CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014074
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Replication initiator 1 
Protein Synonyms/Alias
 Zinc finger protein 464; Zfp-464 
Gene Name
 Repin1 
Gene Synonyms/Alias
 Zfp464 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
477CGKAFSQKSNLVSHRubiquitination[1]
505CDRSFSQKSNLITHRubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional 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 (By similarity). 
Sequence Annotation
 ZN_FING 52 74 C2H2-type 1; atypical.
 ZN_FING 80 102 C2H2-type 2.
 ZN_FING 111 133 C2H2-type 3.
 ZN_FING 140 162 C2H2-type 4; atypical.
 ZN_FING 172 194 C2H2-type 5.
 ZN_FING 229 251 C2H2-type 6.
 ZN_FING 257 279 C2H2-type 7.
 ZN_FING 285 307 C2H2-type 8.
 ZN_FING 353 375 C2H2-type 9.
 ZN_FING 381 403 C2H2-type 10.
 ZN_FING 409 431 C2H2-type 11.
 ZN_FING 437 459 C2H2-type 12.
 ZN_FING 465 487 C2H2-type 13.
 ZN_FING 493 515 C2H2-type 14.
 ZN_FING 521 543 C2H2-type 15.
 MOD_RES 27 27 Phosphoserine (By similarity).
 MOD_RES 269 269 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; DNA replication; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 545 AA 
Protein Sequence
MLEQRCRGPT AMGPAQPWLF SGPSQESSQP DRGLRYQGKS AQPRGQTPGK VHRCAHCRKR 60
FPGWVALWLH ARRCQARLPL PCHECNQRFR HAPFLALHLQ VHASAVPDLG FICHLCGHSF 120
RGWVALVLHL RAHSASKRPI TCPECDRRFW RQKQLRAHLR RCQPPVPEAR PFICGNCGRS 180
FAQWDQLVVH KRVHVAEALE EAAAKALGPR PRGRPAAPRP GGDAVDRPFQ CACCGKRFRH 240
KPNLIAHRRV HTGERPHQCP ECGKRFTNKP YLTSHRRIHT GEKPYPCTEC GRRFRHKPNL 300
LSHSKIHKRL EVSAQAAPHP ESHQIAAEPM AQPALGVPLG SPRTPAEAPA LLHSCSDCGR 360
SFRLERFLRL HQRQHTGERP FACTECGKNF GKKTHLVAHS RVHSGERPFA CEECGRRFSQ 420
GSHLAAHRRD HAPERPFVCP DCGKAFRHKP YLAAHRRIHT GEKPYVCPDC GKAFSQKSNL 480
VSHRRIHTGE RPYACPDCDR SFSQKSNLIT HRKSHIRDGA FCCAICGQTF DDEDRLLMHQ 540
KKHDA 545 
Gene Ontology
 GO:0022626; C:cytosolic ribosome; IDA:MGI.
 GO:0005811; C:lipid particle; IDA:MGI.
 GO:0031965; C:nuclear membrane; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:2000191; P:regulation of fatty acid transport; IMP:MGI.
 GO:2001273; P:regulation of glucose import in response to insulin stimulus; IMP:MGI. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00096; zf-C2H2 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS