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O95870 (ABHGA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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:
Abhydrolase domain-containing protein 16A

EC=3.-.-.-
Alternative name(s):
HLA-B-associated transcript 5
Protein G5
Gene names
Name:ABHD16A
Synonyms:BAT5, G5, NG26
ORF Names:PP199
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the AB hydrolase superfamily. ABHD16 family.

Sequence caution

The sequence CAI17808.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAI18401.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAM26084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAM45793.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95870-1)

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: O95870-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: MAKLLSCVLG...PFAFFYLYRK → MPPPALFLSS...SLYSGELAGG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 558557Abhydrolase domain-containing protein 16A
PRO_0000064833

Regions

Transmembrane60 – 8021Helical; Potential
Transmembrane93 – 11321Helical; Potential

Sites

Active site3551Charge relay system By similarity
Active site4301Charge relay system By similarity
Active site5071Charge relay system By similarity

Natural variations

Alternative sequence1 – 8585MAKLL…YLYRK → MPPPALFLSSLYPRLEFQND FYRSCIRRSSPQPPPNLAWR PESLYSGELAGG in isoform 2.
VSP_043825

Experimental info

Sequence conflict271A → V in AAG22475. Ref.1

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: BC46EDA0725D44EA

FASTA55863,243
        10         20         30         40         50         60 
MAKLLSCVLG PRLYKIYRER DSERAPASVP ETPTAVTAPH SSSWDTYYQP RALEKHADSI 

        70         80         90        100        110        120 
LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT 

       130        140        150        160        170        180 
NPQYRQFITI LEATHRNQSS ENKRQLANYN FDFRSWPVDF HWEEPSSRKE SRGGPSRRGV 

       190        200        210        220        230        240 
ALLRPEPLHR GTADTLLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG 

       250        260        270        280        290        300 
QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP 

       310        320        330        340        350        360 
LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDII IYAWSIGGFT 

       370        380        390        400        410        420 
ATWAAMSYPD VSAMILDASF DDLVPLALKV MPDSWRGLVT RTVRQHLNLN NAEQLCRYQG 

       430        440        450        460        470        480 
PVLLIRRTKD EIITTTVPED IMSNRGNDLL LKLLQHRYPR VMAEEGLRVV RQWLEASSQL 

       490        500        510        520        530        540 
EEASIYSRWE VEEDWCLSVL RSYQAEHGPD FPWSVGEDMS ADGRRQLALF LARKHLHNFE 

       550 
ATHCTPLPAQ NFQMPWHL 

« Hide

Isoform 2 [UniParc].

Checksum: A69C57A1A3550711
Show »

FASTA52559,383

References

« Hide 'large scale' references
[1]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"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: Teratocarcinoma.
[3]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Brain.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12 (ISOFORM 1).
Tissue: Platelet.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF193047 mRNA. Translation: AAG22475.1.
AK001207 mRNA. Translation: BAA91553.1.
AK023194 mRNA. Translation: BAB14455.1.
AK297712 mRNA. Translation: BAH12652.1.
AF129756 Genomic DNA. Translation: AAD18079.1.
BA000025 Genomic DNA. Translation: BAB63383.1.
AL662899 Genomic DNA. Translation: CAI18401.2. Different initiation.
AL670886 Genomic DNA. Translation: CAI17808.2. Different initiation.
AL805934 Genomic DNA. Translation: CAI18530.1.
BX248244, BX511262 Genomic DNA. Translation: CAM26084.1. Different initiation.
BX511262, BX248244 Genomic DNA. Translation: CAM45793.1. Different initiation.
CR354443 Genomic DNA. No translation available.
CR753842 Genomic DNA. No translation available.
CR759761 Genomic DNA. No translation available.
CR759787 Genomic DNA. No translation available.
BC031839 mRNA. Translation: AAH31839.1.
CCDSCCDS4713.1. [O95870-1]
CCDS54988.1. [O95870-2]
RefSeqNP_001170986.1. NM_001177515.1. [O95870-2]
NP_066983.1. NM_021160.2. [O95870-1]
UniGeneHs.388188.

3D structure databases

ProteinModelPortalO95870.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113650. 14 interactions.
IntActO95870. 16 interactions.
MINTMINT-1032766.

Chemistry

BindingDBO95870.
ChEMBLCHEMBL6168.

Protein family/group databases

MEROPSS09.065.

PTM databases

PhosphoSiteO95870.

Proteomic databases

MaxQBO95870.
PaxDbO95870.
PRIDEO95870.

Protocols and materials databases

DNASU7920.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395952; ENSP00000379282; ENSG00000204427. [O95870-1]
ENST00000440843; ENSP00000410347; ENSG00000204427. [O95870-2]
ENST00000446529; ENSP00000395665; ENSG00000206403. [O95870-1]
ENST00000546528; ENSP00000446494; ENSG00000224552. [O95870-1]
ENST00000547161; ENSP00000448497; ENSG00000235676. [O95870-1]
ENST00000547325; ENSP00000447271; ENSG00000236063. [O95870-1]
ENST00000548592; ENSP00000448431; ENSG00000206403. [O95870-2]
ENST00000549543; ENSP00000449006; ENSG00000231488. [O95870-1]
ENST00000549722; ENSP00000447549; ENSG00000230475. [O95870-2]
ENST00000549853; ENSP00000447846; ENSG00000236063. [O95870-2]
ENST00000550556; ENSP00000447498; ENSG00000235676. [O95870-2]
ENST00000550719; ENSP00000449881; ENSG00000230475. [O95870-1]
ENST00000551038; ENSP00000449579; ENSG00000231488. [O95870-2]
ENST00000552042; ENSP00000448451; ENSG00000224552. [O95870-2]
GeneID7920.
KEGGhsa:7920.
UCSCuc003nvx.2. human. [O95870-1]
uc011dny.2. human. [O95870-2]

Organism-specific databases

CTD7920.
GeneCardsGC06M031665.
GC06Mj31642.
GC06Mk31636.
GC06Ml31694.
GC06Mm31731.
GC06Mn31644.
GC06Mo31644.
H-InvDBHIX0016012.
HIX0040568.
HGNCHGNC:13921. ABHD16A.
HPAHPA058606.
MIM142620. gene.
neXtProtNX_O95870.
PharmGKBPA25266.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1073.
HOVERGENHBG050666.
InParanoidO95870.
PhylomeDBO95870.
TreeFamTF314267.

Gene expression databases

ArrayExpressO95870.
BgeeO95870.
CleanExHS_BAT5.
GenevestigatorO95870.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
IPR026604. ABHD16A.
[Graphical view]
PANTHERPTHR12277:SF54. PTHR12277:SF54. 1 hit.
PfamPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

ChiTaRSABHD16A. human.
GeneWikiBAT5.
GenomeRNAi7920.
NextBio30411.
PROO95870.
SOURCESearch...

Entry information

Entry nameABHGA_HUMAN
AccessionPrimary (citable) accession number: O95870
Secondary accession number(s): A2BEY3 expand/collapse secondary AC list , B7Z4R6, Q5SRR1, Q5SRR2, Q8WYH0, Q9NW33
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM