CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001023
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Checkpoint protein HUS1 
Protein Synonyms/Alias
 hHUS1 
Gene Name
 HUS1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38TLRISPDKLNFILCDubiquitination[1]
136VTHDIPIKVIPRKLWubiquitination[1, 2]
164SIYLPVLKTMKSVVEubiquitination[3]
167LPVLKTMKSVVEKMKubiquitination[1]
250GQQVNPTKALCNIVNubiquitination[1]
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] 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]
 [3] 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
Functional Description
 Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 280 AA 
Protein Sequence
MKFRAKIVDG ACLNHFTRIS NMIAKLAKTC TLRISPDKLN FILCDKLANG GVSMWCELEQ 60
ENFFNEFQME GVSAENNEIY LELTSENLSR ALKTAQNARA LKIKLTNKHF PCLTVSVELL 120
SMSSSSRIVT HDIPIKVIPR KLWKDLQEPV VPDPDVSIYL PVLKTMKSVV EKMKNISNHL 180
VIEANLDGEL NLKIETELVC VTTHFKDLGN PPLASESTHE DRNVEHMAEV HIDIRKLLQF 240
LAGQQVNPTK ALCNIVNNKM VHFDLLHEDV SLQYFIPALS 280 
Gene Ontology
 GO:0030896; C:checkpoint clamp complex; IEA:InterPro.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
 GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006260; P:DNA replication; TAS:Reactome.
 GO:0000724; P:double-strand break repair via homologous recombination; IEA:Compara.
 GO:0009790; P:embryo development; IEA:Compara.
 GO:0008156; P:negative regulation of DNA replication; IEA:Compara.
 GO:0006468; P:protein phosphorylation; IEA:Compara.
 GO:0001932; P:regulation of protein phosphorylation; IEA:Compara.
 GO:0009411; P:response to UV; IEA:Compara. 
Interpro
 IPR016580; Cell_cycle_HUS1.
 IPR007150; Hus1/Mec3. 
Pfam
 PF04005; Hus1 
SMART
  
PROSITE
  
PRINTS