Full text data of ABHD14B
ABHD14B
(CIB)
[Confidence: low (only semi-automatic identification from reviews)]
Alpha/beta hydrolase domain-containing protein 14B; Abhydrolase domain-containing protein 14B; 3.-.-.- (CCG1-interacting factor B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alpha/beta hydrolase domain-containing protein 14B; Abhydrolase domain-containing protein 14B; 3.-.-.- (CCG1-interacting factor B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96IU4
ID ABHEB_HUMAN Reviewed; 210 AA.
AC Q96IU4; Q86VK8; Q8N8W5;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 14B;
DE Short=Abhydrolase domain-containing protein 14B;
DE EC=3.-.-.-;
DE AltName: Full=CCG1-interacting factor B;
GN Name=ABHD14B; Synonyms=CIB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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.,
RA Buerckstuemmer T., 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, ACTIVE SITE,
RP SUBCELLULAR 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
RT (CIB).";
RL J. Biol. Chem. 279:9615-9624(2004).
CC -!- FUNCTION: Has hydrolase activity towards p-nitrophenyl butyrate
CC (in vitro). May activate transcription.
CC -!- SUBUNIT: May interact with TAF1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in spleen, thymus,
CC prostate, testis, ovary, small intestine, colon, peripheral blood
CC leukocyte, heart, placenta, lung, liver, skeletal muscle, pancreas
CC and kidney.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD14
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50650.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_001139786.1; NM_001146314.1.
DR RefSeq; NP_001241682.1; NM_001254753.1.
DR RefSeq; NP_116139.1; NM_032750.2.
DR RefSeq; XP_005265571.1; XM_005265514.1.
DR UniGene; Hs.420796; -.
DR PDB; 1IMJ; X-ray; 2.20 A; A=1-210.
DR PDBsum; 1IMJ; -.
DR ProteinModelPortal; Q96IU4; -.
DR SMR; Q96IU4; 2-209.
DR MINT; MINT-5001888; -.
DR MEROPS; S33.983; -.
DR PhosphoSite; Q96IU4; -.
DR DMDM; 34222621; -.
DR OGP; Q96IU4; -.
DR REPRODUCTION-2DPAGE; IPI00063827; -.
DR SWISS-2DPAGE; Q96IU4; -.
DR PaxDb; Q96IU4; -.
DR PeptideAtlas; Q96IU4; -.
DR PRIDE; Q96IU4; -.
DR Ensembl; ENST00000361143; ENSP00000354841; ENSG00000114779.
DR Ensembl; ENST00000395008; ENSP00000378455; ENSG00000114779.
DR Ensembl; ENST00000483233; ENSP00000420065; ENSG00000114779.
DR Ensembl; ENST00000525795; ENSP00000433388; ENSG00000114779.
DR GeneID; 84836; -.
DR KEGG; hsa:84836; -.
DR UCSC; uc003dcm.3; human.
DR CTD; 84836; -.
DR GeneCards; GC03M052003; -.
DR HGNC; HGNC:28235; ABHD14B.
DR HPA; HPA036444; -.
DR HPA; HPA036642; -.
DR neXtProt; NX_Q96IU4; -.
DR PharmGKB; PA142672660; -.
DR eggNOG; COG0596; -.
DR HOGENOM; HOG000028065; -.
DR HOVERGEN; HBG001936; -.
DR InParanoid; Q96IU4; -.
DR KO; K13706; -.
DR OMA; VMKGAGH; -.
DR OrthoDB; EOG7WDN4H; -.
DR PhylomeDB; Q96IU4; -.
DR ChiTaRS; ABHD14B; human.
DR EvolutionaryTrace; Q96IU4; -.
DR GenomeRNAi; 84836; -.
DR NextBio; 75053; -.
DR PRO; PR:Q96IU4; -.
DR ArrayExpress; Q96IU4; -.
DR Bgee; Q96IU4; -.
DR CleanEx; HS_ABHD14B; -.
DR Genevestigator; Q96IU4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR026764; ABHD14B.
DR PANTHER; PTHR10992:SF281; PTHR10992:SF281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 210 Alpha/beta hydrolase domain-containing
FT protein 14B.
FT /FTId=PRO_0000065038.
FT ACT_SITE 111 111 Charge relay system (By similarity).
FT ACT_SITE 162 162 Charge relay system (By similarity).
FT ACT_SITE 188 188 Charge relay system (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 69 MAASVEQREGTIQVQGQALFFREALPGSGQARFSVLLLHGI
FT RFSSETWQNLGTLHRLAQAGYRAVAIDL -> MGPGLFPAF
FT LLRPQVTASTRLLPVCASPRSS (in isoform 2).
FT /FTId=VSP_008058.
FT STRAND 5 7
FT STRAND 12 14
FT STRAND 17 19
FT STRAND 21 25
FT STRAND 27 29
FT STRAND 34 37
FT HELIX 45 51
FT HELIX 53 59
FT STRAND 63 67
FT HELIX 73 75
FT HELIX 91 100
FT STRAND 106 110
FT HELIX 111 113
FT HELIX 114 121
FT STRAND 129 135
FT HELIX 139 141
FT HELIX 144 148
FT STRAND 154 159
FT HELIX 163 172
FT STRAND 175 183
FT HELIX 190 193
FT HELIX 195 207
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
//
ID ABHEB_HUMAN Reviewed; 210 AA.
