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RAD9B_HUMAN
ID   RAD9B_HUMAN             Reviewed;         426 AA.
AC   Q6WBX8; Q5U5K0; Q6NVJ1; Q6ZVT7; Q8N7T9; Q96LI8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Cell cycle checkpoint control protein RAD9B;
DE   AltName: Full=DNA repair exonuclease rad9 homolog B;
DE            Short=hRAD9B;
GN   Name=RAD9B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HUS1; HUS1B; RAD1
RP   AND RAD9A, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=14500360;
RA   Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B.;
RT   "Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control
RT   genes in normal and cancerous testicular tissue.";
RL   Cancer Res. 63:5291-5298(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH HUS1; HUS1B; RAD1 AND RAD17, AND TISSUE SPECIFICITY.
RX   PubMed=14611806; DOI=10.1016/s0888-7543(03)00200-3;
RA   Dufault V.M., Oestreich A.J., Vroman B.T., Karnitz L.M.;
RT   "Identification and characterization of RAD9B, a paralog of the RAD9
RT   checkpoint gene.";
RL   Genomics 82:644-651(2003).
CC   -!- SUBUNIT: Interacts with HUS1, HUS1B, RAD1, RAD9A and RAD17.
CC       {ECO:0000269|PubMed:14500360, ECO:0000269|PubMed:14611806}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=5;
CC         IsoId=Q6WBX8-5; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q6WBX8-1; Sequence=VSP_017446;
CC       Name=2;
CC         IsoId=Q6WBX8-2; Sequence=VSP_017445, VSP_017446;
CC       Name=3;
CC         IsoId=Q6WBX8-3; Sequence=VSP_017444, VSP_017446;
CC       Name=4;
CC         IsoId=Q6WBX8-4; Sequence=VSP_017444;
CC   -!- TISSUE SPECIFICITY: Expressed in testis and skeletal muscle.
CC       {ECO:0000269|PubMed:14500360, ECO:0000269|PubMed:14611806}.
CC   -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000305}.
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DR   EMBL; AY297459; AAQ62859.1; -; mRNA.
DR   EMBL; AK058176; BAB71704.1; -; mRNA.
DR   EMBL; AK097665; BAC05138.1; -; mRNA.
DR   EMBL; AK124109; BAC85774.1; -; mRNA.
DR   EMBL; AC002350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047645; AAH47645.1; -; mRNA.
DR   EMBL; BC068031; AAH68031.2; -; mRNA.
DR   CCDS; CCDS73527.1; -. [Q6WBX8-2]
DR   RefSeq; NP_001273460.1; NM_001286531.1. [Q6WBX8-2]
DR   RefSeq; NP_001273461.1; NM_001286532.1. [Q6WBX8-2]
DR   RefSeq; NP_001273462.1; NM_001286533.1. [Q6WBX8-3]
DR   RefSeq; NP_001273463.1; NM_001286534.1. [Q6WBX8-3]
DR   RefSeq; NP_001273464.1; NM_001286535.1.
DR   RefSeq; NP_001273465.1; NM_001286536.1.
DR   RefSeq; NP_689655.3; NM_152442.3.
DR   RefSeq; XP_011536276.1; XM_011537974.2.
DR   RefSeq; XP_016874367.1; XM_017018878.1.
DR   RefSeq; XP_016874371.1; XM_017018882.1. [Q6WBX8-3]
DR   AlphaFoldDB; Q6WBX8; -.
DR   SMR; Q6WBX8; -.
DR   BioGRID; 126872; 10.
DR   CORUM; Q6WBX8; -.
DR   STRING; 9606.ENSP00000376440; -.
DR   iPTMnet; Q6WBX8; -.
DR   PhosphoSitePlus; Q6WBX8; -.
DR   BioMuta; RAD9B; -.
DR   MassIVE; Q6WBX8; -.
DR   PaxDb; Q6WBX8; -.
DR   PeptideAtlas; Q6WBX8; -.
DR   PRIDE; Q6WBX8; -.
DR   ProteomicsDB; 67754; -. [Q6WBX8-5]
DR   ProteomicsDB; 67755; -. [Q6WBX8-1]
DR   ProteomicsDB; 67756; -. [Q6WBX8-2]
DR   ProteomicsDB; 67757; -. [Q6WBX8-3]
DR   ProteomicsDB; 67758; -. [Q6WBX8-4]
DR   Antibodypedia; 31019; 87 antibodies from 20 providers.
DR   DNASU; 144715; -.
DR   Ensembl; ENST00000409246.5; ENSP00000387329.1; ENSG00000151164.19. [Q6WBX8-2]
DR   Ensembl; ENST00000409425.5; ENSP00000386629.1; ENSG00000151164.19. [Q6WBX8-2]
DR   GeneID; 144715; -.
DR   KEGG; hsa:144715; -.
DR   UCSC; uc001tre.6; human. [Q6WBX8-5]
DR   CTD; 144715; -.
DR   DisGeNET; 144715; -.
DR   GeneCards; RAD9B; -.
DR   HGNC; HGNC:21700; RAD9B.
DR   HPA; ENSG00000151164; Tissue enriched (testis).
DR   MalaCards; RAD9B; -.
DR   MIM; 608368; gene.
DR   neXtProt; NX_Q6WBX8; -.
DR   OpenTargets; ENSG00000151164; -.
DR   PharmGKB; PA134889252; -.
DR   VEuPathDB; HostDB:ENSG00000151164; -.
DR   eggNOG; KOG2810; Eukaryota.
DR   GeneTree; ENSGT00390000005767; -.
DR   InParanoid; Q6WBX8; -.
DR   OMA; HTKIWSE; -.
DR   OrthoDB; 1176140at2759; -.
DR   PhylomeDB; Q6WBX8; -.
DR   PathwayCommons; Q6WBX8; -.
DR   Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR   SignaLink; Q6WBX8; -.
DR   BioGRID-ORCS; 144715; 41 hits in 1081 CRISPR screens.
DR   ChiTaRS; RAD9B; human.
DR   GenomeRNAi; 144715; -.
DR   Pharos; Q6WBX8; Tdark.
DR   PRO; PR:Q6WBX8; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q6WBX8; protein.
DR   Bgee; ENSG00000151164; Expressed in right testis and 100 other tissues.
DR   ExpressionAtlas; Q6WBX8; baseline and differential.
DR   Genevisible; Q6WBX8; HS.
DR   GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR   InterPro; IPR026584; Rad9.
DR   InterPro; IPR007268; Rad9/Ddc1.
DR   PANTHER; PTHR15237; PTHR15237; 1.
DR   Pfam; PF04139; Rad9; 1.
DR   PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Cell cycle checkpoint control protein RAD9B"
FT                   /id="PRO_0000226698"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6WBX7"
FT   VAR_SEQ         1..155
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017444"
FT   VAR_SEQ         1..69
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_017445"
FT   VAR_SEQ         409..426
FT                   /note="VCCRKEFNGSDAKYFCII -> GSFSIF (in isoform 1, isoform
FT                   2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14500360,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017446"
FT   CONFLICT        226
FT                   /note="C -> Y (in Ref. 2; BAC05138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="D -> G (in Ref. 2; BAB71704)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  47832 MW;  876E5F8E8F259A03 CRC64;
     MLKCVMSGSQ VKVFGKAVQA LSRISDEFWL DPSKKGLALR CVNSSRSAYG CVLFSPVFFQ
     HYQWSALVKM SENELDTTLH LKCKLGMKSI LPIFRCLNSL ERNIEKCRIF TRSDKCKVVI
     QFFYRHGIKR THNICFQESQ PLQVIFDKNV CTNTLMIQPR LLADAIVLFT SSQEEVTLAV
     TPLNFCLKSS NEESMDLSNA VHSEMFVGSD EFDFFQIGMD TEITFCFKEL KGILTFSEAT
     HAPISIYFDF PGKPLALSID DMLVEANFIL ATLADEQSRA SSPQSLCLSQ KRKRSDLIEK
     KAGKNVTGQA LECISKKAAP RRLYPKETLT NISALENCGS PAMKRVDGDV SEVSESSVSN
     TEEVPGSLCL RKFSCMFFGA VSSDQQEHFN HPFDSLARAS DSEEDMNNVC CRKEFNGSDA
     KYFCII
 
 
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