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FA72A_HUMAN
ID   FA72A_HUMAN             Reviewed;         149 AA.
AC   Q5TYM5; B2RV15; Q5TYM4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Protein FAM72A;
DE   AltName: Full=Latent membrane protein 1-induced protein;
DE            Short=LMP1-induced protein;
DE            Short=LMPIP;
GN   Name=FAM72A; Synonyms=UGENE;
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 [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   [2]
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   [3]
RP   INTERACTION WITH UNG, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF TRP-125.
RX   PubMed=18676834; DOI=10.1158/0008-5472.can-08-1259;
RA   Guo C., Zhang X., Fink S.P., Platzer P., Wilson K., Willson J.K., Wang Z.,
RA   Markowitz S.D.;
RT   "Ugene, a newly identified protein that is commonly overexpressed in cancer
RT   and binds uracil DNA glycosylase.";
RL   Cancer Res. 68:6118-6126(2008).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY EBV INFECTION.
RX   PubMed=21317926; DOI=10.1038/onc.2011.16;
RA   Wang L.T., Lin C.S., Chai C.Y., Liu K.Y., Chen J.Y., Hsu S.H.;
RT   "Functional interaction of Ugene and EBV infection mediates tumorigenic
RT   effects.";
RL   Oncogene 30:2921-2932(2011).
CC   -!- FUNCTION: May play a role in the regulation of cellular reactive oxygen
CC       species metabolism. May participate in cell growth regulation.
CC       {ECO:0000269|PubMed:21317926}.
CC   -!- SUBUNIT: Interacts with UNG. {ECO:0000269|PubMed:18676834}.
CC   -!- INTERACTION:
CC       Q5TYM5; Q15777: MPPED2; NbExp=3; IntAct=EBI-10237116, EBI-2350461;
CC       Q5TYM5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10237116, EBI-741158;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=A V5 epitope-
CC       tagged construct has been shown to localize to the nucleus
CC       (PubMed:18676834). 5-7% of total FAM72A is associated with mitochondria
CC       around the nucleus in HEK293 cells (PubMed:21317926).
CC       {ECO:0000269|PubMed:18676834, ECO:0000269|PubMed:21317926}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ugene-p;
CC         IsoId=Q5TYM5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5TYM5-2; Sequence=VSP_034205;
CC   -!- TISSUE SPECIFICITY: May be up-regulated in malignant colon cancers,
CC       compared to normal colon and colon adenomas. Expression is also
CC       elevated in other common cancer types, including breast, lung, uterus,
CC       and ovary. {ECO:0000269|PubMed:18676834}.
CC   -!- INDUCTION: Up-regulated in peripheral blood mononuclear cells following
CC       Epstein-Barr virus (EBV) infection or following transfection with EBV
CC       LMP1 protein. {ECO:0000269|PubMed:21317926}.
CC   -!- MISCELLANEOUS: Highly homologous to GCUD2 but localized to a distinct
CC       locus.
CC   -!- SIMILARITY: Belongs to the FAM72 family. {ECO:0000305}.
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DR   EMBL; CR407567; CAH72365.1; -; Genomic_DNA.
DR   EMBL; CR407567; CAH72366.1; -; Genomic_DNA.
DR   EMBL; BC035696; AAH35696.1; -; mRNA.
DR   EMBL; BC146978; AAI46979.1; -; mRNA.
DR   EMBL; BC146992; AAI46993.1; -; mRNA.
DR   CCDS; CCDS73016.1; -. [Q5TYM5-1]
DR   RefSeq; NP_001116640.1; NM_001123168.2. [Q5TYM5-1]
DR   RefSeq; NP_001304830.1; NM_001317901.1.
DR   RefSeq; XP_011508269.1; XM_011509967.1. [Q5TYM5-2]
DR   AlphaFoldDB; Q5TYM5; -.
DR   BioGRID; 609932; 2.
DR   IntAct; Q5TYM5; 2.
DR   STRING; 9606.ENSP00000356096; -.
DR   iPTMnet; Q5TYM5; -.
DR   PhosphoSitePlus; Q5TYM5; -.
DR   BioMuta; FAM72A; -.
DR   DMDM; 74746671; -.
DR   PaxDb; Q5TYM5; -.
DR   PeptideAtlas; Q5TYM5; -.
DR   PRIDE; Q5TYM5; -.
DR   Antibodypedia; 47104; 34 antibodies from 12 providers.
DR   DNASU; 729533; -.
DR   Ensembl; ENST00000341209.9; ENSP00000340661.5; ENSG00000196550.11. [Q5TYM5-2]
DR   Ensembl; ENST00000367128.8; ENSP00000356096.3; ENSG00000196550.11. [Q5TYM5-1]
DR   GeneID; 729533; -.
DR   KEGG; hsa:729533; -.
DR   MANE-Select; ENST00000367128.8; ENSP00000356096.3; NM_001123168.3; NP_001116640.1.
DR   UCSC; uc001hdr.5; human. [Q5TYM5-1]
DR   CTD; 729533; -.
DR   DisGeNET; 729533; -.
DR   GeneCards; FAM72A; -.
DR   HGNC; HGNC:24044; FAM72A.
DR   HPA; ENSG00000196550; Tissue enhanced (lymphoid).
DR   MIM; 614710; gene.
DR   neXtProt; NX_Q5TYM5; -.
DR   OpenTargets; ENSG00000196550; -.
DR   PharmGKB; PA142671833; -.
DR   VEuPathDB; HostDB:ENSG00000196550; -.
DR   eggNOG; ENOG502S1HA; Eukaryota.
DR   GeneTree; ENSGT00390000005106; -.
DR   HOGENOM; CLU_2176611_0_0_1; -.
DR   InParanoid; Q5TYM5; -.
DR   OMA; DICKCKL; -.
DR   PhylomeDB; Q5TYM5; -.
DR   TreeFam; TF329231; -.
DR   PathwayCommons; Q5TYM5; -.
DR   SignaLink; Q5TYM5; -.
DR   BioGRID-ORCS; 729533; 45 hits in 294 CRISPR screens.
DR   ChiTaRS; FAM72A; human.
DR   GenomeRNAi; 729533; -.
DR   Pharos; Q5TYM5; Tbio.
DR   PRO; PR:Q5TYM5; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5TYM5; protein.
DR   Bgee; ENSG00000196550; Expressed in ventricular zone and 95 other tissues.
DR   ExpressionAtlas; Q5TYM5; baseline and differential.
DR   Genevisible; Q5TYM5; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   InterPro; IPR026768; FAM72.
DR   PANTHER; PTHR31841; PTHR31841; 1.
DR   Pfam; PF14976; FAM72; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Mitochondrion; Reference proteome.
FT   CHAIN           1..149
FT                   /note="Protein FAM72A"
FT                   /id="PRO_0000340256"
FT   VAR_SEQ         11..51
FT                   /note="RCVSILCCKFCKQVLSSRGMKAVLLADTEIDLFSTDIPPTN -> S (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034205"
FT   MUTAGEN         125
FT                   /note="W->R: Loss of UNG-binding."
FT                   /evidence="ECO:0000269|PubMed:18676834"
SQ   SEQUENCE   149 AA;  16619 MW;  EB55B1921DED9EBB CRC64;
     MSTNICSFKD RCVSILCCKF CKQVLSSRGM KAVLLADTEI DLFSTDIPPT NAVDFTGRCY
     FTKICKCKLK DIACLKCGNI VGYHVIVPCS SCLLSCNNGH FWMFHSQAVY DINRLDSTGV
     NVLLWGNLPE IEESTDEDVL NISAEECIR
 
 
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