AC Q96IU4; Q86VK8; Q8N8W5;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 14B;
DE Short=Abhydrolase domain-containing protein 14B;
DE EC=3.-.-.-;
DE AltName: Full=CCG1-interacting factor B;
GN Name=ABHD14B; Synonyms=CIB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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.,
RA Buerckstuemmer T., 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, ACTIVE SITE,
RP SUBCELLULAR 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
RT (CIB).";
RL J. Biol. Chem. 279:9615-9624(2004).
CC -!- FUNCTION: Has hydrolase activity towards p-nitrophenyl butyrate
CC (in vitro). May activate transcription.
CC -!- SUBUNIT: May interact with TAF1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in spleen, thymus,
CC prostate, testis, ovary, small intestine, colon, peripheral blood
CC leukocyte, heart, placenta, lung, liver, skeletal muscle, pancreas
CC and kidney.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD14
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50650.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_001139786.1; NM_001146314.1.
DR RefSeq; NP_001241682.1; NM_001254753.1.
DR RefSeq; NP_116139.1; NM_032750.2.
DR RefSeq; XP_005265571.1; XM_005265514.1.
DR UniGene; Hs.420796; -.
DR PDB; 1IMJ; X-ray; 2.20 A; A=1-210.
DR PDBsum; 1IMJ; -.
DR ProteinModelPortal; Q96IU4; -.
DR SMR; Q96IU4; 2-209.
DR MINT; MINT-5001888; -.
DR MEROPS; S33.983; -.
DR PhosphoSite; Q96IU4; -.
DR DMDM; 34222621; -.
DR OGP; Q96IU4; -.
DR REPRODUCTION-2DPAGE; IPI00063827; -.
DR SWISS-2DPAGE; Q96IU4; -.
DR PaxDb; Q96IU4; -.
DR PeptideAtlas; Q96IU4; -.
DR PRIDE; Q96IU4; -.
DR Ensembl; ENST00000361143; ENSP00000354841; ENSG00000114779.
DR Ensembl; ENST00000395008; ENSP00000378455; ENSG00000114779.
DR Ensembl; ENST00000483233; ENSP00000420065; ENSG00000114779.
DR Ensembl; ENST00000525795; ENSP00000433388; ENSG00000114779.
DR GeneID; 84836; -.
DR KEGG; hsa:84836; -.
DR UCSC; uc003dcm.3; human.
DR CTD; 84836; -.
DR GeneCards; GC03M052003; -.
DR HGNC; HGNC:28235; ABHD14B.
DR HPA; HPA036444; -.
DR HPA; HPA036642; -.
DR neXtProt; NX_Q96IU4; -.
DR PharmGKB; PA142672660; -.
DR eggNOG; COG0596; -.
DR HOGENOM; HOG000028065; -.
DR HOVERGEN; HBG001936; -.
DR InParanoid; Q96IU4; -.
DR KO; K13706; -.
DR OMA; VMKGAGH; -.
DR OrthoDB; EOG7WDN4H; -.
DR PhylomeDB; Q96IU4; -.
DR ChiTaRS; ABHD14B; human.
DR EvolutionaryTrace; Q96IU4; -.
DR GenomeRNAi; 84836; -.
DR NextBio; 75053; -.
DR PRO; PR:Q96IU4; -.
DR ArrayExpress; Q96IU4; -.
DR Bgee; Q96IU4; -.
DR CleanEx; HS_ABHD14B; -.
DR Genevestigator; Q96IU4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR026764; ABHD14B.
DR PANTHER; PTHR10992:SF281; PTHR10992:SF281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 210 Alpha/beta hydrolase domain-containing
FT protein 14B.
FT /FTId=PRO_0000065038.
FT ACT_SITE 111 111 Charge relay system (By similarity).
FT ACT_SITE 162 162 Charge relay system (By similarity).
FT ACT_SITE 188 188 Charge relay system (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 69 MAASVEQREGTIQVQGQALFFREALPGSGQARFSVLLLHGI
FT RFSSETWQNLGTLHRLAQAGYRAVAIDL -> MGPGLFPAF
FT LLRPQVTASTRLLPVCASPRSS (in isoform 2).
FT /FTId=VSP_008058.
FT STRAND 5 7
FT STRAND 12 14
FT STRAND 17 19
FT STRAND 21 25
FT STRAND 27 29
FT STRAND 34 37
FT HELIX 45 51
FT HELIX 53 59
FT STRAND 63 67
FT HELIX 73 75
FT HELIX 91 100
FT STRAND 106 110
FT HELIX 111 113
FT HELIX 114 121
FT STRAND 129 135
FT HELIX 139 141
FT HELIX 144 148
FT STRAND 154 159
FT HELIX 163 172
FT STRAND 175 183
FT HELIX 190 193
FT HELIX 195 207
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
//