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SEHL2_HUMAN
ID   SEHL2_HUMAN             Reviewed;         314 AA.
AC   Q9H4I8; B1AHE9; B1AHF0; Q0VDJ1; Q5H973; Q9BR29; Q9BR30; Q9Y3I9;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Serine hydrolase-like protein 2;
DE            EC=3.1.-.-;
GN   Name=SERHL2; Synonyms=SERHL;
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 MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Kidney, and Testis;
RX   PubMed=12529303; DOI=10.1101/gr.695703;
RA   Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA   Bye J.M., Beare D.M., Dunham I.;
RT   "Reevaluating human gene annotation: a second-generation analysis of
RT   chromosome 22.";
RL   Genome Res. 13:27-36(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC   -!- FUNCTION: Probable serine hydrolase. May be related to cell muscle
CC       hypertrophy.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC       Peroxisome {ECO:0000250}. Note=Concentrated in perinuclear vesicles.
CC       May be located in peroxisomes. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q9H4I8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H4I8-2; Sequence=VSP_003968, VSP_003969;
CC       Name=3;
CC         IsoId=Q9H4I8-3; Sequence=VSP_003970;
CC   -!- MISCELLANEOUS: This gene may have been partially duplicated (see
CC       SERHL).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AL450314; CAC16804.1; -; mRNA.
DR   EMBL; AL590120; CAC34873.1; -; mRNA.
DR   EMBL; AL590118; CAC34871.1; -; mRNA.
DR   EMBL; AL589866; CAC34477.1; -; mRNA.
DR   EMBL; Z93241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC119650; AAI19651.1; -; mRNA.
DR   EMBL; BC127635; AAI27636.1; -; mRNA.
DR   EMBL; BC127636; AAI27637.1; -; mRNA.
DR   CCDS; CCDS14037.1; -. [Q9H4I8-1]
DR   CCDS; CCDS63498.1; -. [Q9H4I8-2]
DR   RefSeq; NP_001271263.1; NM_001284334.1. [Q9H4I8-2]
DR   RefSeq; NP_055324.2; NM_014509.4. [Q9H4I8-1]
DR   AlphaFoldDB; Q9H4I8; -.
DR   SMR; Q9H4I8; -.
DR   BioGRID; 128960; 8.
DR   IntAct; Q9H4I8; 6.
DR   STRING; 9606.ENSP00000331376; -.
DR   ESTHER; human-SERHL2; SERHL.
DR   MEROPS; S33.012; -.
DR   iPTMnet; Q9H4I8; -.
DR   PhosphoSitePlus; Q9H4I8; -.
DR   BioMuta; SERHL2; -.
DR   DMDM; 21362935; -.
DR   MassIVE; Q9H4I8; -.
DR   PaxDb; Q9H4I8; -.
DR   PeptideAtlas; Q9H4I8; -.
DR   PRIDE; Q9H4I8; -.
DR   ProteomicsDB; 80845; -. [Q9H4I8-1]
DR   ProteomicsDB; 80846; -. [Q9H4I8-2]
DR   ProteomicsDB; 80847; -. [Q9H4I8-3]
DR   Antibodypedia; 45931; 62 antibodies from 12 providers.
DR   DNASU; 253190; -.
DR   Ensembl; ENST00000327678.10; ENSP00000331376.5; ENSG00000183569.18. [Q9H4I8-1]
DR   Ensembl; ENST00000335879.5; ENSP00000336578.5; ENSG00000183569.18. [Q9H4I8-2]
DR   Ensembl; ENST00000407614.8; ENSP00000385691.4; ENSG00000183569.18. [Q9H4I8-3]
DR   GeneID; 253190; -.
DR   KEGG; hsa:253190; -.
DR   MANE-Select; ENST00000327678.10; ENSP00000331376.5; NM_014509.5; NP_055324.2.
DR   UCSC; uc003bcr.5; human. [Q9H4I8-1]
DR   CTD; 253190; -.
DR   DisGeNET; 253190; -.
DR   GeneCards; SERHL2; -.
DR   HGNC; HGNC:29446; SERHL2.
DR   HPA; ENSG00000183569; Tissue enriched (breast).
DR   MIM; 619045; gene.
DR   neXtProt; NX_Q9H4I8; -.
DR   OpenTargets; ENSG00000183569; -.
DR   PharmGKB; PA142670935; -.
DR   VEuPathDB; HostDB:ENSG00000183569; -.
DR   eggNOG; KOG1454; Eukaryota.
DR   GeneTree; ENSGT00530000063960; -.
DR   HOGENOM; CLU_135400_0_0_1; -.
DR   InParanoid; Q9H4I8; -.
DR   OMA; RGLMPVP; -.
DR   OrthoDB; 1285824at2759; -.
DR   PhylomeDB; Q9H4I8; -.
DR   TreeFam; TF326547; -.
DR   PathwayCommons; Q9H4I8; -.
DR   SignaLink; Q9H4I8; -.
DR   BioGRID-ORCS; 253190; 14 hits in 1071 CRISPR screens.
DR   ChiTaRS; SERHL2; human.
DR   GenomeRNAi; 253190; -.
DR   Pharos; Q9H4I8; Tdark.
DR   PRO; PR:Q9H4I8; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9H4I8; protein.
DR   Bgee; ENSG00000183569; Expressed in oocyte and 105 other tissues.
DR   ExpressionAtlas; Q9H4I8; baseline and differential.
DR   Genevisible; Q9H4I8; HS.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Peroxisome; Reference proteome.
FT   CHAIN           1..314
FT                   /note="Serine hydrolase-like protein 2"
FT                   /id="PRO_0000097692"
FT   DOMAIN          33..293
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         8..57
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12529303"
FT                   /id="VSP_003968"
FT   VAR_SEQ         12..191
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12529303"
FT                   /id="VSP_003970"
FT   VAR_SEQ         96..109
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12529303"
FT                   /id="VSP_003969"
FT   VARIANT         3
FT                   /note="E -> K (in dbSNP:rs3213549)"
FT                   /id="VAR_051334"
FT   VARIANT         46
FT                   /note="S -> N (in dbSNP:rs926333)"
FT                   /id="VAR_021962"
FT   VARIANT         306
FT                   /note="C -> R (in dbSNP:rs137055)"
FT                   /id="VAR_051335"
SQ   SEQUENCE   314 AA;  35369 MW;  2572F470136E4427 CRC64;
     MSENAAPGLI SELKLAVPWG HIAAKAWGSL QGPPVLCLHG WLDNASSFDR LIPLLPQDFY
     YVAMDFGGHG LSSHYSPGVP YYLQTFVSEI RRVVAALKWN RFSILGHSFG GVVGGMFFCT
     FPEMVDKLIL LDTPLFLLES DEMENLLTYK RRAIEHVLQV EASQEPSHVF SLKQLLQRLL
     KSNSHLSEEC GELLLQRGTT KVATGLVLNR DQRLAWAENS IDFISRELCA HSIRKLQAHV
     LLIKAVHGYF DSRQNYSEKE SLSFMIDTMK STLKEQFQFV EVPGNHCVHM SEPQHVASII
     SSFLQCTHML PAQL
 
 
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