RUSC1_HUMAN
ID RUSC1_HUMAN Reviewed; 902 AA.
AC Q9BVN2; B3KWM9; Q5T9U9; Q5T9V0; Q5T9V1; Q5T9V2; Q9UPY4; Q9Y4T5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=AP-4 complex accessory subunit RUSC1 {ECO:0000305};
DE AltName: Full=New molecule containing SH3 at the carboxy-terminus {ECO:0000303|PubMed:19365808};
DE Short=Nesca {ECO:0000303|PubMed:19365808};
DE AltName: Full=RUN and SH3 domain-containing protein 1;
GN Name=RUSC1 {ECO:0000303|PubMed:30262884, ECO:0000312|HGNC:HGNC:17153};
GN Synonyms=NESCA {ECO:0000303|PubMed:19365808};
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).
RX PubMed=10760598; DOI=10.1016/s0167-4781(00)00049-x;
RA Matsuda S., Miyazaki K., Ichigotani Y., Kurata H., Takenouchi Y.,
RA Yamamoto T., Nimura Y., Irimura T., Nakatsugawa S., Hamaguchi M.;
RT "Molecular cloning and characterization of a novel human gene (NESCA) which
RT encodes a putative adapter protein containing SH3.";
RL Biochim. Biophys. Acta 1491:321-326(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
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 MRNA] (ISOFORM 2).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Endometrium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Lung, and Placenta;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP LEU-531.
RX PubMed=15024033; DOI=10.1083/jcb.200309081;
RA MacDonald J.I.S., Kubu C.J., Meakin S.O.;
RT "Nesca, a novel adapter, translocates to the nuclear envelope and regulates
RT neurotrophin-induced neurite outgrowth.";
RL J. Cell Biol. 164:851-862(2004).
RN [9]
RP FUNCTION, INTERACTION WITH IKBKG AND TRAF6, AND UBIQUITINATION.
RX PubMed=19365808; DOI=10.1002/jcp.21782;
RA Napolitano G., Mirra S., Monfregola J., Lavorgna A., Leonardi A.,
RA Ursini M.V.;
RT "NESCA: a new NEMO/IKKgamma and TRAF6 interacting protein.";
RL J. Cell. Physiol. 220:410-417(2009).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE AP-4 COMPLEX.
RX PubMed=30262884; DOI=10.1038/s41467-018-06172-7;
RA Davies A.K., Itzhak D.N., Edgar J.R., Archuleta T.L., Hirst J.,
RA Jackson L.P., Robinson M.S., Borner G.H.H.;
RT "AP-4 vesicles contribute to spatial control of autophagy via RUSC-
RT dependent peripheral delivery of ATG9A.";
RL Nat. Commun. 9:3958-3958(2018).
CC -!- FUNCTION: Associates with the adapter-like complex 4 (AP-4) and may
CC therefore play a role in vesicular trafficking of proteins at the
CC trans-Golgi network (PubMed:30262884). Signaling adapter which plays a
CC role in neuronal differentiation (PubMed:15024033). Involved in
CC regulation of NGF-dependent neurite outgrowth (PubMed:15024033). May
CC play a role in neuronal vesicular trafficking, specifically involving
CC pre-synaptic membrane proteins (By similarity). Seems to be involved in
CC signaling pathways that are regulated by the prolonged activation of
CC MAPK (PubMed:15024033). Can regulate the polyubiquitination of IKBKG
CC and thus may be involved in regulation of the NF-kappa-B pathway
CC (PubMed:19365808). {ECO:0000250|UniProtKB:Q8BG26,
CC ECO:0000269|PubMed:15024033, ECO:0000269|PubMed:19365808,
CC ECO:0000269|PubMed:30262884}.
CC -!- SUBUNIT: Associated component of the adapter-like complex 4 (AP-4)
CC (PubMed:30262884). Interacts with IKBKG and TRAF6 (PubMed:19365808).
CC Interacts with F-actin, acetylated actin, TUBB3, STX1A, KIF5B and KLC1
CC (By similarity). {ECO:0000250|UniProtKB:Q8BG26,
CC ECO:0000269|PubMed:19365808, ECO:0000269|PubMed:30262884}.
CC -!- INTERACTION:
CC Q9BVN2; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-6257312, EBI-12318443;
CC Q9BVN2; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-6257312, EBI-2813554;
CC Q9BVN2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-6257312, EBI-11096309;
CC Q9BVN2; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-6257312, EBI-357530;
CC Q9BVN2; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-6257312, EBI-11954519;
CC Q9BVN2; Q8N8Y2: ATP6V0D2; NbExp=3; IntAct=EBI-6257312, EBI-3923949;
CC Q9BVN2; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-6257312, EBI-953896;
CC Q9BVN2; Q9NX04: C1orf109; NbExp=5; IntAct=EBI-6257312, EBI-8643161;
CC Q9BVN2; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-6257312, EBI-744556;
CC Q9BVN2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-6257312, EBI-10961624;
CC Q9BVN2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-6257312, EBI-10175300;
CC Q9BVN2; P24863: CCNC; NbExp=3; IntAct=EBI-6257312, EBI-395261;
CC Q9BVN2; P42772: CDKN2B; NbExp=3; IntAct=EBI-6257312, EBI-711280;
CC Q9BVN2; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-6257312, EBI-1054315;
CC Q9BVN2; Q03060-25: CREM; NbExp=3; IntAct=EBI-6257312, EBI-12884642;
CC Q9BVN2; P53672: CRYBA2; NbExp=3; IntAct=EBI-6257312, EBI-750444;
CC Q9BVN2; P78358: CTAG1B; NbExp=3; IntAct=EBI-6257312, EBI-1188472;
CC Q9BVN2; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-6257312, EBI-9679045;
CC Q9BVN2; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-6257312, EBI-2880244;
CC Q9BVN2; Q01658: DR1; NbExp=3; IntAct=EBI-6257312, EBI-750300;
CC Q9BVN2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-6257312, EBI-740376;
CC Q9BVN2; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-6257312, EBI-742102;
CC Q9BVN2; Q96B26: EXOSC8; NbExp=6; IntAct=EBI-6257312, EBI-371922;
CC Q9BVN2; Q8IZU0: FAM9B; NbExp=5; IntAct=EBI-6257312, EBI-10175124;
CC Q9BVN2; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-6257312, EBI-10242151;
CC Q9BVN2; O75603: GCM2; NbExp=3; IntAct=EBI-6257312, EBI-10188645;
CC Q9BVN2; Q00403: GTF2B; NbExp=3; IntAct=EBI-6257312, EBI-389564;
CC Q9BVN2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-6257312, EBI-1054873;
CC Q9BVN2; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-6257312, EBI-740641;
CC Q9BVN2; P52597: HNRNPF; NbExp=3; IntAct=EBI-6257312, EBI-352986;
CC Q9BVN2; Q1MX18: INSC; NbExp=3; IntAct=EBI-6257312, EBI-12081118;
CC Q9BVN2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-6257312, EBI-4397613;
CC Q9BVN2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-6257312, EBI-12811111;
CC Q9BVN2; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-6257312, EBI-1048945;
CC Q9BVN2; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-6257312, EBI-11962084;
CC Q9BVN2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-6257312, EBI-10261141;
CC Q9BVN2; P0CW20: LIMS4; NbExp=3; IntAct=EBI-6257312, EBI-10196832;
CC Q9BVN2; P25791-3: LMO2; NbExp=3; IntAct=EBI-6257312, EBI-11959475;
CC Q9BVN2; P43357: MAGEA3; NbExp=3; IntAct=EBI-6257312, EBI-5651459;
CC Q9BVN2; P43360: MAGEA6; NbExp=3; IntAct=EBI-6257312, EBI-1045155;
CC Q9BVN2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-6257312, EBI-716006;
CC Q9BVN2; Q71SY5: MED25; NbExp=3; IntAct=EBI-6257312, EBI-394558;
CC Q9BVN2; O14770-4: MEIS2; NbExp=3; IntAct=EBI-6257312, EBI-8025850;
CC Q9BVN2; Q8IVT2: MISP; NbExp=3; IntAct=EBI-6257312, EBI-2555085;
CC Q9BVN2; Q96BY2: MOAP1; NbExp=3; IntAct=EBI-6257312, EBI-739825;
CC Q9BVN2; Q6PF18: MORN3; NbExp=3; IntAct=EBI-6257312, EBI-9675802;
CC Q9BVN2; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-6257312, EBI-5662487;
CC Q9BVN2; O15049: N4BP3; NbExp=3; IntAct=EBI-6257312, EBI-2512055;
CC Q9BVN2; Q9BSH3: NICN1; NbExp=3; IntAct=EBI-6257312, EBI-13324229;
CC Q9BVN2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-6257312, EBI-741158;
CC Q9BVN2; Q9BRQ3: NUDT22; NbExp=4; IntAct=EBI-6257312, EBI-10297093;
CC Q9BVN2; O43482: OIP5; NbExp=3; IntAct=EBI-6257312, EBI-536879;
CC Q9BVN2; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-6257312, EBI-10181968;
CC Q9BVN2; Q99471: PFDN5; NbExp=3; IntAct=EBI-6257312, EBI-357275;
CC Q9BVN2; Q92569: PIK3R3; NbExp=3; IntAct=EBI-6257312, EBI-79893;
CC Q9BVN2; O60733: PLA2G6; NbExp=3; IntAct=EBI-6257312, EBI-12089905;
CC Q9BVN2; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-6257312, EBI-11339910;
CC Q9BVN2; Q8ND90: PNMA1; NbExp=8; IntAct=EBI-6257312, EBI-302345;
CC Q9BVN2; O15160: POLR1C; NbExp=3; IntAct=EBI-6257312, EBI-1055079;
CC Q9BVN2; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-6257312, EBI-3957793;
CC Q9BVN2; P0CG20: PRR35; NbExp=3; IntAct=EBI-6257312, EBI-11986293;
CC Q9BVN2; Q93062: RBPMS; NbExp=4; IntAct=EBI-6257312, EBI-740322;
CC Q9BVN2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-6257312, EBI-740343;
CC Q9BVN2; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-6257312, EBI-358436;
CC Q9BVN2; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-6257312, EBI-8463848;
CC Q9BVN2; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-6257312, EBI-12288855;
CC Q9BVN2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-6257312, EBI-11959123;
CC Q9BVN2; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-6257312, EBI-357085;
CC Q9BVN2; P51687: SUOX; NbExp=3; IntAct=EBI-6257312, EBI-3921347;
CC Q9BVN2; Q3MII6: TBC1D25; NbExp=3; IntAct=EBI-6257312, EBI-11899977;
CC Q9BVN2; Q9BT92: TCHP; NbExp=3; IntAct=EBI-6257312, EBI-740781;
CC Q9BVN2; Q8WW24: TEKT4; NbExp=5; IntAct=EBI-6257312, EBI-750487;
CC Q9BVN2; Q96A09: TENT5B; NbExp=3; IntAct=EBI-6257312, EBI-752030;
CC Q9BVN2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-6257312, EBI-11741437;
CC Q9BVN2; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-6257312, EBI-8451480;
CC Q9BVN2; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-6257312, EBI-10259086;
CC Q9BVN2; Q96PN8: TSSK3; NbExp=5; IntAct=EBI-6257312, EBI-3918381;
CC Q9BVN2; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-6257312, EBI-948354;
CC Q9BVN2; Q86TV6: TTC7B; NbExp=3; IntAct=EBI-6257312, EBI-12006098;
CC Q9BVN2; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-6257312, EBI-12068150;
CC Q9BVN2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-6257312, EBI-11957216;
CC Q9BVN2; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-6257312, EBI-12040603;
CC Q9BVN2; O00308: WWP2; NbExp=3; IntAct=EBI-6257312, EBI-743923;
CC Q9BVN2; Q15915: ZIC1; NbExp=3; IntAct=EBI-6257312, EBI-11963196;
CC Q9BVN2; Q9H0C1: ZMYND12; NbExp=5; IntAct=EBI-6257312, EBI-12030590;
CC Q9BVN2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-6257312, EBI-4395669;
CC Q9BVN2; Q7L2R6-2: ZNF765; NbExp=3; IntAct=EBI-6257312, EBI-12834294;
CC Q9BVN2; Q15935: ZNF77; NbExp=3; IntAct=EBI-6257312, EBI-12840750;
CC Q9BVN2-2; Q9Y6K9: IKBKG; NbExp=4; IntAct=EBI-6257338, EBI-81279;
CC Q9BVN2-2; Q9Y4K3: TRAF6; NbExp=2; IntAct=EBI-6257338, EBI-359276;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15024033}. Nucleus
CC {ECO:0000269|PubMed:15024033}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8BG26}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q8BG26}. Early endosome
CC {ECO:0000250|UniProtKB:Q8BG26}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q8BG26}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8BG26}. Note=Translocated to the nuclear
CC envelope upon stimulation with NGF (PubMed:15024033). Associated with
CC membranes and microtubules (By similarity).
CC {ECO:0000250|UniProtKB:Q8BG26, ECO:0000269|PubMed:15024033}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BVN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVN2-2; Sequence=VSP_010855;
CC Name=3;
CC IsoId=Q9BVN2-3; Sequence=VSP_054052;
CC Name=4;
CC IsoId=Q9BVN2-4; Sequence=VSP_054053;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC {ECO:0000269|PubMed:15024033}.
CC -!- DOMAIN: The RUN domain is necessary for NGF induced nuclear
CC redistribution. {ECO:0000269|PubMed:15024033}.
CC -!- PTM: Phosphorylated on serine residues following nuclear translocation.
CC {ECO:0000269|PubMed:15024033}.
CC -!- PTM: Polyubiquitinated; polyubiquitination involves TRAF6.
CC {ECO:0000269|PubMed:19365808}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52277.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG54191.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026894; BAA77507.2; -; mRNA.
DR EMBL; AL080083; CAB45702.1; -; mRNA.
DR EMBL; AK314559; BAG37144.1; -; mRNA.
DR EMBL; AK074982; BAG52045.1; -; mRNA.
DR EMBL; AK055451; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK125378; BAG54191.1; ALT_INIT; mRNA.
DR EMBL; BX640612; CAE45718.1; -; mRNA.
DR EMBL; AL139410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53069.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53071.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53072.1; -; Genomic_DNA.
DR EMBL; BC001045; AAH01045.1; -; mRNA.
DR EMBL; BC025680; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC052277; AAH52277.1; ALT_INIT; mRNA.
DR CCDS; CCDS1112.1; -. [Q9BVN2-2]
DR CCDS; CCDS41410.1; -. [Q9BVN2-1]
DR CCDS; CCDS41411.1; -. [Q9BVN2-4]
DR CCDS; CCDS41412.1; -. [Q9BVN2-3]
DR PIR; T12473; T12473.
DR RefSeq; NP_001098673.1; NM_001105203.1. [Q9BVN2-1]
DR RefSeq; NP_001098674.1; NM_001105204.1. [Q9BVN2-4]
DR RefSeq; NP_001098675.1; NM_001105205.1. [Q9BVN2-3]
DR RefSeq; NP_001265156.1; NM_001278227.1.
DR RefSeq; NP_001265157.1; NM_001278228.1.
DR RefSeq; NP_001265158.1; NM_001278229.1.
DR RefSeq; NP_001265159.1; NM_001278230.1. [Q9BVN2-2]
DR RefSeq; NP_055143.2; NM_014328.4. [Q9BVN2-2]
DR RefSeq; XP_006711320.1; XM_006711257.1. [Q9BVN2-2]
DR RefSeq; XP_016856381.1; XM_017000892.1.
DR PDB; 4GIW; X-ray; 2.00 A; A/B=477-666.
DR PDBsum; 4GIW; -.
DR AlphaFoldDB; Q9BVN2; -.
DR SMR; Q9BVN2; -.
DR BioGRID; 117155; 102.
DR IntAct; Q9BVN2; 105.
DR MINT; Q9BVN2; -.
DR STRING; 9606.ENSP00000357336; -.
DR iPTMnet; Q9BVN2; -.
DR PhosphoSitePlus; Q9BVN2; -.
DR BioMuta; RUSC1; -.
DR DMDM; 160380712; -.
DR EPD; Q9BVN2; -.
DR jPOST; Q9BVN2; -.
DR MassIVE; Q9BVN2; -.
DR MaxQB; Q9BVN2; -.
DR PaxDb; Q9BVN2; -.
DR PeptideAtlas; Q9BVN2; -.
DR PRIDE; Q9BVN2; -.
DR ProteomicsDB; 64815; -.
DR ProteomicsDB; 79221; -. [Q9BVN2-1]
DR ProteomicsDB; 79222; -. [Q9BVN2-2]
DR Antibodypedia; 34192; 125 antibodies from 23 providers.
