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RUN3A_HUMAN
ID   RUN3A_HUMAN             Reviewed;         446 AA.
AC   Q59EK9; B2R974; O15483; O60651; Q7Z3S2; Q9UF50;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=RUN domain-containing protein 3A;
DE   AltName: Full=Rap2-interacting protein 8;
DE            Short=RPIP-8;
GN   Name=RUNDC3A; Synonyms=RAP2IP, RPIP8;
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 2), AND IDENTIFICATION (ISOFORM 1).
RX   PubMed=9523700; DOI=10.1046/j.1432-1327.1998.2520290.x;
RA   Janoueix-Lerosey I., Pasheva E., de Tand M.-F., Tavitian A.,
RA   de Gunzburg J.;
RT   "Identification of a specific effector of the small GTP-binding protein
RT   Rap2.";
RL   Eur. J. Biochem. 252:290-298(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Caudate nucleus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   TISSUE=Cerebellum, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Lung;
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).
CC   -!- FUNCTION: May act as an effector of RAP2A in neuronal cells.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the GTP-bound form of RAP2A. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q59EK9; Q9BXS5: AP1M1; NbExp=4; IntAct=EBI-747225, EBI-541426;
CC       Q59EK9; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-747225, EBI-742909;
CC       Q59EK9; Q96S94: CCNL2; NbExp=3; IntAct=EBI-747225, EBI-1045974;
CC       Q59EK9; P26196: DDX6; NbExp=3; IntAct=EBI-747225, EBI-351257;
CC       Q59EK9; P60228: EIF3E; NbExp=4; IntAct=EBI-747225, EBI-347740;
CC       Q59EK9; Q3B820: FAM161A; NbExp=3; IntAct=EBI-747225, EBI-719941;
CC       Q59EK9; P55040: GEM; NbExp=3; IntAct=EBI-747225, EBI-744104;
CC       Q59EK9; O15481: MAGEB4; NbExp=3; IntAct=EBI-747225, EBI-751857;
CC       Q59EK9; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-747225, EBI-746778;
CC       Q59EK9; Q9P015: MRPL15; NbExp=3; IntAct=EBI-747225, EBI-2371967;
CC       Q59EK9; P61225: RAP2B; NbExp=4; IntAct=EBI-747225, EBI-750871;
CC       Q59EK9; O00560: SDCBP; NbExp=3; IntAct=EBI-747225, EBI-727004;
CC       Q59EK9; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-747225, EBI-745392;
CC       Q59EK9; Q05BL0: TBRG1; NbExp=3; IntAct=EBI-747225, EBI-10223693;
CC       Q59EK9; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-747225, EBI-10178002;
CC       Q59EK9; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-747225, EBI-740727;
CC       Q59EK9; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-747225, EBI-6427977;
CC       Q59EK9; Q9H614; NbExp=3; IntAct=EBI-747225, EBI-10249899;
CC       Q59EK9-3; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-11957366, EBI-541426;
CC       Q59EK9-3; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-11957366, EBI-742909;
CC       Q59EK9-3; Q96S94-5: CCNL2; NbExp=3; IntAct=EBI-11957366, EBI-12024864;
CC       Q59EK9-3; P60228: EIF3E; NbExp=3; IntAct=EBI-11957366, EBI-347740;
CC       Q59EK9-3; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-11957366, EBI-744099;
CC       Q59EK9-3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11957366, EBI-739832;
CC       Q59EK9-3; O15481: MAGEB4; NbExp=3; IntAct=EBI-11957366, EBI-751857;
CC       Q59EK9-3; Q8NHZ7: MBD3L2; NbExp=3; IntAct=EBI-11957366, EBI-11989378;
CC       Q59EK9-3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-11957366, EBI-1567797;
CC       Q59EK9-3; P10114: RAP2A; NbExp=3; IntAct=EBI-11957366, EBI-602366;
CC       Q59EK9-3; P61225: RAP2B; NbExp=3; IntAct=EBI-11957366, EBI-750871;
CC       Q59EK9-3; O00560: SDCBP; NbExp=3; IntAct=EBI-11957366, EBI-727004;
CC       Q59EK9-3; A0A0S2Z4F2: TEAD4; NbExp=3; IntAct=EBI-11957366, EBI-16429215;
CC       Q59EK9-3; Q15561: TEAD4; NbExp=3; IntAct=EBI-11957366, EBI-747736;
CC       Q59EK9-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-11957366, EBI-10241197;
CC       Q59EK9-3; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-11957366, EBI-17208936;
CC       Q59EK9-3; O75604: USP2; NbExp=3; IntAct=EBI-11957366, EBI-743272;
CC       Q59EK9-3; P15622-3: ZNF250; NbExp=3; IntAct=EBI-11957366, EBI-10177272;
CC       Q59EK9-3; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-11957366, EBI-740727;
CC       Q59EK9-3; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-11957366, EBI-6427977;
CC       Q59EK9-3; O75541-2: ZNF821; NbExp=3; IntAct=EBI-11957366, EBI-14544035;
CC       Q59EK9-3; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-11957366, EBI-5667516;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q59EK9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q59EK9-2; Sequence=VSP_032153, VSP_032155, VSP_032156;
CC       Name=3;
CC         IsoId=Q59EK9-3; Sequence=VSP_032155, VSP_032156;
CC       Name=4;
CC         IsoId=Q59EK9-4; Sequence=VSP_032154;
CC   -!- SIMILARITY: Belongs to the RUNDC3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD93039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U93871; AAB68767.1; -; mRNA.
DR   EMBL; AF055026; AAC09366.1; -; mRNA.
DR   EMBL; AK313669; BAG36421.1; -; mRNA.
DR   EMBL; CR456748; CAG33029.1; -; mRNA.
DR   EMBL; AB209802; BAD93039.1; ALT_INIT; mRNA.
DR   EMBL; BX537443; CAD97685.1; -; mRNA.
DR   EMBL; AL133657; CAB63771.1; -; mRNA.
DR   EMBL; CH471178; EAW51609.1; -; Genomic_DNA.
DR   EMBL; CH471178; EAW51610.1; -; Genomic_DNA.
DR   EMBL; BC006194; AAH06194.1; -; mRNA.
DR   CCDS; CCDS45698.1; -. [Q59EK9-1]
DR   CCDS; CCDS45699.1; -. [Q59EK9-3]
DR   CCDS; CCDS59294.1; -. [Q59EK9-2]
DR   RefSeq; NP_001138297.1; NM_001144825.1. [Q59EK9-1]
DR   RefSeq; NP_001138298.1; NM_001144826.1. [Q59EK9-2]
DR   RefSeq; NP_006686.1; NM_006695.4. [Q59EK9-3]
DR   AlphaFoldDB; Q59EK9; -.
DR   SMR; Q59EK9; -.
DR   BioGRID; 116106; 61.
DR   IntAct; Q59EK9; 57.
DR   MINT; Q59EK9; -.
DR   STRING; 9606.ENSP00000410862; -.
DR   iPTMnet; Q59EK9; -.
DR   PhosphoSitePlus; Q59EK9; -.
DR   BioMuta; RUNDC3A; -.
DR   DMDM; 172045944; -.
DR   jPOST; Q59EK9; -.
DR   MassIVE; Q59EK9; -.
DR   PaxDb; Q59EK9; -.
DR   PeptideAtlas; Q59EK9; -.
DR   PRIDE; Q59EK9; -.
DR   ProteomicsDB; 62634; -. [Q59EK9-1]
DR   ProteomicsDB; 62635; -. [Q59EK9-2]
DR   ProteomicsDB; 62636; -. [Q59EK9-3]
DR   ProteomicsDB; 62637; -. [Q59EK9-4]
DR   Antibodypedia; 8218; 220 antibodies from 24 providers.
DR   DNASU; 10900; -.
DR   Ensembl; ENST00000225441.11; ENSP00000225441.7; ENSG00000108309.14. [Q59EK9-3]
DR   Ensembl; ENST00000426726.8; ENSP00000410862.2; ENSG00000108309.14. [Q59EK9-1]
DR   Ensembl; ENST00000590941.5; ENSP00000468214.1; ENSG00000108309.14. [Q59EK9-2]
DR   GeneID; 10900; -.
DR   KEGG; hsa:10900; -.
DR   MANE-Select; ENST00000426726.8; ENSP00000410862.2; NM_001144825.2; NP_001138297.1.
DR   UCSC; uc002igi.4; human. [Q59EK9-1]
DR   CTD; 10900; -.
DR   DisGeNET; 10900; -.
DR   GeneCards; RUNDC3A; -.
DR   HGNC; HGNC:16984; RUNDC3A.
DR   HPA; ENSG00000108309; Tissue enhanced (brain, choroid plexus, pituitary gland).
DR   MIM; 605448; gene.
DR   neXtProt; NX_Q59EK9; -.
DR   OpenTargets; ENSG00000108309; -.
DR   PharmGKB; PA162402277; -.
DR   VEuPathDB; HostDB:ENSG00000108309; -.
DR   eggNOG; KOG4381; Eukaryota.
DR   GeneTree; ENSGT00940000158922; -.
DR   HOGENOM; CLU_045987_0_0_1; -.
DR   InParanoid; Q59EK9; -.
DR   OMA; MSEYIAT; -.
DR   OrthoDB; 714315at2759; -.
DR   PhylomeDB; Q59EK9; -.
DR   TreeFam; TF323904; -.
DR   PathwayCommons; Q59EK9; -.
DR   SignaLink; Q59EK9; -.
DR   BioGRID-ORCS; 10900; 15 hits in 1059 CRISPR screens.
DR   ChiTaRS; RUNDC3A; human.
DR   GeneWiki; RUNDC3A; -.
DR   GenomeRNAi; 10900; -.
DR   Pharos; Q59EK9; Tdark.
DR   PRO; PR:Q59EK9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q59EK9; protein.
DR   Bgee; ENSG00000108309; Expressed in right frontal lobe and 160 other tissues.
DR   Genevisible; Q59EK9; HS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0030695; F:GTPase regulator activity; TAS:ProtInc.
DR   GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR   Gene3D; 1.20.58.900; -; 1.
DR   InterPro; IPR004012; Run_dom.
DR   InterPro; IPR037213; Run_dom_sf.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00593; RUN; 1.
DR   SUPFAM; SSF140741; SSF140741; 1.
DR   PROSITE; PS50826; RUN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome.
FT   CHAIN           1..446
FT                   /note="RUN domain-containing protein 3A"
FT                   /id="PRO_0000324155"
FT   DOMAIN          52..189
FT                   /note="RUN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT   REGION          1..298
FT                   /note="Interaction with RAP2A"
FT                   /evidence="ECO:0000250"
FT   REGION          216..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          267..322
FT                   /evidence="ECO:0000255"
FT   MOD_RES         215
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O08576"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08576"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08576"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08576"
FT   VAR_SEQ         75..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9523700"
FT                   /id="VSP_032153"
FT   VAR_SEQ         365..446
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_032154"
FT   VAR_SEQ         401..405
FT                   /note="KDPTP -> SSEPN (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9523700, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_032155"
FT   VAR_SEQ         406..446
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9523700, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_032156"
FT   CONFLICT        134
FT                   /note="M -> V (in Ref. 6; CAD97685)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   446 AA;  49747 MW;  2C753EA8619B1024 CRC64;
     MEASFVQTTM ALGLSSKKAS SRNVAVERKN LITVCRFSVK TLLEKYTAEP IDDSSEEFVN
     FAAILEQILS HRFKACAPAG PVSWFSSDGQ RGFWDYIRLA CSKVPNNCVS SIENMENIST
     ARAKGRAWIR VALMEKRMSE YITTALRDTR TTRRFYDSGA IMLRDEATIL TGMLIGLSAI
     DFSFCLKGEV LDGKTPVVID YTPYLKFTQS YDYLTDEEER HSAESSTSED NSPEHPYLPL
     VTDEDSWYSK WHKMEQKFRI VYAQKGYLEE LVRLRESQLK DLEAENRRLQ LQLEEAAAQN
     QREKRELEGV ILELQEQLTG LIPSDHAPLA QGSKELTTPL VNQWPSLGTL NGAEGASNSK
     LYRRHSFMST EPLSAEASLS SDSQRLGEGT RDEEPWGPIG KDPTPSMLGL CGSLASIPSC
     KSLASFKSNE CLVSDSPEGS PALSPS
 
 
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