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NIF3L_HUMAN
ID   NIF3L_HUMAN             Reviewed;         377 AA.
AC   Q9GZT8; Q53TX4; Q6X735; Q9H2D2; Q9HC18;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=NIF3-like protein 1 {ECO:0000305|PubMed:11124544};
DE   AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 1 protein {ECO:0000303|PubMed:11161814};
GN   Name=NIF3L1 {ECO:0000312|HGNC:HGNC:13390};
GN   Synonyms=ALS2CR1 {ECO:0000303|PubMed:11161814}; ORFNames=MDS015, My018;
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), AND SUBCELLULAR LOCATION.
RX   PubMed=11124544; DOI=10.1159/000056799;
RA   Tascou S., Uedelhoven J., Dixkens C., Nayernia K., Engel W., Burfeind P.;
RT   "Isolation and characterization of a novel human gene, NIF3L1, and its
RT   mouse ortholog, Nif3l1, highly conserved from bacteria to mammals.";
RL   Cytogenet. Cell Genet. 90:330-336(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=11161814; DOI=10.1006/geno.2000.6392;
RA   Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J., Martindale D.,
RA   Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A., Ikeda J.-E.,
RA   Hayden M.R.;
RT   "Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and
RT   ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical
RT   region at chromosome 2q33-q34: candidate genes for ALS2.";
RL   Genomics 71:200-213(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Merla G., Reymond A.;
RT   "NIF3L1 interacts with WBSCR14.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Mao Y.M., Xie Y., Huang X.Y., Ying K., Dai J.L.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Hematopoietic stem cell;
RA   Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT   "Novel genes expressed in hematopoietic stem/progenitor cells from
RT   myelodysplastic syndrome patients.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Ovarian carcinoma;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
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   [10]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), HOMODIMERIZATION, INTERACTION WITH
RP   THOC7, AND SUBCELLULAR LOCATION.
RX   PubMed=12951069; DOI=10.1016/j.bbrc.2003.07.008;
RA   Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P.;
RT   "Identification and characterization of NIF3L1 BP1, a novel cytoplasmic
RT   interaction partner of the NIF3L1 protein.";
RL   Biochem. Biophys. Res. Commun. 309:440-448(2003).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
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   [13]
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).
CC   -!- FUNCTION: May function as a transcriptional corepressor through its
CC       interaction with COPS2, negatively regulating the expression of genes
CC       involved in neuronal differentiation. {ECO:0000250|UniProtKB:Q9EQ80}.
CC   -!- SUBUNIT: Homodimer (PubMed:12951069). Interacts with COPS2 (By
CC       similarity). Interacts with THOC7 (PubMed:12951069).
CC       {ECO:0000250|UniProtKB:Q9EQ80, ECO:0000269|PubMed:12951069}.
CC   -!- INTERACTION:
CC       Q9GZT8; Q9NXW9: ALKBH4; NbExp=5; IntAct=EBI-740897, EBI-8637516;
CC       Q9GZT8; Q2VPB7: AP5B1; NbExp=3; IntAct=EBI-740897, EBI-5917279;
CC       Q9GZT8; Q7Z6K5: ARPIN; NbExp=3; IntAct=EBI-740897, EBI-10258086;
CC       Q9GZT8; Q8N7W2: BEND7; NbExp=3; IntAct=EBI-740897, EBI-743382;
CC       Q9GZT8; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-740897, EBI-725606;
CC       Q9GZT8; P55210: CASP7; NbExp=3; IntAct=EBI-740897, EBI-523958;
CC       Q9GZT8; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-740897, EBI-10171570;
CC       Q9GZT8; P42772: CDKN2B; NbExp=3; IntAct=EBI-740897, EBI-711280;
CC       Q9GZT8; P42773: CDKN2C; NbExp=6; IntAct=EBI-740897, EBI-711290;
CC       Q9GZT8; P55273: CDKN2D; NbExp=3; IntAct=EBI-740897, EBI-745859;
CC       Q9GZT8; Q9NUQ9: CYRIB; NbExp=3; IntAct=EBI-740897, EBI-1055930;
CC       Q9GZT8; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-740897, EBI-10303987;
CC       Q9GZT8; P49366: DHPS; NbExp=3; IntAct=EBI-740897, EBI-741925;
CC       Q9GZT8; Q14565: DMC1; NbExp=9; IntAct=EBI-740897, EBI-930865;
CC       Q9GZT8; Q86UW9: DTX2; NbExp=3; IntAct=EBI-740897, EBI-740376;
CC       Q9GZT8; Q9BVJ7: DUSP23; NbExp=3; IntAct=EBI-740897, EBI-724940;
CC       Q9GZT8; Q68J44: DUSP29; NbExp=3; IntAct=EBI-740897, EBI-1054321;
CC       Q9GZT8; P51808: DYNLT3; NbExp=3; IntAct=EBI-740897, EBI-743027;
CC       Q9GZT8; P38919: EIF4A3; NbExp=3; IntAct=EBI-740897, EBI-299104;
CC       Q9GZT8; Q9GZV4: EIF5A2; NbExp=3; IntAct=EBI-740897, EBI-748028;
CC       Q9GZT8; O15197-2: EPHB6; NbExp=3; IntAct=EBI-740897, EBI-10182490;
CC       Q9GZT8; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-740897, EBI-11526128;
CC       Q9GZT8; P51116: FXR2; NbExp=3; IntAct=EBI-740897, EBI-740459;
CC       Q9GZT8; P62993: GRB2; NbExp=3; IntAct=EBI-740897, EBI-401755;
CC       Q9GZT8; Q96PC2: IP6K3; NbExp=3; IntAct=EBI-740897, EBI-10990676;
CC       Q9GZT8; Q9NZI2-2: KCNIP1; NbExp=6; IntAct=EBI-740897, EBI-22452746;
CC       Q9GZT8; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-740897, EBI-11954971;
CC       Q9GZT8; Q7L273: KCTD9; NbExp=3; IntAct=EBI-740897, EBI-4397613;
CC       Q9GZT8; Q9UHA4: LAMTOR3; NbExp=3; IntAct=EBI-740897, EBI-1038192;
CC       Q9GZT8; P25791: LMO2; NbExp=3; IntAct=EBI-740897, EBI-739696;
CC       Q9GZT8; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-740897, EBI-11742507;
CC       Q9GZT8; Q8N6N6: NATD1; NbExp=6; IntAct=EBI-740897, EBI-8656665;
CC       Q9GZT8; Q9HC98-4: NEK6; NbExp=5; IntAct=EBI-740897, EBI-11750983;
CC       Q9GZT8; Q9NPG2: NGB; NbExp=5; IntAct=EBI-740897, EBI-10311409;
CC       Q9GZT8; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-740897, EBI-740897;
CC       Q9GZT8; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-740897, EBI-744782;
CC       Q9GZT8; O95848: NUDT14; NbExp=6; IntAct=EBI-740897, EBI-536866;
CC       Q9GZT8; A4D0P7: ORC5L; NbExp=3; IntAct=EBI-740897, EBI-10173275;
CC       Q9GZT8; Q15102: PAFAH1B3; NbExp=3; IntAct=EBI-740897, EBI-711522;
CC       Q9GZT8; O15160: POLR1C; NbExp=3; IntAct=EBI-740897, EBI-1055079;
CC       Q9GZT8; O43447: PPIH; NbExp=3; IntAct=EBI-740897, EBI-1055615;
CC       Q9GZT8; Q15257-2: PTPA; NbExp=3; IntAct=EBI-740897, EBI-12164121;
CC       Q9GZT8; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-740897, EBI-712367;
CC       Q9GZT8; P21673: SAT1; NbExp=5; IntAct=EBI-740897, EBI-711613;
CC       Q9GZT8; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-740897, EBI-693002;
CC       Q9GZT8; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-740897, EBI-742688;
CC       Q9GZT8; O75716: STK16; NbExp=3; IntAct=EBI-740897, EBI-749295;
CC       Q9GZT8; P50226: SULT1A2; NbExp=3; IntAct=EBI-740897, EBI-6137631;
CC       Q9GZT8; P0DMM9: SULT1A3; NbExp=3; IntAct=EBI-740897, EBI-10196922;
CC       Q9GZT8; Q06520: SULT2A1; NbExp=3; IntAct=EBI-740897, EBI-3921363;
CC       Q9GZT8; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-740897, EBI-745392;
CC       Q9GZT8; P56279: TCL1A; NbExp=5; IntAct=EBI-740897, EBI-749995;
CC       Q9GZT8; P14373: TRIM27; NbExp=5; IntAct=EBI-740897, EBI-719493;
CC       Q9GZT8; Q15645: TRIP13; NbExp=3; IntAct=EBI-740897, EBI-358993;
CC       Q9GZT8; P10599: TXN; NbExp=3; IntAct=EBI-740897, EBI-594644;
CC       Q9GZT8; P07947: YES1; NbExp=3; IntAct=EBI-740897, EBI-515331;
CC       Q9GZT8; P14079: tax; Xeno; NbExp=3; IntAct=EBI-740897, EBI-9675698;
CC       Q9GZT8; Q85601; Xeno; NbExp=3; IntAct=EBI-740897, EBI-9676175;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11124544,
CC       ECO:0000269|PubMed:12951069}. Nucleus {ECO:0000250|UniProtKB:Q9EQ80}.
CC       Note=Interaction with COPS2 may regulate localization to the nucleus.
CC       {ECO:0000250|UniProtKB:Q9EQ80}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9GZT8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9GZT8-2; Sequence=VSP_029328;
CC       Name=3; Synonyms=beta;
CC         IsoId=Q9GZT8-3; Sequence=VSP_043248;
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG14952.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF283538; AAG44846.1; -; mRNA.
DR   EMBL; AB038949; BAB32499.1; -; mRNA.
DR   EMBL; AY251943; AAP84063.1; -; mRNA.
DR   EMBL; AF060513; AAG43131.1; -; mRNA.
DR   EMBL; AF182416; AAG14952.1; ALT_FRAME; mRNA.
DR   EMBL; AK023378; BAB14551.1; -; mRNA.
DR   EMBL; AC005037; AAY14724.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70224.1; -; Genomic_DNA.
DR   EMBL; BC007654; AAH07654.1; -; mRNA.
DR   CCDS; CCDS42797.1; -. [Q9GZT8-2]
DR   CCDS; CCDS46485.1; -. [Q9GZT8-1]
DR   CCDS; CCDS46486.1; -. [Q9GZT8-3]
DR   RefSeq; NP_001129511.1; NM_001136039.2. [Q9GZT8-1]
DR   RefSeq; NP_001135827.1; NM_001142355.1. [Q9GZT8-2]
DR   RefSeq; NP_001135828.1; NM_001142356.1. [Q9GZT8-3]
DR   RefSeq; NP_068596.2; NM_021824.3. [Q9GZT8-2]
DR   RefSeq; XP_005246799.1; XM_005246742.3.
DR   RefSeq; XP_011509884.1; XM_011511582.1.
DR   RefSeq; XP_011509885.1; XM_011511583.1.
DR   RefSeq; XP_011509886.1; XM_011511584.1.
DR   RefSeq; XP_011509887.1; XM_011511585.1.
DR   RefSeq; XP_016860119.1; XM_017004630.1.
DR   AlphaFoldDB; Q9GZT8; -.
DR   SMR; Q9GZT8; -.
DR   BioGRID; 121922; 173.
DR   IntAct; Q9GZT8; 113.
DR   MINT; Q9GZT8; -.
DR   STRING; 9606.ENSP00000386394; -.
DR   iPTMnet; Q9GZT8; -.
DR   MetOSite; Q9GZT8; -.
DR   PhosphoSitePlus; Q9GZT8; -.
DR   BioMuta; NIF3L1; -.
DR   DMDM; 160112850; -.
DR   EPD; Q9GZT8; -.
DR   jPOST; Q9GZT8; -.
DR   MassIVE; Q9GZT8; -.
DR   MaxQB; Q9GZT8; -.
DR   PaxDb; Q9GZT8; -.
DR   PeptideAtlas; Q9GZT8; -.
DR   PRIDE; Q9GZT8; -.
DR   ProteomicsDB; 80135; -. [Q9GZT8-1]
DR   ProteomicsDB; 80136; -. [Q9GZT8-2]
DR   ProteomicsDB; 80137; -. [Q9GZT8-3]
DR   Antibodypedia; 34126; 322 antibodies from 31 providers.
DR   DNASU; 60491; -.
DR   Ensembl; ENST00000359683.8; ENSP00000352711.4; ENSG00000196290.17. [Q9GZT8-2]
DR   Ensembl; ENST00000409020.6; ENSP00000386394.1; ENSG00000196290.17. [Q9GZT8-1]
DR   Ensembl; ENST00000409357.5; ENSP00000387315.1; ENSG00000196290.17. [Q9GZT8-1]
DR   Ensembl; ENST00000409588.1; ENSP00000387021.1; ENSG00000196290.17. [Q9GZT8-3]
DR   Ensembl; ENST00000651500.1; ENSP00000498853.1; ENSG00000196290.17. [Q9GZT8-1]
DR   GeneID; 60491; -.
DR   KEGG; hsa:60491; -.
DR   MANE-Select; ENST00000409020.6; ENSP00000386394.1; NM_001369441.2; NP_001356370.1.
DR   UCSC; uc002uwn.3; human. [Q9GZT8-1]
DR   CTD; 60491; -.
DR   DisGeNET; 60491; -.
DR   GeneCards; NIF3L1; -.
DR   HGNC; HGNC:13390; NIF3L1.
DR   HPA; ENSG00000196290; Low tissue specificity.
DR   MIM; 605778; gene.
DR   neXtProt; NX_Q9GZT8; -.
DR   OpenTargets; ENSG00000196290; -.
DR   PharmGKB; PA31629; -.
DR   VEuPathDB; HostDB:ENSG00000196290; -.
DR   eggNOG; KOG4131; Eukaryota.
DR   GeneTree; ENSGT00390000003590; -.
DR   HOGENOM; CLU_037423_0_0_1; -.
DR   InParanoid; Q9GZT8; -.
DR   OMA; EVAYDIY; -.
DR   PhylomeDB; Q9GZT8; -.
DR   TreeFam; TF324125; -.
DR   PathwayCommons; Q9GZT8; -.
DR   SignaLink; Q9GZT8; -.
DR   BioGRID-ORCS; 60491; 15 hits in 1082 CRISPR screens.
DR   GeneWiki; NIF3L1; -.
DR   GenomeRNAi; 60491; -.
DR   Pharos; Q9GZT8; Tbio.
DR   PRO; PR:Q9GZT8; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9GZT8; protein.
DR   Bgee; ENSG00000196290; Expressed in secondary oocyte and 201 other tissues.
DR   ExpressionAtlas; Q9GZT8; baseline and differential.
DR   Genevisible; Q9GZT8; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR017222; DUF34/NIF3_animal.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   PIRSF; PIRSF037490; UCP037490_NIF3_euk; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..377
FT                   /note="NIF3-like protein 1"
FT                   /id="PRO_0000147353"
FT   REGION          244..377
FT                   /note="Mediates interaction with COPS2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQ80"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         255
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQ80"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQ80"
FT   VAR_SEQ         1..27
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11161814,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4,
FT                   ECO:0000303|Ref.5"
FT                   /id="VSP_029328"
FT   VAR_SEQ         243..377
FT                   /note="PLLLHTGMGRLCTLDESVSLATMIDRIKRHLKLSHIRLALGVGRTLESQVKV
FT                   VALCAGSGSSVLQGVEADLYLTGEMSHHDTLDAASQGINVILCEHSNTERGFLSDLRDM
FT                   LDSHLENKINIILSETDRDPLQVV -> SLKSKSWPCVLVLGAAFCRVLRLTFTSQVRC
FT                   PIMILWMLLPKE (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_043248"
FT   VARIANT         324
FT                   /note="T -> I (in dbSNP:rs7917)"
FT                   /id="VAR_037084"
FT   CONFLICT        109
FT                   /note="K -> E (in Ref. 5; AAG14952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  41968 MW;  41BDCADDD81CA0D8 CRC64;
     MLSSCVRPVP TTVRFVDSLI CNSSRSFMDL KALLSSLNDF ASLSFAESWD NVGLLVEPSP
     PHTVNTLFLT NDLTEEVMEE VLQKKADLIL SYHPPIFRPM KRITWNTWKE RLVIRALENR
     VGIYSPHTAY DAAPQGVNNW LAKGLGACTS RPIHPSKAPN YPTEGNHRVE FNVNYTQDLD
     KVMSAVKGID GVSVTSFSAR TGNEEQTRIN LNCTQKALMQ VVDFLSRNKQ LYQKTEILSL
     EKPLLLHTGM GRLCTLDESV SLATMIDRIK RHLKLSHIRL ALGVGRTLES QVKVVALCAG
     SGSSVLQGVE ADLYLTGEMS HHDTLDAASQ GINVILCEHS NTERGFLSDL RDMLDSHLEN
     KINIILSETD RDPLQVV
 
 
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