ID ABHEB_HUMAN Reviewed; 210 AA. AC Q96IU4; Q86VK8; Q8N8W5; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Putative protein-lysine deacylase ABHD14B {ECO:0000305}; DE EC=2.3.1.- {ECO:0000305|PubMed:31478652}; DE AltName: Full=Alpha/beta hydrolase domain-containing protein 14B {ECO:0000305}; DE Short=Abhydrolase domain-containing protein 14B {ECO:0000312|HGNC:HGNC:28235}; DE AltName: Full=CCG1-interacting factor B {ECO:0000303|PubMed:11053859}; GN Name=ABHD14B {ECO:0000303|PubMed:31478652, GN ECO:0000312|HGNC:HGNC:28235}; GN Synonyms=CIB {ECO:0000303|PubMed:11053859}; 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 AND 2). RC TISSUE=Kidney, Ovarian carcinoma, and Placenta; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and 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 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 [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP 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). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF SER-111. RX PubMed=31478652; DOI=10.1021/acs.biochem.9b00703; RA Rajendran A., Vaidya K., Mendoza J., Bridwell-Rabb J., Kamat S.S.; RT "Functional annotation of ABHD14B, an orphan serine hydrolase enzyme."; RL Biochemistry 59:183-196(2020). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), INTERACTION WITH TAF1, AND RP SUBCELLULAR LOCATION. RX PubMed=11053859; DOI=10.1107/s0907444900010957; RA Padmanabhan B., Kuzuhara T., Mizuno H., Horikoshi M.; RT "Purification, crystallization and preliminary X-ray crystallographic RT analysis of human CCG1-interacting factor B."; RL Acta Crystallogr. D 56:1479-1481(2000). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, ACTIVE SITES, SUBCELLULAR RP LOCATION, INTERACTION WITH TAF1, AND TISSUE SPECIFICITY. RX PubMed=14672934; DOI=10.1074/jbc.m312165200; RA Padmanabhan B., Kuzuhara T., Adachi N., Horikoshi M.; RT "The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB)."; RL J. Biol. Chem. 279:9615-9624(2004). CC -!- FUNCTION: Acts as an atypical protein-lysine deacetylase in vitro CC (PubMed:31478652). Catalyzes the deacetylation of lysine residues using CC CoA as substrate, generating acetyl-CoA and the free amine of protein- CC lysine residues (PubMed:31478652). Additional experiments are however CC required to confirm the protein-lysine deacetylase activity in vivo CC (Probable). Has hydrolase activity towards various surrogate p- CC nitrophenyl (pNp) substrates, such as pNp-butyrate, pNp-acetate and CC pNp-octanoate in vitro, with a strong preference for pNp-acetate CC (PubMed:31478652, PubMed:14672934). May activate transcription CC (PubMed:14672934). {ECO:0000269|PubMed:14672934, CC ECO:0000269|PubMed:31478652, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000305|PubMed:31478652}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45950; CC Evidence={ECO:0000305|PubMed:31478652}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.8 mM for p-nitrophenyl-acetate {ECO:0000269|PubMed:31478652}; CC KM=3.1 mM for p-nitrophenyl-butyrate {ECO:0000269|PubMed:31478652}; CC KM=3.9 mM for p-nitrophenyl-octanoate {ECO:0000269|PubMed:31478652}; CC Note=kcat is 2.2 min(-1) for p-nitrophenyl-acetate (PubMed:31478652). CC kcat is 0.6 min(-1) for p-nitrophenyl-butyrate (PubMed:31478652). CC kcat is 0.2 min(-1) for p-nitrophenyl-octanoate (PubMed:31478652). CC {ECO:0000269|PubMed:31478652}; CC -!- SUBUNIT: May interact with TAF1. {ECO:0000269|PubMed:11053859, CC ECO:0000269|PubMed:14672934}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11053859, CC ECO:0000269|PubMed:14672934, ECO:0000269|PubMed:31478652}. Nucleus CC {ECO:0000269|PubMed:11053859, ECO:0000269|PubMed:14672934, CC ECO:0000269|PubMed:31478652}. Note=Predominantly cytoplasmic. CC {ECO:0000269|PubMed:14672934}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96IU4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96IU4-2; Sequence=VSP_008058; CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:14672934). Detected in spleen, CC thymus, prostate, testis, ovary, small intestine, colon, peripheral CC blood leukocyte, heart, placenta, lung, liver, skeletal muscle, CC pancreas and kidney (PubMed:14672934). {ECO:0000269|PubMed:14672934}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD14 family. CC {ECO:0000305}. CC -!- CAUTION: The protein-lysine deacetylase activity using CoA as substrate CC is unclear as this protein belongs to a family of serine hydrolases, CC and that the reaction shown in the publication is not hydrolyzing CC H(2)O. Additional experiments are therefore required to confirm this CC activity in vivo. {ECO:0000305|PubMed:31478652}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50650.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK075034; BAC11366.1; -; mRNA. DR EMBL; AK075112; BAC11408.1; -; mRNA. DR EMBL; AK096073; BAC04696.1; -; mRNA. DR EMBL; BC007234; AAH07234.1; -; mRNA. DR EMBL; BC050650; AAH50650.1; ALT_INIT; mRNA. DR EMBL; BC056411; AAH56411.1; -; mRNA. DR CCDS; CCDS2842.1; -. [Q96IU4-1] DR RefSeq; NP_001139786.1; NM_001146314.1. [Q96IU4-1] DR RefSeq; NP_001241682.1; NM_001254753.1. [Q96IU4-2] DR RefSeq; NP_116139.1; NM_032750.2. [Q96IU4-1] DR PDB; 1IMJ; X-ray; 2.20 A; A=1-210. DR PDBsum; 1IMJ; -. DR AlphaFoldDB; Q96IU4; -. DR SMR; Q96IU4; -. DR BioGRID; 124289; 26. DR IntAct; Q96IU4; 6. DR STRING; 9606.ENSP00000420065; -. DR ESTHER; human-CIB; CIB-CCG1-interacting-factor-B. DR MEROPS; S33.983; -. DR GlyGen; Q96IU4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96IU4; -. DR MetOSite; Q96IU4; -. DR PhosphoSitePlus; Q96IU4; -. DR BioMuta; ABHD14B; -. DR DMDM; 34222621; -. DR OGP; Q96IU4; -. DR REPRODUCTION-2DPAGE; IPI00063827; -. DR EPD; Q96IU4; -. DR jPOST; Q96IU4; -. DR MassIVE; Q96IU4; -. DR MaxQB; Q96IU4; -. DR PaxDb; 9606-ENSP00000420065; -. DR PeptideAtlas; Q96IU4; -. DR ProteomicsDB; 76854; -. [Q96IU4-1] DR ProteomicsDB; 76855; -. [Q96IU4-2] DR Pumba; Q96IU4; -. DR TopDownProteomics; Q96IU4-1; -. [Q96IU4-1] DR Antibodypedia; 46121; 274 antibodies from 31 providers. DR DNASU; 84836; -. DR Ensembl; ENST00000361143.10; ENSP00000354841.5; ENSG00000114779.20. [Q96IU4-1] DR Ensembl; ENST00000395008.6; ENSP00000378455.2; ENSG00000114779.20. [Q96IU4-1] DR Ensembl; ENST00000483233.5; ENSP00000420065.1; ENSG00000114779.20. [Q96IU4-1] DR Ensembl; ENST00000525795.1; ENSP00000433388.1; ENSG00000114779.20. [Q96IU4-1] DR GeneID; 84836; -. DR KEGG; hsa:84836; -. DR MANE-Select; ENST00000361143.10; ENSP00000354841.5; NM_001146314.2; NP_001139786.1. DR AGR; HGNC:28235; -. DR CTD; 84836; -. DR DisGeNET; 84836; -. DR GeneCards; ABHD14B; -. DR HGNC; HGNC:28235; ABHD14B. DR HPA; ENSG00000114779; Low tissue specificity. DR neXtProt; NX_Q96IU4; -. DR OpenTargets; ENSG00000114779; -. DR PharmGKB; PA142672660; -. DR VEuPathDB; HostDB:ENSG00000114779; -. DR eggNOG; ENOG502QR0B; Eukaryota. DR GeneTree; ENSGT00940000159388; -. DR HOGENOM; CLU_020336_28_0_1; -. DR InParanoid; Q96IU4; -. DR OMA; HACYLHN; -. DR OrthoDB; 2963153at2759; -. DR PhylomeDB; Q96IU4; -. DR TreeFam; TF314465; -. DR BioCyc; MetaCyc:ENSG00000114779-MONOMER; -. DR PathwayCommons; Q96IU4; -. DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules. DR SignaLink; Q96IU4; -. DR BioGRID-ORCS; 84836; 13 hits in 1167 CRISPR screens. DR ChiTaRS; ABHD14B; human. DR EvolutionaryTrace; Q96IU4; -. DR GenomeRNAi; 84836; -. DR Pharos; Q96IU4; Tdark. DR PRO; PR:Q96IU4; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q96IU4; Protein. DR Bgee; ENSG00000114779; Expressed in ileal mucosa and 169 other cell types or tissues. DR ExpressionAtlas; Q96IU4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IEA:RHEA. DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR46197; PROTEIN ABHD14B-LIKE; 1. DR PANTHER; PTHR46197:SF2; PROTEIN-LYSINE DEACYLASE ABHD14B-RELATED; 1. DR Pfam; PF12697; Abhydrolase_6; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SWISS-2DPAGE; Q96IU4; -. DR Genevisible; Q96IU4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing; KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..210 FT /note="Putative protein-lysine deacylase ABHD14B" FT /id="PRO_0000065038" FT ACT_SITE 111 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:14672934, FT ECO:0000305|PubMed:31478652" FT ACT_SITE 162 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:14672934" FT ACT_SITE 188 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:14672934" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..69 FT /note="MAASVEQREGTIQVQGQALFFREALPGSGQARFSVLLLHGIRFSSETWQNLG FT TLHRLAQAGYRAVAIDL -> MGPGLFPAFLLRPQVTASTRLLPVCASPRSS (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_008058" FT MUTAGEN 111 FT /note="S->A: Abolished protein-lysine deacetylase activity FT in vitro." FT /evidence="ECO:0000269|PubMed:31478652" FT STRAND 5..7 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 21..25 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 45..51 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 53..59 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 114..121 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 144..148 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 163..172 FT /evidence="ECO:0007829|PDB:1IMJ" FT STRAND 175..183 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 190..193 FT /evidence="ECO:0007829|PDB:1IMJ" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:1IMJ" SQ SEQUENCE 210 AA; 22346 MW; 3CACE8759A2ADFAD CRC64; MAASVEQREG TIQVQGQALF FREALPGSGQ ARFSVLLLHG IRFSSETWQN LGTLHRLAQA GYRAVAIDLP GLGHSKEAAA PAPIGELAPG SFLAAVVDAL ELGPPVVISP SLSGMYSLPF LTAPGSQLPG FVPVAPICTD KINAANYASV KTPALIVYGD QDPMGQTSFE HLKQLPNHRV LIMKGAGHPC YLDKPEEWHT GLLDFLQGLQ //