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RITA1_HUMAN
ID   RITA1_HUMAN             Reviewed;         269 AA.
AC   Q96K30; B3KVZ4; C9JIN1; F8VRG5; Q53GM3; Q96K25;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=RBPJ-interacting and tubulin-associated protein 1;
DE   AltName: Full=RBPJ-interacting and tubulin-associated protein;
GN   Name=RITA1; Synonyms=C12orf52, RITA; ORFNames=PSEC0043;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Neuroblastoma, Ovary, and Teratocarcinoma;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 1).
RC   TISSUE=Ovary;
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   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBPJ, TUBULIN-BINDING, AND
RP   MUTAGENESIS OF LEU-7; MET-12; LEU-15 AND 95-ARG--LYS-97.
RX   PubMed=21102556; DOI=10.1038/emboj.2010.289;
RA   Wacker S.A., Alvarado C., von Wichert G., Knippschild U., Wiedenmann J.,
RA   Clauss K., Nienhaus G.U., Hameister H., Baumann B., Borggrefe T.,
RA   Knochel W., Oswald F.;
RT   "RITA, a novel modulator of Notch signalling, acts via nuclear export of
RT   RBP-J.";
RL   EMBO J. 30:43-56(2011).
CC   -!- FUNCTION: Tubulin-binding protein that acts as a negative regulator of
CC       Notch signaling pathway. Shuttles between the cytoplasm and the nucleus
CC       and mediates the nuclear export of RBPJ/RBPSUH, thereby preventing the
CC       interaction between RBPJ/RBPSUH and NICD product of Notch proteins
CC       (Notch intracellular domain), leading to down-regulate Notch-mediated
CC       transcription. May play a role in neurogenesis.
CC       {ECO:0000269|PubMed:21102556}.
CC   -!- SUBUNIT: Interacts with RBPJ/RBPSUH. {ECO:0000269|PubMed:21102556}.
CC   -!- INTERACTION:
CC       Q96K30; Q9NPI6: DCP1A; NbExp=4; IntAct=EBI-2836148, EBI-374238;
CC       Q96K30; Q08379: GOLGA2; NbExp=4; IntAct=EBI-2836148, EBI-618309;
CC       Q96K30; Q06330: RBPJ; NbExp=10; IntAct=EBI-2836148, EBI-632552;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21102556}. Nucleus
CC       {ECO:0000269|PubMed:21102556}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:21102556}.
CC       Note=Shuttles rapidly between the cytoplasm and the nucleus. The
CC       function of centrosome localization is still unclear.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96K30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96K30-2; Sequence=VSP_026636, VSP_026637;
CC       Name=3;
CC         IsoId=Q96K30-3; Sequence=VSP_055649;
CC   -!- SIMILARITY: Belongs to the RITA family. {ECO:0000305}.
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DR   EMBL; AK075358; BAC11568.1; -; mRNA.
DR   EMBL; AK027733; BAB55328.1; -; mRNA.
DR   EMBL; AK027741; BAB55333.1; -; mRNA.
DR   EMBL; AK123762; BAG53956.1; -; mRNA.
DR   EMBL; AK222908; BAD96628.1; -; mRNA.
DR   EMBL; AC089999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC022092; AAH22092.1; -; mRNA.
DR   CCDS; CCDS66473.1; -. [Q96K30-3]
DR   CCDS; CCDS9166.1; -. [Q96K30-1]
DR   RefSeq; NP_001273144.1; NM_001286215.1. [Q96K30-3]
DR   RefSeq; NP_116237.1; NM_032848.2. [Q96K30-1]
DR   RefSeq; XP_005254029.1; XM_005253972.2. [Q96K30-1]
DR   PDB; 5EG6; X-ray; 2.09 A; R=133-148.
DR   PDBsum; 5EG6; -.
DR   AlphaFoldDB; Q96K30; -.
DR   SMR; Q96K30; -.
DR   BioGRID; 124368; 14.
DR   IntAct; Q96K30; 11.
DR   MINT; Q96K30; -.
DR   STRING; 9606.ENSP00000448680; -.
DR   iPTMnet; Q96K30; -.
DR   PhosphoSitePlus; Q96K30; -.
DR   BioMuta; RITA1; -.
DR   MassIVE; Q96K30; -.
DR   PaxDb; Q96K30; -.
DR   PeptideAtlas; Q96K30; -.
DR   PRIDE; Q96K30; -.
DR   ProteomicsDB; 28435; -.
DR   Antibodypedia; 51448; 90 antibodies from 14 providers.
DR   DNASU; 84934; -.
DR   Ensembl; ENST00000548278.2; ENSP00000449841.1; ENSG00000139405.16. [Q96K30-1]
DR   Ensembl; ENST00000549621.5; ENSP00000448289.1; ENSG00000139405.16. [Q96K30-1]
DR   Ensembl; ENST00000552495.1; ENSP00000448680.1; ENSG00000139405.16. [Q96K30-3]
DR   GeneID; 84934; -.
DR   KEGG; hsa:84934; -.
DR   MANE-Select; ENST00000548278.2; ENSP00000449841.1; NM_032848.3; NP_116237.1.
DR   UCSC; uc001tur.2; human. [Q96K30-1]
DR   CTD; 84934; -.
DR   DisGeNET; 84934; -.
DR   GeneCards; RITA1; -.
DR   HGNC; HGNC:25925; RITA1.
DR   HPA; ENSG00000139405; Low tissue specificity.
DR   neXtProt; NX_Q96K30; -.
DR   OpenTargets; ENSG00000139405; -.
DR   PharmGKB; PA143485381; -.
DR   VEuPathDB; HostDB:ENSG00000139405; -.
DR   eggNOG; ENOG502S61Y; Eukaryota.
DR   GeneTree; ENSGT00390000013005; -.
DR   HOGENOM; CLU_062251_0_0_1; -.
DR   InParanoid; Q96K30; -.
DR   OrthoDB; 1387213at2759; -.
DR   PhylomeDB; Q96K30; -.
DR   TreeFam; TF337291; -.
DR   PathwayCommons; Q96K30; -.
DR   SignaLink; Q96K30; -.
DR   SIGNOR; Q96K30; -.
DR   BioGRID-ORCS; 84934; 33 hits in 1076 CRISPR screens.
DR   ChiTaRS; RITA1; human.
DR   GenomeRNAi; 84934; -.
DR   Pharos; Q96K30; Tbio.
DR   PRO; PR:Q96K30; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q96K30; protein.
DR   Bgee; ENSG00000139405; Expressed in left adrenal gland cortex and 172 other tissues.
DR   ExpressionAtlas; Q96K30; baseline and differential.
DR   Genevisible; Q96K30; HS.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0051168; P:nuclear export; IDA:UniProtKB.
DR   InterPro; IPR031418; RITA1.
DR   PANTHER; PTHR34917; PTHR34917; 1.
DR   Pfam; PF17066; RITA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Neurogenesis;
KW   Notch signaling pathway; Nucleus; Reference proteome.
FT   CHAIN           1..269
FT                   /note="RBPJ-interacting and tubulin-associated protein 1"
FT                   /id="PRO_0000294429"
FT   REGION          66..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..156
FT                   /note="Interaction with RBPJ/RBPSUH"
FT                   /evidence="ECO:0000269|PubMed:21102556"
FT   REGION          141..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..269
FT                   /note="Interaction with tubulin"
FT   MOTIF           5..17
FT                   /note="Nuclear export signal"
FT   MOTIF           92..108
FT                   /note="Nuclear localization signal"
FT   COMPBIAS        81..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1
FT                   /note="M -> MLREPRKQGLAGRAHLLSPGTTGSM (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_055649"
FT   VAR_SEQ         161..177
FT                   /note="LRAIHPAGPSKTEPGPA -> VPPTQMGLRISGLPRQG (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026636"
FT   VAR_SEQ         178..269
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026637"
FT   VARIANT         113
FT                   /note="S -> W (in dbSNP:rs16942601)"
FT                   /id="VAR_050865"
FT   VARIANT         220
FT                   /note="T -> K (in dbSNP:rs34831139)"
FT                   /id="VAR_033175"
FT   MUTAGEN         7
FT                   /note="L->A: Results in nuclear accumulation; when
FT                   associated with A-12 and A-15."
FT                   /evidence="ECO:0000269|PubMed:21102556"
FT   MUTAGEN         12
FT                   /note="M->A: Results in nuclear accumulation; when
FT                   associated with A-7 and A-15."
FT                   /evidence="ECO:0000269|PubMed:21102556"
FT   MUTAGEN         15
FT                   /note="L->A: Results in nuclear accumulation; when
FT                   associated with A-7 and A-12."
FT                   /evidence="ECO:0000269|PubMed:21102556"
FT   MUTAGEN         95..97
FT                   /note="RKK->AAA: Abolishes nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:21102556"
FT   CONFLICT        73
FT                   /note="A -> S (in Ref. 1; BAG53956)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="A -> V (in Ref. 2; BAD96628)"
FT                   /evidence="ECO:0000305"
FT   STRAND          135..138
FT                   /evidence="ECO:0007829|PDB:5EG6"
SQ   SEQUENCE   269 AA;  28619 MW;  3F053E1454F60773 CRC64;
     MKTPVELAVS GMQTLGLQHR CRGGYRVKAR TSYVDETLFG SPAGTRPTPP DFDPPWVEKA
     NRTRGVGKEA SKALGAKGSC ETTPSRGSTP TLTPRKKNKY RPISHTPSYC DESLFGSRSE
     GASFGAPRMA KGDAAKLRAL LWTPPPTPRG SHSPRPREAP LRAIHPAGPS KTEPGPAADS
     QKLSMGGLHS SRPLKRGLSH SLTHLNVPST GHPATSAPHT NGPQDLRPST SGVTFRSPLV
     TSRARSVSIS VPSTPRRGGA TQKPKPPWK
 
 
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