Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha/beta hydrolase domain-containing protein 14B

Gene

ABHD14B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111Charge relay systemBy similarity
Active sitei162 – 1621Charge relay systemBy similarity
Active sitei188 – 1881Charge relay systemBy similarity

GO - Molecular functioni

  • hydrolase activity Source: UniProtKB

GO - Biological processi

  • metabolic process Source: GOC
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERihuman-CIB. CIB-CCG1-interacting-factor-B.
MEROPSiS33.983.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha/beta hydrolase domain-containing protein 14B (EC:3.-.-.-)
Short name:
Abhydrolase domain-containing protein 14B
Alternative name(s):
CCG1-interacting factor B
Gene namesi
Name:ABHD14B
Synonyms:CIB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:28235. ABHD14B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672660.

Polymorphism and mutation databases

BioMutaiABHD14B.
DMDMi34222621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 210209Alpha/beta hydrolase domain-containing protein 14BPRO_0000065038Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei91 – 911Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ96IU4.
PeptideAtlasiQ96IU4.
PRIDEiQ96IU4.

2D gel databases

OGPiQ96IU4.
REPRODUCTION-2DPAGEIPI00063827.
SWISS-2DPAGEQ96IU4.

PTM databases

PhosphoSiteiQ96IU4.

Expressioni

Tissue specificityi

Ubiquitous. Detected in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, placenta, lung, liver, skeletal muscle, pancreas and kidney.1 Publication

Gene expression databases

BgeeiQ96IU4.
CleanExiHS_ABHD14B.
ExpressionAtlasiQ96IU4. baseline and differential.
GenevisibleiQ96IU4. HS.

Organism-specific databases

HPAiHPA036444.
HPA036642.

Interactioni

Subunit structurei

May interact with TAF1.

Protein-protein interaction databases

MINTiMINT-5001888.
STRINGi9606.ENSP00000354841.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi12 – 143Combined sources
Beta strandi17 – 193Combined sources
Beta strandi21 – 255Combined sources
Beta strandi27 – 293Combined sources
Beta strandi34 – 374Combined sources
Helixi45 – 517Combined sources
Helixi53 – 597Combined sources
Beta strandi63 – 675Combined sources
Helixi73 – 753Combined sources
Helixi91 – 10010Combined sources
Beta strandi106 – 1105Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 1218Combined sources
Beta strandi129 – 1357Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 1485Combined sources
Beta strandi154 – 1596Combined sources
Helixi163 – 17210Combined sources
Beta strandi175 – 1839Combined sources
Helixi190 – 1934Combined sources
Helixi195 – 20713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IMJX-ray2.20A1-210[»]
ProteinModelPortaliQ96IU4.
SMRiQ96IU4. Positions 2-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96IU4.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. ABHD14 family.Curated

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00510000046860.
HOGENOMiHOG000028065.
HOVERGENiHBG001936.
InParanoidiQ96IU4.
KOiK13706.
OMAiVMKGAGH.
OrthoDBiEOG7WDN4H.
PhylomeDBiQ96IU4.
TreeFamiTF314465.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
IPR026764. ABHD14B.
[Graphical view]
PANTHERiPTHR10992:SF281. PTHR10992:SF281. 1 hit.
PfamiPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96IU4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASVEQREG TIQVQGQALF FREALPGSGQ ARFSVLLLHG IRFSSETWQN
60 70 80 90 100
LGTLHRLAQA GYRAVAIDLP GLGHSKEAAA PAPIGELAPG SFLAAVVDAL
110 120 130 140 150
ELGPPVVISP SLSGMYSLPF LTAPGSQLPG FVPVAPICTD KINAANYASV
160 170 180 190 200
KTPALIVYGD QDPMGQTSFE HLKQLPNHRV LIMKGAGHPC YLDKPEEWHT
210
GLLDFLQGLQ
Length:210
Mass (Da):22,346
Last modified:December 1, 2001 - v1
Checksum:i3CACE8759A2ADFAD
GO
Isoform 2 (identifier: Q96IU4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MAASVEQREG...AGYRAVAIDL → MGPGLFPAFLLRPQVTASTRLLPVCASPRSS

Note: No experimental confirmation available.
Show »
Length:172
Mass (Da):18,046
Checksum:i4C73568207B54B5C
GO

Sequence cautioni

The sequence AAH50650.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969MAASV…VAIDL → MGPGLFPAFLLRPQVTASTR LLPVCASPRSS in isoform 2. 1 PublicationVSP_008058Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075034 mRNA. Translation: BAC11366.1.
AK075112 mRNA. Translation: BAC11408.1.
AK096073 mRNA. Translation: BAC04696.1.
BC007234 mRNA. Translation: AAH07234.1.
BC050650 mRNA. Translation: AAH50650.1. Different initiation.
BC056411 mRNA. Translation: AAH56411.1.
CCDSiCCDS2842.1. [Q96IU4-1]
RefSeqiNP_001139786.1. NM_001146314.1. [Q96IU4-1]
NP_001241682.1. NM_001254753.1. [Q96IU4-2]
NP_116139.1. NM_032750.2. [Q96IU4-1]
XP_011532464.1. XM_011534162.1. [Q96IU4-1]
UniGeneiHs.420796.

Genome annotation databases

EnsembliENST00000361143; ENSP00000354841; ENSG00000114779.
ENST00000395008; ENSP00000378455; ENSG00000114779.
ENST00000483233; ENSP00000420065; ENSG00000114779.
ENST00000525795; ENSP00000433388; ENSG00000114779.
GeneIDi84836.
KEGGihsa:84836.
UCSCiuc003dcm.3. human. [Q96IU4-1]
uc021wza.1. human. [Q96IU4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075034 mRNA. Translation: BAC11366.1.
AK075112 mRNA. Translation: BAC11408.1.
AK096073 mRNA. Translation: BAC04696.1.
BC007234 mRNA. Translation: AAH07234.1.
BC050650 mRNA. Translation: AAH50650.1. Different initiation.
BC056411 mRNA. Translation: AAH56411.1.
CCDSiCCDS2842.1. [Q96IU4-1]
RefSeqiNP_001139786.1. NM_001146314.1. [Q96IU4-1]
NP_001241682.1. NM_001254753.1. [Q96IU4-2]
NP_116139.1. NM_032750.2. [Q96IU4-1]
XP_011532464.1. XM_011534162.1. [Q96IU4-1]
UniGeneiHs.420796.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IMJX-ray2.20A1-210[»]
ProteinModelPortaliQ96IU4.
SMRiQ96IU4. Positions 2-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-5001888.
STRINGi9606.ENSP00000354841.

Protein family/group databases

ESTHERihuman-CIB. CIB-CCG1-interacting-factor-B.
MEROPSiS33.983.

PTM databases

PhosphoSiteiQ96IU4.

Polymorphism and mutation databases

BioMutaiABHD14B.
DMDMi34222621.

2D gel databases

OGPiQ96IU4.
REPRODUCTION-2DPAGEIPI00063827.
SWISS-2DPAGEQ96IU4.

Proteomic databases

PaxDbiQ96IU4.
PeptideAtlasiQ96IU4.
PRIDEiQ96IU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361143; ENSP00000354841; ENSG00000114779.
ENST00000395008; ENSP00000378455; ENSG00000114779.
ENST00000483233; ENSP00000420065; ENSG00000114779.
ENST00000525795; ENSP00000433388; ENSG00000114779.
GeneIDi84836.
KEGGihsa:84836.
UCSCiuc003dcm.3. human. [Q96IU4-1]
uc021wza.1. human. [Q96IU4-2]

Organism-specific databases

CTDi84836.
GeneCardsiGC03M052003.
HGNCiHGNC:28235. ABHD14B.
HPAiHPA036444.
HPA036642.
neXtProtiNX_Q96IU4.
PharmGKBiPA142672660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00510000046860.
HOGENOMiHOG000028065.
HOVERGENiHBG001936.
InParanoidiQ96IU4.
KOiK13706.
OMAiVMKGAGH.
OrthoDBiEOG7WDN4H.
PhylomeDBiQ96IU4.
TreeFamiTF314465.

Miscellaneous databases

ChiTaRSiABHD14B. human.
EvolutionaryTraceiQ96IU4.
GenomeRNAii84836.
NextBioi75053.
PROiQ96IU4.

Gene expression databases

BgeeiQ96IU4.
CleanExiHS_ABHD14B.
ExpressionAtlasiQ96IU4. baseline and differential.
GenevisibleiQ96IU4. HS.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
IPR026764. ABHD14B.
[Graphical view]
PANTHERiPTHR10992:SF281. PTHR10992:SF281. 1 hit.
PfamiPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Kidney, Ovarian carcinoma and Placenta.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Skin.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Purification, crystallization and preliminary X-ray crystallographic analysis of human CCG1-interacting factor B."
    Padmanabhan B., Kuzuhara T., Mizuno H., Horikoshi M.
    Acta Crystallogr. D 56:1479-1481(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), INTERACTION WITH TAF1, SUBCELLULAR LOCATION.
  7. "The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB)."
    Padmanabhan B., Kuzuhara T., Adachi N., Horikoshi M.
    J. Biol. Chem. 279:9615-9624(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, ACTIVE SITE, SUBCELLULAR LOCATION, INTERACTION WITH TAF1, TISSUE SPECIFICITY.

Entry informationi

Entry nameiABHEB_HUMAN
AccessioniPrimary (citable) accession number: Q96IU4
Secondary accession number(s): Q86VK8, Q8N8W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.