Tag | Content |
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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 |
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477 | CGKAFSQKSNLVSHR | ubiquitination | [1] | 505 | CDRSFSQKSNLITHR | ubiquitination | [1] |
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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. |
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