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Q96IU4 (ABHEB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha/beta hydrolase domain-containing protein 14B

Short name=Abhydrolase domain-containing protein 14B
EC=3.-.-.-
Alternative name(s):
CCG1-interacting factor B
Gene names
Name:ABHD14B
Synonyms:CIB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription. Ref.6

Subunit structure

May interact with TAF1.

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Ref.5 Ref.6

Tissue specificity

Ubiquitous. Detected in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, placenta, lung, liver, skeletal muscle, pancreas and kidney. Ref.6

Sequence similarities

Belongs to the AB hydrolase superfamily. ABHD14 family.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96IU4-1)

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.
Isoform 2 (identifier: Q96IU4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MAASVEQREG...AGYRAVAIDL → MGPGLFPAFLLRPQVTASTRLLPVCASPRSS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 210209Alpha/beta hydrolase domain-containing protein 14B
PRO_0000065038

Sites

Active site1111Charge relay system By similarity
Active site1621Charge relay system By similarity
Active site1881Charge relay system By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Natural variations

Alternative sequence1 – 6969MAASV…VAIDL → MGPGLFPAFLLRPQVTASTR LLPVCASPRSS in isoform 2.
VSP_008058

Secondary structure

........................................... 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 3CACE8759A2ADFAD

FASTA21022,346
        10         20         30         40         50         60 
MAASVEQREG TIQVQGQALF FREALPGSGQ ARFSVLLLHG IRFSSETWQN LGTLHRLAQA 

        70         80         90        100        110        120 
GYRAVAIDLP GLGHSKEAAA PAPIGELAPG SFLAAVVDAL ELGPPVVISP SLSGMYSLPF 

       130        140        150        160        170        180 
LTAPGSQLPG FVPVAPICTD KINAANYASV KTPALIVYGD QDPMGQTSFE HLKQLPNHRV 

       190        200        210 
LIMKGAGHPC YLDKPEEWHT GLLDFLQGLQ 

« Hide

Isoform 2 [UniParc].

Checksum: 4C73568207B54B5C
Show »

FASTA17218,046

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[5]"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.
[6]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2842.1. [Q96IU4-1]
RefSeqNP_001139786.1. NM_001146314.1. [Q96IU4-1]
NP_001241682.1. NM_001254753.1. [Q96IU4-2]
NP_116139.1. NM_032750.2. [Q96IU4-1]
UniGeneHs.420796.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IMJX-ray2.20A1-210[»]
ProteinModelPortalQ96IU4.
SMRQ96IU4. Positions 2-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124289. 1 interaction.
MINTMINT-5001888.

Protein family/group databases

MEROPSS33.983.

PTM databases

PhosphoSiteQ96IU4.

Polymorphism databases

DMDM34222621.

2D gel databases

OGPQ96IU4.
REPRODUCTION-2DPAGEIPI00063827.
SWISS-2DPAGEQ96IU4.

Proteomic databases

MaxQBQ96IU4.
PaxDbQ96IU4.
PeptideAtlasQ96IU4.
PRIDEQ96IU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361143; ENSP00000354841; ENSG00000114779. [Q96IU4-1]
ENST00000395008; ENSP00000378455; ENSG00000114779. [Q96IU4-1]
ENST00000483233; ENSP00000420065; ENSG00000114779. [Q96IU4-1]
ENST00000525795; ENSP00000433388; ENSG00000114779. [Q96IU4-1]
GeneID84836.
KEGGhsa:84836.
UCSCuc003dcm.3. human. [Q96IU4-1]
uc021wza.1. human. [Q96IU4-2]

Organism-specific databases

CTD84836.
GeneCardsGC03M052003.
HGNCHGNC:28235. ABHD14B.
HPAHPA036444.
HPA036642.
neXtProtNX_Q96IU4.
PharmGKBPA142672660.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0596.
HOGENOMHOG000028065.
HOVERGENHBG001936.
InParanoidQ96IU4.
KOK13706.
OMAAPICTEK.
OrthoDBEOG7WDN4H.
PhylomeDBQ96IU4.
TreeFamTF314465.

Gene expression databases

ArrayExpressQ96IU4.
BgeeQ96IU4.
CleanExHS_ABHD14B.
GenevestigatorQ96IU4.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
IPR026764. ABHD14B.
[Graphical view]
PANTHERPTHR10992:SF281. PTHR10992:SF281. 1 hit.
PfamPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

ChiTaRSABHD14B. human.
EvolutionaryTraceQ96IU4.
GenomeRNAi84836.
NextBio75053.
PROQ96IU4.

Entry information

Entry nameABHEB_HUMAN
AccessionPrimary (citable) accession number: Q96IU4
Secondary accession number(s): Q86VK8, Q8N8W5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM