ID   RINT1_HUMAN             Reviewed;         792 AA.
AC   Q6NUQ1; Q75MG9; Q75MH0; Q96IW8; Q9H229; Q9HAD9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=RAD50-interacting protein 1;
DE   AltName: Full=RAD50 interactor 1;
DE            Short=HsRINT-1;
DE            Short=RINT-1;
GN   Name=RINT1;
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], FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION
RP   WITH RAD50.
RC   TISSUE=B-cell;
RX   PubMed=11096100; DOI=10.1074/jbc.m008893200;
RA   Xiao J., Liu C.-C., Chen P.-L., Lee W.-H.;
RT   "RINT-1, a novel Rad50-interacting protein, participates in radiation-
RT   induced G2/M checkpoint control.";
RL   J. Biol. Chem. 276:6105-6111(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 367-792.
RC   TISSUE=Embryo;
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   [5]
RP   PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, INTERACTION WITH ZW10, AND IDENTIFICATION IN A COMPLEX WITH
RP   SEC22B; STX18; USE1L AND ZW10.
RX   PubMed=15029241; DOI=10.1038/sj.emboj.7600135;
RA   Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M.,
RA   Tani K., Yamamoto A., Tohyama M., Tagaya M.;
RT   "Implication of ZW10 in membrane trafficking between the endoplasmic
RT   reticulum and Golgi.";
RL   EMBO J. 23:1267-1278(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH BNIP1.
RX   PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA   Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA   Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT   "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT   fusion.";
RL   EMBO J. 23:3216-3226(2004).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH RBL2.
RX   PubMed=16600870; DOI=10.1016/j.molcel.2006.02.016;
RA   Kong L.-J., Meloni A.R., Nevins J.R.;
RT   "The Rb-related p130 protein controls telomere lengthening through an
RT   interaction with a Rad50-interacting protein, RINT-1.";
RL   Mol. Cell 22:63-71(2006).
RN   [8]
RP   SUBUNIT.
RX   PubMed=19369418; DOI=10.1091/mbc.e08-11-1104;
RA   Aoki T., Ichimura S., Itoh A., Kuramoto M., Shinkawa T., Isobe T.,
RA   Tagaya M.;
RT   "Identification of the neuroblastoma-amplified gene product as a component
RT   of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum
RT   retrograde transport.";
RL   Mol. Biol. Cell 20:2639-2649(2009).
RN   [9]
RP   IDENTIFICATION IN THE NRZ COMPLEX.
RX   PubMed=20462495; DOI=10.1016/j.str.2010.02.014;
RA   Civril F., Wehenkel A., Giorgi F.M., Santaguida S., Di Fonzo A.,
RA   Grigorean G., Ciccarelli F.D., Musacchio A.;
RT   "Structural analysis of the RZZ complex reveals common ancestry with
RT   multisubunit vesicle tethering machinery.";
RL   Structure 18:616-626(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   INTERACTION WITH UVRAG.
RX   PubMed=24056303; DOI=10.1038/ncb2848;
RA   He S., Ni D., Ma B., Lee J.H., Zhang T., Ghozalli I., Pirooz S.D., Zhao Z.,
RA   Bharatham N., Li B., Oh S., Lee W.H., Takahashi Y., Wang H.G.,
RA   Minassian A., Feng P., Deretic V., Pepperkok R., Tagaya M., Yoon H.S.,
RA   Liang C.;
RT   "PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport
RT   by differential interactions with the ER tether and the beclin 1 complex.";
RL   Nat. Cell Biol. 15:1206-1219(2013).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [14]
RP   INVOLVEMENT IN ILFS3, AND VARIANTS ILFS3 THR-368; PRO-370 AND
RP   618-VAL-LYS-619 DEL.
RX   PubMed=31204009; DOI=10.1016/j.ajhg.2019.05.011;
RA   Cousin M.A., Conboy E., Wang J.S., Lenz D., Schwab T.L., Williams M.,
RA   Abraham R.S., Barnett S., El-Youssef M., Graham R.P.,
RA   Gutierrez Sanchez L.H., Hasadsri L., Hoffmann G.F., Hull N.C.,
RA   Kopajtich R., Kovacs-Nagy R., Li J.Q., Marx-Berger D., McLin V.,
RA   McNiven M.A., Mounajjed T., Prokisch H., Rymen D., Schulze R.J.,
RA   Staufner C., Yang Y., Clark K.J., Lanpher B.C., Klee E.W.;
RT   "RINT1 bi-allelic variations cause infantile-onset recurrent acute liver
RT   failure and skeletal abnormalities.";
RL   Am. J. Hum. Genet. 105:108-121(2019).
CC   -!- FUNCTION: Involved in regulation of membrane traffic between the Golgi
CC       and the endoplasmic reticulum (ER); the function is proposed to depend
CC       on its association in the NRZ complex which is believed to play a role
CC       in SNARE assembly at the ER. May play a role in cell cycle checkpoint
CC       control (PubMed:11096100). Essential for telomere length control
CC       (PubMed:16600870). {ECO:0000269|PubMed:11096100,
CC       ECO:0000269|PubMed:16600870, ECO:0000305}.
CC   -!- SUBUNIT: Component of the NRZ complex composed of NBAS, ZW10 and
CC       RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and
CC       SEC22B (the assembly has been described as syntaxin 18 complex)
CC       (PubMed:15029241, PubMed:20462495, PubMed:19369418). Interacts directly
CC       with BNIP1/SEC20L and ZW10 (PubMed:15029241, PubMed:15272311).
CC       Interacts with UVRAG (PubMed:24056303). Interacts with RAD50 during
CC       late S and G2/M phases (PubMed:11096100). Interacts with RBL2,
CC       preferentially with the active, hypophosphorylated form
CC       (PubMed:16600870). {ECO:0000269|PubMed:11096100,
CC       ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15272311,
CC       ECO:0000269|PubMed:16600870, ECO:0000269|PubMed:19369418,
CC       ECO:0000269|PubMed:20462495, ECO:0000269|PubMed:24056303}.
CC   -!- INTERACTION:
CC       Q6NUQ1; Q9NX04: AIRIM; NbExp=6; IntAct=EBI-726876, EBI-8643161;
CC       Q6NUQ1; X5D778: ANKRD11; NbExp=3; IntAct=EBI-726876, EBI-17183751;
CC       Q6NUQ1; Q92619: ARHGAP45; NbExp=5; IntAct=EBI-726876, EBI-2825900;
CC       Q6NUQ1; Q13515: BFSP2; NbExp=3; IntAct=EBI-726876, EBI-10229433;
CC       Q6NUQ1; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-726876, EBI-465781;
CC       Q6NUQ1; Q9UFG5: C19orf25; NbExp=4; IntAct=EBI-726876, EBI-741214;
CC       Q6NUQ1; Q9H6X5-2: C19orf44; NbExp=3; IntAct=EBI-726876, EBI-12061599;
CC       Q6NUQ1; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-726876, EBI-744556;
CC       Q6NUQ1; Q6ZUS5: CCDC121; NbExp=4; IntAct=EBI-726876, EBI-2836982;
CC       Q6NUQ1; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-726876, EBI-10247802;
CC       Q6NUQ1; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-726876, EBI-10961624;
CC       Q6NUQ1; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-726876, EBI-347573;
CC       Q6NUQ1; Q8TD31-3: CCHCR1; NbExp=5; IntAct=EBI-726876, EBI-10175300;
CC       Q6NUQ1; Q86X02: CDR2L; NbExp=3; IntAct=EBI-726876, EBI-11063830;
CC       Q6NUQ1; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-726876, EBI-10181988;
CC       Q6NUQ1; Q1MSJ5-1: CSPP1; NbExp=3; IntAct=EBI-726876, EBI-10239122;
CC       Q6NUQ1; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-726876, EBI-5453285;
CC       Q6NUQ1; Q13561: DCTN2; NbExp=3; IntAct=EBI-726876, EBI-715074;
CC       Q6NUQ1; O43602: DCX; NbExp=4; IntAct=EBI-726876, EBI-8646694;
CC       Q6NUQ1; Q92785: DPF2; NbExp=3; IntAct=EBI-726876, EBI-359932;
CC       Q6NUQ1; Q9H2F5: EPC1; NbExp=5; IntAct=EBI-726876, EBI-769270;
CC       Q6NUQ1; P62508-3: ESRRG; NbExp=3; IntAct=EBI-726876, EBI-12001340;
CC       Q6NUQ1; Q8IYI6: EXOC8; NbExp=5; IntAct=EBI-726876, EBI-742102;
CC       Q6NUQ1; O95990-3: FAM107A; NbExp=3; IntAct=EBI-726876, EBI-10192902;
CC       Q6NUQ1; Q9BQ89: FAM110A; NbExp=6; IntAct=EBI-726876, EBI-1752811;
CC       Q6NUQ1; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-726876, EBI-741626;
CC       Q6NUQ1; Q3B820: FAM161A; NbExp=3; IntAct=EBI-726876, EBI-719941;
CC       Q6NUQ1; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-726876, EBI-7225287;
CC       Q6NUQ1; Q96LP2: FAM81B; NbExp=5; IntAct=EBI-726876, EBI-10290827;
CC       Q6NUQ1; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-726876, EBI-6658203;
CC       Q6NUQ1; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-726876, EBI-11958845;
CC       Q6NUQ1; O95995: GAS8; NbExp=3; IntAct=EBI-726876, EBI-1052570;
CC       Q6NUQ1; P56524: HDAC4; NbExp=3; IntAct=EBI-726876, EBI-308629;
CC       Q6NUQ1; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-726876, EBI-16429135;
CC       Q6NUQ1; P42858: HTT; NbExp=3; IntAct=EBI-726876, EBI-466029;
CC       Q6NUQ1; Q15735: INPP5J; NbExp=3; IntAct=EBI-726876, EBI-10236940;
CC       Q6NUQ1; Q8N9B5-2: JMY; NbExp=3; IntAct=EBI-726876, EBI-10268138;
CC       Q6NUQ1; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-726876, EBI-10188326;
CC       Q6NUQ1; P04264: KRT1; NbExp=3; IntAct=EBI-726876, EBI-298429;
CC       Q6NUQ1; P25791: LMO2; NbExp=4; IntAct=EBI-726876, EBI-739696;
CC       Q6NUQ1; Q0VAF8: LOC729862; NbExp=3; IntAct=EBI-726876, EBI-10226726;
CC       Q6NUQ1; Q0VAF9: LOC729862; NbExp=3; IntAct=EBI-726876, EBI-10226748;
CC       Q6NUQ1; Q96S90: LYSMD1; NbExp=3; IntAct=EBI-726876, EBI-10293291;
CC       Q6NUQ1; O95983-2: MBD3; NbExp=3; IntAct=EBI-726876, EBI-11978579;
CC       Q6NUQ1; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-726876, EBI-14086479;
CC       Q6NUQ1; Q8IVT2: MISP; NbExp=3; IntAct=EBI-726876, EBI-2555085;
CC       Q6NUQ1; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-726876, EBI-742459;
CC       Q6NUQ1; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-726876, EBI-5662487;
CC       Q6NUQ1; Q15742: NAB2; NbExp=3; IntAct=EBI-726876, EBI-8641936;
CC       Q6NUQ1; Q16649: NFIL3; NbExp=3; IntAct=EBI-726876, EBI-3951858;
CC       Q6NUQ1; O00459: PIK3R2; NbExp=3; IntAct=EBI-726876, EBI-346930;
CC       Q6NUQ1; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-726876, EBI-2568609;
CC       Q6NUQ1; Q99633: PRPF18; NbExp=3; IntAct=EBI-726876, EBI-2798416;
CC       Q6NUQ1; A0A0S2Z528: PSTPIP1; NbExp=3; IntAct=EBI-726876, EBI-16430249;
CC       Q6NUQ1; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-726876, EBI-744023;
CC       Q6NUQ1; Q96IZ5: RBM41; NbExp=6; IntAct=EBI-726876, EBI-740773;
CC       Q6NUQ1; Q8N443: RIBC1; NbExp=7; IntAct=EBI-726876, EBI-10265323;
CC       Q6NUQ1; Q9H2S5: RNF39; NbExp=3; IntAct=EBI-726876, EBI-12235180;
CC       Q6NUQ1; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-726876, EBI-16428950;
CC       Q6NUQ1; Q7L4I2-2: RSRC2; NbExp=3; IntAct=EBI-726876, EBI-10256202;
CC       Q6NUQ1; Q14D33: RTP5; NbExp=3; IntAct=EBI-726876, EBI-10217913;
CC       Q6NUQ1; Q9BWG6: SCNM1; NbExp=5; IntAct=EBI-726876, EBI-748391;
CC       Q6NUQ1; Q86XK3: SFR1; NbExp=4; IntAct=EBI-726876, EBI-1104535;
CC       Q6NUQ1; Q96ES7: SGF29; NbExp=7; IntAct=EBI-726876, EBI-743117;
CC       Q6NUQ1; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-726876, EBI-747035;
CC       Q6NUQ1; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-726876, EBI-10308083;
CC       Q6NUQ1; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-726876, EBI-455078;
CC       Q6NUQ1; Q13573: SNW1; NbExp=7; IntAct=EBI-726876, EBI-632715;
CC       Q6NUQ1; O43815: STRN; NbExp=3; IntAct=EBI-726876, EBI-1046642;
CC       Q6NUQ1; P51687: SUOX; NbExp=3; IntAct=EBI-726876, EBI-3921347;
CC       Q6NUQ1; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-726876, EBI-747797;
CC       Q6NUQ1; A0A0S2Z5Z9: TEX9; NbExp=3; IntAct=EBI-726876, EBI-16431655;
CC       Q6NUQ1; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-726876, EBI-11525489;
CC       Q6NUQ1; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-726876, EBI-2559824;
CC       Q6NUQ1; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-726876, EBI-10687282;
CC       Q6NUQ1; Q63HK5: TSHZ3; NbExp=5; IntAct=EBI-726876, EBI-9053916;
CC       Q6NUQ1; P40222: TXLNA; NbExp=6; IntAct=EBI-726876, EBI-359793;
CC       Q6NUQ1; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-726876, EBI-739895;
CC       Q6NUQ1; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-726876, EBI-11737646;
CC       Q6NUQ1; Q9P2Y5: UVRAG; NbExp=18; IntAct=EBI-726876, EBI-2952704;
CC       Q6NUQ1; Q9UKW4: VAV3; NbExp=3; IntAct=EBI-726876, EBI-297568;
CC       Q6NUQ1; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-726876, EBI-2559305;
CC       Q6NUQ1; Q05516: ZBTB16; NbExp=3; IntAct=EBI-726876, EBI-711925;
CC       Q6NUQ1; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-726876, EBI-14104088;
CC       Q6NUQ1; Q5T619: ZNF648; NbExp=3; IntAct=EBI-726876, EBI-11985915;
CC       Q6NUQ1; Q8N720: ZNF655; NbExp=5; IntAct=EBI-726876, EBI-625509;
CC       Q6NUQ1; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-726876, EBI-16429014;
CC       Q6NUQ1; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-726876, EBI-16429989;
CC       Q6NUQ1; Q8N508: ZNF697; NbExp=3; IntAct=EBI-726876, EBI-10265733;
CC       Q6NUQ1; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-726876, EBI-5667516;
CC       Q6NUQ1; A6NJL1: ZSCAN5B; NbExp=3; IntAct=EBI-726876, EBI-17968892;
CC       Q6NUQ1; O43264: ZW10; NbExp=16; IntAct=EBI-726876, EBI-1001217;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane;
CC       Peripheral membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle.
CC       {ECO:0000269|PubMed:11096100}.
CC   -!- DISEASE: Infantile liver failure syndrome 3 (ILFS3) [MIM:618641]: A
CC       form of infantile liver failure syndrome, a life-threatening disorder
CC       of hepatic function that manifests with acute liver failure in the
CC       first months or years of life. ILFS3 is an autosomal recessive form
CC       characterized by recurrent episodes of acute liver failure often
CC       triggered by infection or fever. Affected individuals also have
CC       skeletal anomalies of the vertebral bodies and femoral heads.
CC       {ECO:0000269|PubMed:31204009}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: According to PubMed:11096100, a longer form, which may
CC       be due to the differential initiation of translation using a non-AUG
CC       codon, may exist. However, the existence of such form has not been
CC       clearly demonstrated.
CC   -!- SIMILARITY: Belongs to the RINT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG42101.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAQ96849.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAQ96850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB13910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF317622; AAG42101.1; ALT_INIT; mRNA.
DR   EMBL; AC073073; AAQ96849.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC073073; AAQ96850.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC007120; AAH07120.2; -; mRNA.
DR   EMBL; BC068483; AAH68483.1; -; mRNA.
DR   EMBL; AK021847; BAB13910.1; ALT_INIT; mRNA.
DR   CCDS; CCDS34726.1; -.
DR   RefSeq; NP_068749.3; NM_021930.5.
DR   AlphaFoldDB; Q6NUQ1; -.
DR   SMR; Q6NUQ1; -.
DR   BioGRID; 121942; 238.
DR   ComplexPortal; CPX-6201; NRZ tethering complex.
DR   CORUM; Q6NUQ1; -.
DR   DIP; DIP-36477N; -.
DR   IntAct; Q6NUQ1; 144.
DR   MINT; Q6NUQ1; -.
DR   STRING; 9606.ENSP00000257700; -.
DR   GlyCosmos; Q6NUQ1; 1 site, 1 glycan.
DR   GlyGen; Q6NUQ1; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q6NUQ1; -.
DR   PhosphoSitePlus; Q6NUQ1; -.
DR   SwissPalm; Q6NUQ1; -.
DR   BioMuta; RINT1; -.
DR   DMDM; 71152944; -.
DR   EPD; Q6NUQ1; -.
DR   jPOST; Q6NUQ1; -.
DR   MassIVE; Q6NUQ1; -.
DR   MaxQB; Q6NUQ1; -.
DR   PaxDb; 9606-ENSP00000257700; -.
DR   PeptideAtlas; Q6NUQ1; -.
DR   ProteomicsDB; 66701; -.
DR   Pumba; Q6NUQ1; -.
DR   Antibodypedia; 17090; 119 antibodies from 23 providers.
DR   DNASU; 60561; -.
DR   Ensembl; ENST00000257700.7; ENSP00000257700.2; ENSG00000135249.8.
DR   GeneID; 60561; -.
DR   KEGG; hsa:60561; -.
DR   MANE-Select; ENST00000257700.7; ENSP00000257700.2; NM_021930.6; NP_068749.3.
DR   UCSC; uc003vda.1; human.
DR   AGR; HGNC:21876; -.
DR   CTD; 60561; -.
DR   DisGeNET; 60561; -.
DR   GeneCards; RINT1; -.
DR   HGNC; HGNC:21876; RINT1.
DR   HPA; ENSG00000135249; Low tissue specificity.
DR   MalaCards; RINT1; -.
DR   MIM; 610089; gene.
DR   MIM; 618641; phenotype.
DR   neXtProt; NX_Q6NUQ1; -.
DR   OpenTargets; ENSG00000135249; -.
DR   Orphanet; 464724; Fever-associated acute infantile liver failure syndrome.
DR   PharmGKB; PA143485595; -.
DR   VEuPathDB; HostDB:ENSG00000135249; -.
DR   eggNOG; KOG2218; Eukaryota.
DR   GeneTree; ENSGT00390000017006; -.
DR   HOGENOM; CLU_020201_0_0_1; -.
DR   InParanoid; Q6NUQ1; -.
DR   OMA; VLKSMRW; -.
DR   OrthoDB; 1405628at2759; -.
DR   PhylomeDB; Q6NUQ1; -.
DR   TreeFam; TF324274; -.
DR   PathwayCommons; Q6NUQ1; -.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   SignaLink; Q6NUQ1; -.
DR   SIGNOR; Q6NUQ1; -.
DR   BioGRID-ORCS; 60561; 539 hits in 1161 CRISPR screens.
DR   ChiTaRS; RINT1; human.
DR   GeneWiki; RINT1; -.
DR   GenomeRNAi; 60561; -.
DR   Pharos; Q6NUQ1; Tbio.
DR   PRO; PR:Q6NUQ1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q6NUQ1; Protein.
DR   Bgee; ENSG00000135249; Expressed in tibia and 171 other cell types or tissues.
DR   ExpressionAtlas; Q6NUQ1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070939; C:Dsl1/NZR complex; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:BHF-UCL.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   Gene3D; 1.20.58.670; Dsl1p vesicle tethering complex, Tip20p subunit, domain D; 1.
DR   InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR   InterPro; IPR007528; RINT1_Tip20.
DR   PANTHER; PTHR13520:SF0; RAD50-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR13520; RAD50-INTERACTING PROTEIN 1 RINT-1; 1.
DR   Pfam; PF04437; RINT1_TIP1; 1.
DR   PROSITE; PS51386; RINT1_TIP20; 1.
DR   Genevisible; Q6NUQ1; HS.
PE   1: Evidence at protein level;
KW   Cell cycle; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..792
FT                   /note="RAD50-interacting protein 1"
FT                   /id="PRO_0000097349"
FT   DOMAIN          220..792
FT                   /note="RINT1/TIP20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00717"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          103..124
FT                   /evidence="ECO:0000255"
FT   VARIANT         40
FT                   /note="S -> C (in dbSNP:rs11556986)"
FT                   /id="VAR_051322"
FT   VARIANT         368
FT                   /note="A -> T (in ILFS3; dbSNP:rs545894353)"
FT                   /evidence="ECO:0000269|PubMed:31204009"
FT                   /id="VAR_083238"
FT   VARIANT         370
FT                   /note="L -> P (in ILFS3; dbSNP:rs1562849964)"
FT                   /evidence="ECO:0000269|PubMed:31204009"
FT                   /id="VAR_083239"
FT   VARIANT         618..619
FT                   /note="Missing (in ILFS3)"
FT                   /evidence="ECO:0000269|PubMed:31204009"
FT                   /id="VAR_083240"
FT   VARIANT         668
FT                   /note="F -> S (in dbSNP:rs35971380)"
FT                   /id="VAR_034418"
FT   VARIANT         759
FT                   /note="P -> L (in dbSNP:rs34310648)"
FT                   /id="VAR_034419"
FT   CONFLICT        758
FT                   /note="L -> P (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        759..760
FT                   /note="PA -> ST (in Ref. 1; AAG42101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   792 AA;  90632 MW;  6671066FCC5E74D6 CRC64;
     MLPAGEIGAS PAAPCCSESG DERKNLEEKS DINVTVLIGS KQVSEGTDNG DLPSYVSAFI
     EKEVGNDLKS LKKLDKLIEQ RTVSKMQLEE QVLTISSEIP KRIRSALKNA EESKQFLNQF
     LEQETHLFSA INSHLLTAQP WMDDLGTMIS QIEEIERHLA YLKWISQIEE LSDNIQQYLM
     TNNVPEAAST LVSMAELDIK LQESSCTHLL GFMRATVKFW HKILKDKLTS DFEEILAQLH
     WPFIAPPQSQ TVGLSRPASA PEIYSYLETL FCQLLKLQTS DELLTEPKQL PEKYSLPASP
     SVILPIQVML TPLQKRFRYH FRGNRQTNVL SKPEWYLAQV LMWIGNHTEF LDEKIQPILD
     KVGSLVNARL EFSRGLMMLV LEKLATDIPC LLYDDNLFCH LVDEVLLFER ELHSVHGYPG
     TFASCMHILS EETCFQRWLT VERKFALQKM DSMLSSEAAW VSQYKDITDV DEMKVPDCAE
     TFMTLLLVIT DRYKNLPTAS RKLQFLELQK DLVDDFRIRL TQVMKEETRA SLGFRYCAIL
     NAVNYISTVL ADWADNVFFL QLQQAALEVF AENNTLSKLQ LGQLASMESS VFDDMINLLE
     RLKHDMLTRQ VDHVFREVKD AAKLYKKERW LSLPSQSEQA VMSLSSSACP LLLTLRDHLL
     QLEQQLCFSL FKIFWQMLVE KLDVYIYQEI ILANHFNEGG AAQLQFDMTR NLFPLFSHYC
     KRPENYFKHI KEACIVLNLN VGSALLLKDV LQSASGQLPA TAALNEVGIY KLAQQDVEIL
     LNLRTNWPNT GK
//