REPI1_HUMAN - dbPTM
REPI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID REPI1_HUMAN
UniProt AC Q9BWE0
Protein Name Replication initiator 1
Gene Name REPIN1
Organism Homo sapiens (Human).
Sequence Length 567
Subcellular Localization Nucleus .
Protein Description Sequence-specific double-stranded DNA-binding protein required for initiation of chromosomal DNA replication. Binds on 5'-ATT-3' reiterated sequences downstream of the origin of bidirectional replication (OBR) and a second, homologous ATT sequence of opposite orientation situated within the OBR zone. Facilitates DNA bending..
Protein Sequence MLERRCRGPLAMGLAQPRLLSGPSQESPQTLGKESRGLRQQGTSVAQSGAQAPGRAHRCAHCRRHFPGWVALWLHTRRCQARLPLPCPECGRRFRHAPFLALHRQVHAAATPDLGFACHLCGQSFRGWVALVLHLRAHSAAKRPIACPKCERRFWRRKQLRAHLRRCHPPAPEARPFICGNCGRSFAQWDQLVAHKRVHVAEALEEAAAKALGPRPRGRPAVTAPRPGGDAVDRPFQCACCGKRFRHKPNLIAHRRVHTGERPHQCPECGKRFTNKPYLTSHRRIHTGEKPYPCKECGRRFRHKPNLLSHSKIHKRSEGSAQAAPGPGSPQLPAGPQESAAEPTPAVPLKPAQEPPPGAPPEHPQDPIEAPPSLYSCDDCGRSFRLERFLRAHQRQHTGERPFTCAECGKNFGKKTHLVAHSRVHSGERPFACEECGRRFSQGSHLAAHRRDHAPDRPFVCPDCGKAFRHKPYLAAHRRIHTGEKPYVCPDCGKAFSQKSNLVSHRRIHTGERPYACPDCDRSFSQKSNLITHRKSHIRDGAFCCAICGQTFDDEERLLAHQKKHDV
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
6 (in isoform 4)Phosphorylation-8.05-
12 (in isoform 4)Phosphorylation-6.27-
21PhosphorylationLAQPRLLSGPSQESP
CCCCHHHCCCCCCCC		53.9325159151
24PhosphorylationPRLLSGPSQESPQTL
CHHHCCCCCCCCCCC		50.5422167270
27PhosphorylationLSGPSQESPQTLGKE
HCCCCCCCCCCCCCC		18.0529255136
30PhosphorylationPSQESPQTLGKESRG
CCCCCCCCCCCCHHC		40.6429255136
33UbiquitinationESPQTLGKESRGLRQ
CCCCCCCCCHHCHHH		56.48-
33AcetylationESPQTLGKESRGLRQ
CCCCCCCCCHHCHHH		56.4819608861
35PhosphorylationPQTLGKESRGLRQQG
CCCCCCCHHCHHHHC		34.8227282143
43PhosphorylationRGLRQQGTSVAQSGA
HCHHHHCCCHHHCCC		18.7128555341
44PhosphorylationGLRQQGTSVAQSGAQ
CHHHHCCCHHHCCCC		23.4528555341
48PhosphorylationQGTSVAQSGAQAPGR
HCCCHHHCCCCCCCH		26.7628555341
76PhosphorylationWVALWLHTRRCQARL
HHHHHHHCCCCCCCC		20.0328348404
78PhosphorylationALWLHTRRCQARLPL
HHHHHCCCCCCCCCC		20.32-
81PhosphorylationLHTRRCQARLPLPCP
HHCCCCCCCCCCCCC		20.71-
84PhosphorylationRRCQARLPLPCPECG
CCCCCCCCCCCCCCC		28.8018669648
87PhosphorylationQARLPLPCPECGRRF
CCCCCCCCCCCCCCC		6.13-
90UbiquitinationLPLPCPECGRRFRHA
CCCCCCCCCCCCCCC		2.8719608861
90UbiquitinationLPLPCPECGRRFRHA
CCCCCCCCCCCCCCC		2.87-
90AcetylationLPLPCPECGRRFRHA
CCCCCCCCCCCCCCC		2.87-
90AcetylationLPLPCPECGRRFRHA
CCCCCCCCCCCCCCC		2.8719608861
196AcetylationWDQLVAHKRVHVAEA
HHHHHHHCCHHHHHH		46.5125953088
223PhosphorylationPRGRPAVTAPRPGGD
CCCCCCCCCCCCCCC		32.8124719451
259PhosphorylationIAHRRVHTGERPHQC
EEECCCCCCCCCCCC		37.5728985074
276AcetylationCGKRFTNKPYLTSHR
CCCCCCCCCCCCCCC		31.7919608861
280PhosphorylationFTNKPYLTSHRRIHT
CCCCCCCCCCCCCCC		19.35-
287PhosphorylationTSHRRIHTGEKPYPC
CCCCCCCCCCCCCCH		44.6728152594
292PhosphorylationIHTGEKPYPCKECGR
CCCCCCCCCHHHCCC		32.1228152594
309PhosphorylationRHKPNLLSHSKIHKR
CCCCCCHHCCCCCCC		28.9625690035
316PhosphorylationSHSKIHKRSEGSAQA
HCCCCCCCCCCCCCC		26.27-
317PhosphorylationHSKIHKRSEGSAQAA
CCCCCCCCCCCCCCC		51.6326074081
320PhosphorylationIHKRSEGSAQAAPGP
CCCCCCCCCCCCCCC		17.1026074081
329PhosphorylationQAAPGPGSPQLPAGP
CCCCCCCCCCCCCCC		16.7725159151
333AcetylationGPGSPQLPAGPQESA
CCCCCCCCCCCCCCC		29.8919608861
339PhosphorylationLPAGPQESAAEPTPA
CCCCCCCCCCCCCCC		27.7726074081
344PhosphorylationQESAAEPTPAVPLKP
CCCCCCCCCCCCCCC		18.5130576142
386PhosphorylationDCGRSFRLERFLRAH
CCCCCHHHHHHHHHH		5.36-
398PhosphorylationRAHQRQHTGERPFTC
HHHHHHHCCCCCEEH		32.1927251275
404PhosphorylationHTGERPFTCAECGKN
HCCCCCEEHHHCCCC		17.3124719451
426PhosphorylationVAHSRVHSGERPFAC
EEECCCCCCCCCCCH		39.2229496963
441PhosphorylationEECGRRFSQGSHLAA
HHHCCCCCCCCCHHH		31.6429214152
444PhosphorylationGRRFSQGSHLAAHRR
CCCCCCCCCHHHHCC		14.0029449344
455PhosphorylationAHRRDHAPDRPFVCP
HHCCCCCCCCCEECC		34.42-
482PhosphorylationAAHRRIHTGEKPYVC
HHCCCCCCCCCCEEC		44.6728152594
483PhosphorylationAHRRIHTGEKPYVCP
HCCCCCCCCCCEECC		27.11-
487PhosphorylationIHTGEKPYVCPDCGK
CCCCCCCEECCCCHH		26.2527732954
498PhosphorylationDCGKAFSQKSNLVSH
CCHHHHHHHCCCCCC		46.90-
500PhosphorylationGKAFSQKSNLVSHRR
HHHHHHHCCCCCCCC		27.97-
510PhosphorylationVSHRRIHTGERPYAC
CCCCCCCCCCCCCCC		38.0629496963
523PhosphorylationACPDCDRSFSQKSNL
CCCCCCCCCCHHHCH		18.9228555341
525PhosphorylationPDCDRSFSQKSNLIT
CCCCCCCCHHHCHHH		37.6328555341
539PhosphorylationTHRKSHIRDGAFCCA
HCCHHHHCCCCEEEE		30.77-
567PhosphorylationAHQKKHDV-------
HHHHHCCC-------		9.39-
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 REPI1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of REPI1_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 REPI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GEMI_HUMANGMNNphysical
16924111
HDAC1_HUMANHDAC1physical
16540471
HDAC2_HUMANHDAC2physical
16540471
GATA3_HUMANGATA3physical
18338249
NEK9_HUMANNEK9physical
22863883
TXND3_HUMANNME8physical
28514442
POTB2_HUMANPOTEB2physical
28514442
RB15B_HUMANRBM15Bphysical
28514442
KCTD2_HUMANKCTD2physical
28514442
ZN672_HUMANZNF672physical
28514442
IPO8_HUMANIPO8physical
28514442
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 REPI1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33 AND LYS-276, AND MASSSPECTROMETRY.
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-27, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory