ABHEB_HUMAN
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 03-AUG-2022, entry version 164.
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, 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};
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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; 13.
DR IntAct; Q96IU4; 6.
DR STRING; 9606.ENSP00000420065; -.
DR ESTHER; human-CIB; CIB-CCG1-interacting-factor-B.
DR MEROPS; S33.983; -.
DR iPTMnet; Q96IU4; -.
DR MetOSite; Q96IU4; -.
DR PhosphoSitePlus; Q96IU4; -.
DR BioMuta; ABHD14B; -.
DR DMDM; 34222621; -.
DR OGP; Q96IU4; -.
DR REPRODUCTION-2DPAGE; IPI00063827; -.
DR SWISS-2DPAGE; Q96IU4; -.
DR EPD; Q96IU4; -.
DR jPOST; Q96IU4; -.
DR MassIVE; Q96IU4; -.
DR MaxQB; Q96IU4; -.
DR PaxDb; Q96IU4; -.
DR PeptideAtlas; Q96IU4; -.
DR PRIDE; Q96IU4; -.
DR ProteomicsDB; 76854; -. [Q96IU4-1]
DR ProteomicsDB; 76855; -. [Q96IU4-2]
DR TopDownProteomics; Q96IU4-1; -. [Q96IU4-1]
DR Antibodypedia; 46121; 252 antibodies from 30 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 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; VPIAPIC; -.
DR PhylomeDB; Q96IU4; -.
DR TreeFam; TF314465; -.
DR BioCyc; MetaCyc:ENSG00000114779-MON; -.
DR PathwayCommons; Q96IU4; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR SignaLink; Q96IU4; -.
DR BioGRID-ORCS; 84836; 13 hits in 1080 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 168 other tissues.
DR ExpressionAtlas; Q96IU4; baseline and differential.
DR Genevisible; Q96IU4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
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
