ABH15_HUMAN
ID ABH15_HUMAN Reviewed; 468 AA.
AC Q6UXT9; Q96EC5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein ABHD15 {ECO:0000305};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 15 {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 15 {ECO:0000312|HGNC:HGNC:26971};
DE Flags: Precursor;
GN Name=ABHD15 {ECO:0000312|HGNC:HGNC:26971}; ORFNames=UNQ6510/PRO21435;
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], AND VARIANT ALA-334.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-334.
RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- INTERACTION:
CC Q6UXT9; O76011: KRT34; NbExp=3; IntAct=EBI-2824666, EBI-1047093;
CC Q6UXT9; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2824666, EBI-11522433;
CC Q6UXT9; P21673: SAT1; NbExp=3; IntAct=EBI-2824666, EBI-711613;
CC Q6UXT9; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-2824666, EBI-11957238;
CC Q6UXT9; Q15007: WTAP; NbExp=3; IntAct=EBI-2824666, EBI-751647;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {ECO:0000305}.
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DR EMBL; AY358212; AAQ88579.1; -; mRNA.
DR EMBL; AC104564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012476; AAH12476.2; -; mRNA.
DR CCDS; CCDS32602.1; -.
DR RefSeq; NP_937790.2; NM_198147.2.
DR AlphaFoldDB; Q6UXT9; -.
DR BioGRID; 125492; 37.
DR IntAct; Q6UXT9; 15.
DR STRING; 9606.ENSP00000302657; -.
DR ESTHER; human-ABHD15; abh_upf0017.
DR iPTMnet; Q6UXT9; -.
DR PhosphoSitePlus; Q6UXT9; -.
DR BioMuta; ABHD15; -.
DR DMDM; 308153403; -.
DR EPD; Q6UXT9; -.
DR jPOST; Q6UXT9; -.
DR MassIVE; Q6UXT9; -.
DR MaxQB; Q6UXT9; -.
DR PaxDb; Q6UXT9; -.
DR PeptideAtlas; Q6UXT9; -.
DR PRIDE; Q6UXT9; -.
DR ProteomicsDB; 67657; -.
DR Antibodypedia; 2595; 51 antibodies from 19 providers.
DR DNASU; 116236; -.
DR Ensembl; ENST00000307201.5; ENSP00000302657.3; ENSG00000168792.5.
DR GeneID; 116236; -.
DR KEGG; hsa:116236; -.
DR MANE-Select; ENST00000307201.5; ENSP00000302657.3; NM_198147.3; NP_937790.2.
DR UCSC; uc002hed.3; human.
DR CTD; 116236; -.
DR DisGeNET; 116236; -.
DR GeneCards; ABHD15; -.
DR HGNC; HGNC:26971; ABHD15.
DR HPA; ENSG00000168792; Tissue enhanced (liver).
DR neXtProt; NX_Q6UXT9; -.
DR OpenTargets; ENSG00000168792; -.
DR PharmGKB; PA164714659; -.
DR VEuPathDB; HostDB:ENSG00000168792; -.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR HOGENOM; CLU_032487_3_0_1; -.
DR InParanoid; Q6UXT9; -.
DR OMA; WKRSYTK; -.
DR OrthoDB; 1162019at2759; -.
DR PhylomeDB; Q6UXT9; -.
DR TreeFam; TF332985; -.
DR PathwayCommons; Q6UXT9; -.
DR SignaLink; Q6UXT9; -.
DR BioGRID-ORCS; 116236; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; ABHD15; human.
DR GenomeRNAi; 116236; -.
DR Pharos; Q6UXT9; Tdark.
DR PRO; PR:Q6UXT9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6UXT9; protein.
DR Bgee; ENSG00000168792; Expressed in granulocyte and 120 other tissues.
DR Genevisible; Q6UXT9; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..468
FT /note="Protein ABHD15"
FT /id="PRO_0000345395"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 391
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 334
FT /note="T -> A (in dbSNP:rs542939)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_045821"
FT CONFLICT 287
FT /note="H -> Y (in Ref. 3; AAH12476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 51771 MW; A910F5F4294B0CC3 CRC64;
MPPWGAALAL ILAVLALLGL LGPRLRGPWG RAVGERTLPG AQDRDDGEEA DGGGPADQFS
DGREPLPGGC SLVCKPSALA QCLLRALRRS EALEAGPRSW FSGPHLQTLC HFVLPVAPGP
ELAREYLQLA DDGLVALDWV VGPCVRGRRI TSAGGLPAVL LVIPNAWGRL TRNVLGLCLL
ALERGYYPVI FHRRGHHGCP LVSPRLQPFG DPSDLKEAVT YIRFRHPAAP LFAVSEGSGS
ALLLSYLGEC GSSSYVTGAA CISPVLRCRE WFEAGLPWPY ERGFLLHQKI ALSRYATALE
DTVDTSRLFR SRSLREFEEA LFCHTKSFPI SWDTYWDRND PLRDVDEAAV PVLCICSADD
PVCGPPDHTL TTELFHSNPY FFLLLSRHGG HCGFLRQEPL PAWSHEVILE SFRALTEFFR
TEERIKGLSR HRASFLGGRR RGGALQRREV SSSSNLEEIF NWKRSYTR
