubiquitinated PCNA..
Protein Description DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks (By similarity)..
Protein Sequence MPTAGSKKKAPTPQISCLTSESYTQLDFLPDKLRTKLLPFQKDGIVFALRRDGRCMVADEMGLGKTIQAIAIAYFYKEEWPLLIVVPSSLRYPWIEELEKWIPELEPEEINVVMNKTDIGRIPGSRVTVLGYGLLTTDAETLLDALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYFGKRRQWDCRGASNLSELHQLLNDIMIRRLKSEVLSQLPPKVRQRIPFDLPPAAVKELNASFEEWQKLMRAPNSGAMETVMGLITRMFKQTAIAKAGAVKDYIKMLLQNDSLKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTRVAILSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLIANGTLDSLMWAMLNRKAQVTGSTLNGRKEKLQATEDDKEKWGFLQFAEAWTPSDSFEELKDSVFTHFEKEKQHDIRSFFLPKLKKRQLETTCDDPEAFKEKITVASDPRKMATSDSTADKNGCEPEAKRLKSLSTEDHSSALEEGPSLQARATSMEVVHEVKPPLASPALPEKGWQCGFCTFLNNPGLPYCEMCENPRSRAAGRNHLQDNNKNDEDAAQESTSKSDQAGLECERQCPERLEAEQSANSKEEALEGGGEDRLPSQPEIGQLNNSGTLPVRETFMFCASRNTDRIHLYTKDGKPMNCNFIPLDIKLDLWEDLPATFQLKQNRSLILRFVREWSSLTAMKQRVLRKSGQLFCSPLLASEEITKQQAKENNTRRYITKEDVAKASMNKVKSDGGHIRLITKESMTQDSSLKKIDSACVPSLNPCPADLTVEPSPSKGYIQAVDKEGRPLCLRCQHPTCQPEQTAKASAWDSRFCSLKCQEEFWIRSNNSYLRAQVFATEHGVCQHCGVDAQELFLRMRDAPKSHRKSLLNAAWTAKLPLEQLNEMLRNPGEGHFWQVDHIRPVYEGGGQCSLDNLQTLCTVCHKERTAQQAKERSQVRRLSLATKHGSDITRFLVKK
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
117PhosphorylationINVVMNKTDIGRIPG
CEEEEECCCCCCCCC		28.0423737553
125PhosphorylationDIGRIPGSRVTVLGY
CCCCCCCCEEEEEEE		20.4418846507
297MethylationEEWQKLMRAPNSGAM
HHHHHHHHCCCCCHH		58.2818959249
306PhosphorylationPNSGAMETVMGLITR
CCCCHHHHHHHHHHH		11.6028059163
322UbiquitinationFKQTAIAKAGAVKDY
HHHHHHHHHHHHHHH		41.0417451654
338PhosphorylationKMLLQNDSLKFLVFA
HHHHCCCHHHHHHHH		40.8028059163
563PhosphorylationKMATSDSTADKNGCE
CCCCCCCCCCCCCCC		43.8128576409
578PhosphorylationPEAKRLKSLSTEDHS
HHHHHHHCCCCCCHH		31.9523984901
580PhosphorylationAKRLKSLSTEDHSSA
HHHHHCCCCCCHHHH		36.5223984901
581PhosphorylationKRLKSLSTEDHSSAL
HHHHCCCCCCHHHHH		51.2123984901
585PhosphorylationSLSTEDHSSALEEGP
CCCCCCHHHHHHHCC		29.6323984901
586PhosphorylationLSTEDHSSALEEGPS
CCCCCHHHHHHHCCC		33.1923984901
613PhosphorylationEVKPPLASPALPEKG
CCCCCCCCCCCCCCC		20.5629514104
709PhosphorylationGGEDRLPSQPEIGQL
CCCCCCCCCCCCCCC		64.0626370283
830AcetylationNTRRYITKEDVAKAS
CCCCEECHHHHHHHH		42.2119855067
840AcetylationVAKASMNKVKSDGGH
HHHHHHHCCCCCCCC		42.2619855075
885PhosphorylationADLTVEPSPSKGYIQ
CCCEECCCCCCCCEE		28.4426643407
887PhosphorylationLTVEPSPSKGYIQAV
CEECCCCCCCCEEEE		42.9526643407
1053PhosphorylationRSQVRRLSLATKHGS
HHHHHHHHHHHHCCC		17.7229895711
1056PhosphorylationVRRLSLATKHGSDIT
HHHHHHHHHCCCCHH		28.9428066266
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 ZRAB3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZRAB3_MOUSE !!
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 ZRAB3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZRAB3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZRAB3_MOUSE

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"A proteomics approach to identify the ubiquitinated proteins in mouseheart.";
Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,Choi H.W., Park Z.-Y., Yoo Y.J.;
Biochem. Biophys. Res. Commun. 357:731-736(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-322, AND MASSSPECTROMETRY.

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