UniProt Accession

 HUS1_HUMAN; O60921 

Genbank Protein ID

 Y16893; AF076844; AF110393; CR536552; BT019481; BT019482; AF503165; BC007013 

Genbank Nucleotide ID

 CAA76518.1; AAC95526.1; AAD25350.1; CAG38789.1; AAV38288.1; AAV38289.1; AAM18968.1; AAH07013.1 

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
38	TLRISPDKLNFILCD	ubiquitination	[1]
136	VTHDIPIKVIPRKLW	ubiquitination	[1, 2]
164	SIYLPVLKTMKSVVE	ubiquitination	[3]
167	LPVLKTMKSVVEKMK	ubiquitination	[1]
250	GQQVNPTKALCNIVN	ubiquitination	[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

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