DR DNASU; 23623; -.
DR Ensembl; ENST00000292254.8; ENSP00000292254.4; ENSG00000160753.16. [Q9BVN2-2]
DR Ensembl; ENST00000368347.8; ENSP00000357331.4; ENSG00000160753.16. [Q9BVN2-3]
DR Ensembl; ENST00000368349.8; ENSP00000357333.4; ENSG00000160753.16. [Q9BVN2-2]
DR Ensembl; ENST00000368352.10; ENSP00000357336.5; ENSG00000160753.16. [Q9BVN2-1]
DR Ensembl; ENST00000368354.7; ENSP00000357338.3; ENSG00000160753.16. [Q9BVN2-4]
DR GeneID; 23623; -.
DR KEGG; hsa:23623; -.
DR MANE-Select; ENST00000368352.10; ENSP00000357336.5; NM_001105203.2; NP_001098673.1.
DR UCSC; uc001fkj.3; human. [Q9BVN2-1]
DR CTD; 23623; -.
DR DisGeNET; 23623; -.
DR GeneCards; RUSC1; -.
DR HGNC; HGNC:17153; RUSC1.
DR HPA; ENSG00000160753; Low tissue specificity.
DR MIM; 617318; gene.
DR neXtProt; NX_Q9BVN2; -.
DR OpenTargets; ENSG00000160753; -.
DR PharmGKB; PA134947113; -.
DR VEuPathDB; HostDB:ENSG00000160753; -.
DR eggNOG; ENOG502QWTC; Eukaryota.
DR GeneTree; ENSGT00900000141033; -.
DR HOGENOM; CLU_014918_0_0_1; -.
DR InParanoid; Q9BVN2; -.
DR OMA; GWKTNTG; -.
DR OrthoDB; 373320at2759; -.
DR PhylomeDB; Q9BVN2; -.
DR TreeFam; TF332235; -.
DR PathwayCommons; Q9BVN2; -.
DR SignaLink; Q9BVN2; -.
DR BioGRID-ORCS; 23623; 23 hits in 1086 CRISPR screens.
DR ChiTaRS; RUSC1; human.
DR GenomeRNAi; 23623; -.
DR Pharos; Q9BVN2; Tbio.
DR PRO; PR:Q9BVN2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BVN2; protein.
DR Bgee; ENSG00000160753; Expressed in right hemisphere of cerebellum and 189 other tissues.
DR ExpressionAtlas; Q9BVN2; baseline and differential.
DR Genevisible; Q9BVN2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF02759; RUN; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00593; RUN; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endosome; Golgi apparatus; Microtubule; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain; Synapse; Ubl conjugation.
FT CHAIN 1..902
FT /note="AP-4 complex accessory subunit RUSC1"
FT /id="PRO_0000097532"
FT DOMAIN 522..666
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 844..902
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 31..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..605
FT /note="Interaction with TRAF6"
FT /evidence="ECO:0000269|PubMed:19365808"
FT REGION 606..672
FT /note="Interaction with IKBKG"
FT /evidence="ECO:0000269|PubMed:19365808"
FT REGION 706..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..469
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10760598,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16303743, ECO:0000303|PubMed:17974005"
FT /id="VSP_010855"
FT VAR_SEQ 1..452
FT /note="MLSPQRALLCNLNHIHLQHVSLGLHLSRRPELQEGPLSTPPPPGDTGGKESR
FT GPCSGTLVDANSNSPAVPCRCCQEHGPGLENRQDPSQEEEGAASPSDPGCSSSLSSCSD
FT LSPDESPVSVYLRDLPGDEDAHPQPSIIPLEQGSPLASAGPGTCSPDSFCCSPDSCSGA
FT SSSPDPGLDSNCNALTTCQDVPSPGLEEEDERAEQDLPTSELLEADDGKIDAGKTEPSW
FT KINPIWKIDTEKTKAEWKTTENNNTGWKNNGNVNSSWKSEPEKFDSGWKTNTRITDSGS
FT KTDAGKIDGGWRSDVSEEPVPHRTITSFHELAQKRKRGPGLPLVPQAKKDRSDWLIVFS
FT PDTELPPSGSPGGSSAPPREVTTFKELRSRSRAPAPPVPPRDPPVGWALVPPRPPPPPV
FT PPRRKKNRPGLQPIAEGQSEEGRAVSPAAGEEAPAAKEPGAQAGLE -> MPPTCSPGL
FT RRQDWAPGRCAGLHLPPRAPSSPALQALAGQAG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054052"
FT VAR_SEQ 621..726
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054053"
FT VARIANT 362
FT /note="S -> F (in dbSNP:rs12061020)"
FT /id="VAR_036803"
FT VARIANT 493
FT /note="V -> A (in dbSNP:rs35826120)"
FT /id="VAR_051329"
FT MUTAGEN 531
FT /note="L->A: Abrogates nuclear redistribution."
