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HIG1A_MOUSE
ID   HIG1A_MOUSE             Reviewed;          95 AA.
AC   Q9JLR9;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=HIG1 domain family member 1A, mitochondrial;
DE   AltName: Full=Hypoxia-inducible gene 1 protein;
GN   Name=Higd1a; Synonyms=Hig1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schindler C., Denko N.C., Koong A.C., Giaccia A.J.;
RT   "Murine HIG1 - a novel hypoxia-induced gene.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RA   Wang J., Steiner D.F.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Liver, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV),
CC       which is the terminal component of the mitochondrial respiratory chain
CC       that catalyzes the reduction of oxygen to water. May play a role in the
CC       assembly of respiratory supercomplexes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associates with cytochrome c oxidase (COX, complex IV);
CC       proposed complex component. Also associates with respiratory chain
CC       supercomplexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00836}. Mitochondrion inner membrane {ECO:0000250}.
CC   -!- INDUCTION: By hypoxia.
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DR   EMBL; AF141312; AAF25721.1; -; mRNA.
DR   EMBL; AY028386; AAK21982.1; -; mRNA.
DR   EMBL; AK004166; BAB23202.1; -; mRNA.
DR   EMBL; AK008756; BAB25877.1; -; mRNA.
DR   EMBL; AK018360; BAB31176.1; -; mRNA.
DR   EMBL; BC021594; AAH21594.1; -; mRNA.
DR   EMBL; BC090259; AAH90259.1; -; mRNA.
DR   CCDS; CCDS40812.1; -.
DR   RefSeq; NP_062788.1; NM_019814.4.
DR   RefSeq; XP_006512264.1; XM_006512201.1.
DR   AlphaFoldDB; Q9JLR9; -.
DR   SMR; Q9JLR9; -.
DR   BioGRID; 207883; 1.
DR   STRING; 10090.ENSMUSP00000054881; -.
DR   iPTMnet; Q9JLR9; -.
DR   PhosphoSitePlus; Q9JLR9; -.
DR   EPD; Q9JLR9; -.
DR   jPOST; Q9JLR9; -.
DR   MaxQB; Q9JLR9; -.
DR   PaxDb; Q9JLR9; -.
DR   PRIDE; Q9JLR9; -.
DR   ProteomicsDB; 269752; -.
DR   Antibodypedia; 45649; 117 antibodies from 27 providers.
DR   DNASU; 56295; -.
DR   Ensembl; ENSMUST00000060251; ENSMUSP00000054881; ENSMUSG00000038412.
DR   Ensembl; ENSMUST00000213124; ENSMUSP00000149531; ENSMUSG00000038412.
DR   Ensembl; ENSMUST00000215300; ENSMUSP00000150726; ENSMUSG00000038412.
DR   GeneID; 56295; -.
DR   KEGG; mmu:56295; -.
DR   UCSC; uc009seb.2; mouse.
DR   CTD; 25994; -.
DR   MGI; MGI:1930666; Higd1a.
DR   VEuPathDB; HostDB:ENSMUSG00000038412; -.
DR   eggNOG; KOG4431; Eukaryota.
DR   GeneTree; ENSGT00940000154276; -.
DR   HOGENOM; CLU_153308_2_0_1; -.
DR   InParanoid; Q9JLR9; -.
DR   OMA; EPVYPEY; -.
DR   OrthoDB; 1581485at2759; -.
DR   PhylomeDB; Q9JLR9; -.
DR   TreeFam; TF314628; -.
DR   BioGRID-ORCS; 56295; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Higd1a; mouse.
DR   PRO; PR:Q9JLR9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JLR9; protein.
DR   Bgee; ENSMUSG00000038412; Expressed in facial nucleus and 248 other tissues.
DR   ExpressionAtlas; Q9JLR9; baseline and differential.
DR   Genevisible; Q9JLR9; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:CACAO.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IDA:MGI.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR   GO; GO:0097250; P:mitochondrial respirasome assembly; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:MGI.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:MGI.
DR   InterPro; IPR007667; Hypoxia_induced_domain.
DR   Pfam; PF04588; HIG_1_N; 1.
DR   PROSITE; PS51503; HIG1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW   Respiratory chain; Stress response; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y241"
FT   CHAIN           2..95
FT                   /note="HIG1 domain family member 1A, mitochondrial"
FT                   /id="PRO_0000215771"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT   DOMAIN          2..93
FT                   /note="HIG1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y241"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VH49"
SQ   SEQUENCE   95 AA;  10425 MW;  B94465D57AB0E3E7 CRC64;
     MSTNTDLSLS SYDEGQGSKF IRKAKETPFV PIGMAGFAAI VAYGLYKLKS RGNTKMSIHL
     IHMRVAAQGF VVGAMTLGMG YSMYQEFWAN PKPKP
 
 
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