CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023234
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase iota 
Protein Synonyms/Alias
 Eta2; RAD30 homolog B 
Gene Name
 POLI 
Gene Synonyms/Alias
 RAD30B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78SNPELKDKPLGVQQKubiquitination[1]
112NVRDAKEKCPQLVLVubiquitination[1]
163DLTEMVEKRLQQLQSubiquitination[2, 3]
228CAGVASNKLLAKLVSubiquitination[1]
270EIPGIGYKTAKCLEAubiquitination[1]
273GIGYKTAKCLEALGIubiquitination[1, 4]
292DLQTFSPKILEKELGubiquitination[1, 4]
296FSPKILEKELGISVAubiquitination[1, 4]
308SVAQRIQKLSFGEDNubiquitination[2, 3]
334FSEEDSFKKCSSEVEubiquitination[1, 2, 3]
335SEEDSFKKCSSEVEAubiquitination[1]
345SEVEAKNKIEELLASubiquitination[1]
446KALNTAKKGLIDYYLubiquitination[1]
511LDTTNFSKEKDINEFubiquitination[2]
547QEEILSGKSREKFQGubiquitination[4, 5]
555SREKFQGKGSVSCPLubiquitination[1, 5, 6]
574GVLSFFSKKQMQDIPubiquitination[4]
575VLSFFSKKQMQDIPIubiquitination[1]
639ERISQGPKEPQGFHFubiquitination[1]
678NHTTDSHKQTVATDSubiquitination[2]
740SDFHIGHK*******ubiquitination[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity. 
Sequence Annotation
 DOMAIN 55 268 UmuC.
 REGION 325 332 DNA binding.
 REGION 368 386 DNA binding.
 ACT_SITE 152 152 Proton acceptor (Potential).
 METAL 59 59 Magnesium.
 METAL 151 151 Magnesium.
 BINDING 64 64 dNTP.
 BINDING 96 96 dNTP.  
Keyword
 3D-structure; Complete proteome; DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Schiff base; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 740 AA 
Protein Sequence
MEKLGVEPEE EGGGDDDEED AEAWAMELAD VGAAASSQGV HDQVLPTPNA SSRVIVHVDL 60
DCFYAQVEMI SNPELKDKPL GVQQKYLVVT CNYEARKLGV KKLMNVRDAK EKCPQLVLVN 120
GEDLTRYREM SYKVTELLEE FSPVVERLGF DENFVDLTEM VEKRLQQLQS DELSAVTVSG 180
HVYNNQSINL LDVLHIRLLV GSQIAAEMRE AMYNQLGLTG CAGVASNKLL AKLVSGVFKP 240
NQQTVLLPES CQHLIHSLNH IKEIPGIGYK TAKCLEALGI NSVRDLQTFS PKILEKELGI 300
SVAQRIQKLS FGEDNSPVIL SGPPQSFSEE DSFKKCSSEV EAKNKIEELL ASLLNRVCQD 360
GRKPHTVRLI IRRYSSEKHY GRESRQCPIP SHVIQKLGTG NYDVMTPMVD ILMKLFRNMV 420
NVKMPFHLTL LSVCFCNLKA LNTAKKGLID YYLMPSLSTT SRSGKHSFKM KDTHMEDFPK 480
DKETNRDFLP SGRIESTRTR ESPLDTTNFS KEKDINEFPL CSLPEGVDQE VFKQLPVDIQ 540
EEILSGKSRE KFQGKGSVSC PLHASRGVLS FFSKKQMQDI PINPRDHLSS SKQVSSVSPC 600
EPGTSGFNSS SSSYMSSQKD YSYYLDNRLK DERISQGPKE PQGFHFTNSN PAVSAFHSFP 660
NLQSEQLFSR NHTTDSHKQT VATDSHEGLT ENREPDSVDE KITFPSDIDP QVFYELPEAV 720
QKELLAEWKR AGSDFHIGHK 740 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:ProtInc.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0003887; F:DNA-directed DNA polymerase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 
Interpro
 IPR017961; DNA_pol_Y-fam_little_finger.
 IPR001126; DNA_repair_prot_UmuC-like.
 IPR017963; DNA_repair_prot_UmuC-like_N. 
Pfam
 PF00817; IMS
 PF11799; IMS_C 
SMART
  
PROSITE
 PS50173; UMUC 
PRINTS