FT /evidence="ECO:0000269|PubMed:15024033"
FT CONFLICT 36
FT /note="P -> S (in Ref. 7; BC025680)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="V -> L (in Ref. 1; BAA77507)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="P -> T (in Ref. 1; BAA77507)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="F -> L (in Ref. 4; CAB45702)"
FT /evidence="ECO:0000305"
FT CONFLICT 793..795
FT /note="GPA -> APP (in Ref. 1; BAA77507)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="L -> F (in Ref. 4; CAB45702)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="F -> Y (in Ref. 4; CAB45702)"
FT /evidence="ECO:0000305"
FT HELIX 484..502
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 508..515
FT /evidence="ECO:0007829|PDB:4GIW"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 521..529
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 531..540
FT /evidence="ECO:0007829|PDB:4GIW"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:4GIW"
FT TURN 550..552
FT /evidence="ECO:0007829|PDB:4GIW"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 559..566
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 574..585
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 592..606
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 632..635
FT /evidence="ECO:0007829|PDB:4GIW"
FT TURN 639..642
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 643..651
FT /evidence="ECO:0007829|PDB:4GIW"
FT HELIX 652..656
FT /evidence="ECO:0007829|PDB:4GIW"
SQ SEQUENCE 902 AA; 96444 MW; 41DB65236E766A82 CRC64;
MLSPQRALLC NLNHIHLQHV SLGLHLSRRP ELQEGPLSTP PPPGDTGGKE SRGPCSGTLV
DANSNSPAVP CRCCQEHGPG LENRQDPSQE EEGAASPSDP GCSSSLSSCS DLSPDESPVS
VYLRDLPGDE DAHPQPSIIP LEQGSPLASA GPGTCSPDSF CCSPDSCSGA SSSPDPGLDS
NCNALTTCQD VPSPGLEEED ERAEQDLPTS ELLEADDGKI DAGKTEPSWK INPIWKIDTE
KTKAEWKTTE NNNTGWKNNG NVNSSWKSEP EKFDSGWKTN TRITDSGSKT DAGKIDGGWR
SDVSEEPVPH RTITSFHELA QKRKRGPGLP LVPQAKKDRS DWLIVFSPDT ELPPSGSPGG
SSAPPREVTT FKELRSRSRA PAPPVPPRDP PVGWALVPPR PPPPPVPPRR KKNRPGLQPI
AEGQSEEGRA VSPAAGEEAP AAKEPGAQAG LEVRSSWSFA GVPGAQRLWM AEAQSGTGQL
QEQKKGLLIA VSVSVDKIIS HFGAARNLVQ KAQLGDSRLS PDVGHLVLTT LCPALHALVA
DGLKPFRKDL ITGQRRSSPW SVVEASVKPG SSTRSLGTLY SQVSRLAPLS SSRSRFHAFI
LGLLNTKQLE LWFSSLQEDA GLLSLLYLPT GFFSLARGGC PSLSTELLLL LQPLSVLTFH
LDLLFEHHHH LPLGPPQAPA PPGPPPALQQ TMQAMLHFGG RLAQSLRGTS KEAASDPSDS
PNLPTPGSWW EQLTQASRVY ASGGTEGFPL SRWAPGRHGT AAEEGAQERP LPTDEMAPGR
GLWLGRLFGV PGGPAENENG ALKSRRPSSW LPPTVSVLAL VKRGAPPEMP SPQELEASAP
RMVQTHRAVR ALCDHTAARP DQLSFRRGEV LRVITTVDED WLRCGRDGME GLVPVGYTSL
VL
