Q96B01 (R51A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 82.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: RAD51-associated protein 1 Alternative name(s): RAD51-interacting protein | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 352 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Functionally cooperates with PALB2 in promoting of D-loop formation by RAD51. Binds to single and double stranded DNA, and is capable of aggregating DNA. Also binds RNA. Ref.1 Ref.10 |
| Subunit structure | Isoform 2 interacts with RAD51. Interacts with PALB2. Ref.1 Ref.5 Ref.10 |
| Subcellular location | Nucleus By similarity. Note: Colocalizes with RAD51 to multiple nuclear foci By similarity. |
| Tissue specificity | Highly expressed in testis and thymus. Lower levels in colon and small intestine. Little or no expression in spleen, prostate, ovary and peripheral blood leukocytes. Ref.1 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA recombination DNA repair |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Ligand | DNA-binding RNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | double-strand break repair via homologous recombination Non-traceable author statement Ref.1. Source: UniProtKB |
| Cellular component | nucleus Inferred by curator Ref.1. Source: UniProtKB |
| Molecular function | RNA binding Inferred from direct assay Ref.1. Source: UniProtKB double-stranded DNA bindingInferred from direct assay Ref.1. Source: UniProtKB protein bindingInferred from physical interaction Ref.10Ref.1. Source: UniProtKB single-stranded DNA bindingInferred from direct assay Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| RAD51 | Q06609 | 4 | EBI-1178743,EBI-297202 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: Q96B01-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 Ref.1 (identifier: Q96B01-2) The sequence of this isoform differs from the canonical sequence as follows: 71-87: Missing. | ||||||
| Isoform 3 Ref.1 (identifier: Q96B01-3) The sequence of this isoform differs from the canonical sequence as follows: 258-307: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 352 | 352 | RAD51-associated protein 1 | PRO_0000097140 | |||||
Regions | |||||||||
| Region | 313 – 352 | 40 | Interaction with RAD51 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 19 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 21 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 66 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 120 | 1 | Phosphoserine Ref.6 Ref.8 | ||||||
| Modified residue | 280 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 327 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 343 | 1 | N6-acetyllysine Ref.9 | ||||||
Natural variations | |||||||||
| Alternative sequence | 71 – 87 | 17 | Missing in isoform 2. Ref.1 | VSP_051739 | |||||
| Alternative sequence | 258 – 307 | 50 | Missing in isoform 3. Ref.1 | VSP_051740 | |||||
| Natural variant | 68 | 1 | K → Q. Corresponds to variant rs34810644 [ dbSNP | Ensembl ]. | VAR_056976 | |||||
Experimental info | |||||||||
| Mutagenesis | 333 | 1 | R → A: Strongly decreases interaction with RAD51; when associated with Q-336; A-345 and A-346. Ref.5 | ||||||
| Mutagenesis | 336 | 1 | L → Q: Strongly decreases interaction with RAD51; when associated with A-333; A-345 and A-346. Ref.5 | ||||||
| Mutagenesis | 345 – 346 | 2 | LH → AA: Strongly decreases interaction with RAD51; when associated with A-333; and Q-336. | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A novel nucleic acid-binding protein that interacts with human rad51 recombinase." Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M. Nucleic Acids Res. 25:4946-4953(1997) [PubMed: 9396801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH RAD51, TISSUE SPECIFICITY. Tissue: Cervix carcinoma. |
| [2] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Bone marrow and Urinary bladder. |
| [5] | "RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51." Kovalenko O.V., Wiese C., Schild D. Nucleic Acids Res. 34:5081-5092(2006) [PubMed: 16990250] [Abstract] Cited for: INTERACTION WITH RAD51, MUTAGENESIS OF ARG-333; LEU-336 AND 345-LEU-HIS-346. |
| [6] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [7] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; THR-66; SER-280 AND SER-327, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [8] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [9] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343, MASS SPECTROMETRY. |
| [10] | "Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2." Dray E., Etchin J., Wiese C., Saro D., Williams G.J., Hammel M., Yu X., Galkin V.E., Liu D., Tsai M.S., Sy S.M., Schild D., Egelman E., Chen J., Sung P. Nat. Struct. Mol. Biol. 17:1255-1259(2010) [PubMed: 20871616] [Abstract] Cited for: FUNCTION, INTERACTION WITH PALB2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF006259 mRNA. Translation: AAC39554.1. AK096930 mRNA. Translation: BAC04902.1. AK291948 mRNA. Translation: BAF84637.1. CH471116 Genomic DNA. Translation: EAW88844.1. BC006992 mRNA. Translation: AAH06992.1. BC016330 mRNA. Translation: AAH16330.1. |
| IPI | IPI00093253. IPI00396551. IPI00607574. |
| RefSeq | NP_001124334.1. NM_001130862.1. NP_006470.1. NM_006479.4. |
| UniGene | Hs.504550. |
3D structure databases | |
| ProteinModelPortal | Q96B01. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-35257N. |
| IntAct | Q96B01. 7 interactions. |
| STRING | Q96B01. |
PTM databases | |
| PhosphoSite | Q96B01. |
Polymorphism databases | |
| DMDM | 68565925. |
Proteomic databases | |
| PRIDE | Q96B01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000228843; ENSP00000228843; ENSG00000111247. |
| GeneID | 10635. |
| KEGG | hsa:10635. |
| UCSC | uc001qmu.1. human. uc001qmw.1. human. |
Organism-specific databases | |
| CTD | 10635. |
| GeneCards | GC12P004647. |
| H-InvDB | HIX0010349. |
| HGNC | HGNC:16956. RAD51AP1. |
| MIM | 603070. gene. |
| neXtProt | NX_Q96B01. |
| PharmGKB | PA134871784. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG17266. |
| GeneTree | ENSGT00530000063784. |
| HOGENOM | HBG283205. |
| HOVERGEN | HBG079699. |
| InParanoid | Q96B01. |
| OMA | DSEPDFA. |
| PhylomeDB | Q96B01. |
Gene expression databases | |
| ArrayExpress | Q96B01. |
| Bgee | Q96B01. |
| CleanEx | HS_RAD51AP1. |
| Genevestigator | Q96B01. |
| GermOnline | ENSG00000111247. Homo sapiens. |
Family and domain databases | |
| ProtoNet | Search... |
Other | |
| NextBio | 40421. |
| SOURCE | Search... |
Entry information
| Entry name | R51A1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96B01 Secondary accession number(s): A8K7D3, O43403, Q7Z779 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |

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