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Protein

Alpha/beta hydrolase domain-containing protein 13

Gene

ABHD13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei193 – 1931Charge relay systemBy similarity
Active sitei268 – 2681Charge relay systemBy similarity
Active sitei298 – 2981Charge relay systemBy similarity

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

MEROPSiS09.051.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha/beta hydrolase domain-containing protein 13 (EC:3.-.-.-)
Short name:
Abhydrolase domain-containing protein 13
Gene namesi
Name:ABHD13
Synonyms:C13orf6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20293. ABHD13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei37 – 5721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134862303.

Polymorphism and mutation databases

BioMutaiABHD13.
DMDMi74749881.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Alpha/beta hydrolase domain-containing protein 13PRO_0000281076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ7L211.
PaxDbiQ7L211.
PeptideAtlasiQ7L211.
PRIDEiQ7L211.

PTM databases

PhosphoSiteiQ7L211.

Expressioni

Gene expression databases

BgeeiQ7L211.
CleanExiHS_ABHD13.
ExpressionAtlasiQ7L211. baseline and differential.
GenevestigatoriQ7L211.

Organism-specific databases

HPAiHPA032143.
HPA032144.

Interactioni

Protein-protein interaction databases

IntActiQ7L211. 1 interaction.
STRINGi9606.ENSP00000365063.

Structurei

3D structure databases

ProteinModelPortaliQ7L211.
SMRiQ7L211. Positions 81-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the serine esterase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1073.
GeneTreeiENSGT00390000000948.
HOGENOMiHOG000007143.
HOVERGENiHBG080816.
InParanoidiQ7L211.
KOiK06889.
OMAiNKQHARN.
OrthoDBiEOG789CBW.
PhylomeDBiQ7L211.
TreeFamiTF315122.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
[Graphical view]
PfamiPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7L211-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSWMLWNF VERWLIALAS WSWALCRISL LPLIVTFHLY GGIILLLLIF
60 70 80 90 100
ISIAGILYKF QDVLLYFPEQ PSSSRLYVPM PTGIPHENIF IRTKDGIRLN
110 120 130 140 150
LILIRYTGDN SPYSPTIIYF HGNAGNIGHR LPNALLMLVN LKVNLLLVDY
160 170 180 190 200
RGYGKSEGEA SEEGLYLDSE AVLDYVMTRP DLDKTKIFLF GRSLGGAVAI
210 220 230 240 250
HLASENSHRI SAIMVENTFL SIPHMASTLF SFFPMRYLPL WCYKNKFLSY
260 270 280 290 300
RKISQCRMPS LFISGLSDQL IPPVMMKQLY ELSPSRTKRL AIFPDGTHND
310 320 330
TWQCQGYFTA LEQFIKEVVK SHSPEEMAKT SSNVTII
Length:337
Mass (Da):38,548
Last modified:October 11, 2004 - v1
Checksum:iD8298BF81784827F
GO

Sequence cautioni

The sequence AAH70226.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AK075195 differs from that shown. Reason: Erroneous termination at position 167. Translated as Leu.Curated
The sequence BAB55387.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431I → V in AK075195 (PubMed:16303743).Curated
Sequence conflicti80 – 801M → I in AK075195 (PubMed:16303743).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027812 mRNA. Translation: BAB55387.1. Different initiation.
AK124864 mRNA. Translation: BAG54109.1.
AK075195 mRNA. No translation available.
AL157762 Genomic DNA. Translation: CAH70630.1.
CH471085 Genomic DNA. Translation: EAX09097.1.
BC022566 mRNA. Translation: AAH22566.2.
BC070226 mRNA. Translation: AAH70226.1. Different initiation.
CCDSiCCDS32007.1.
RefSeqiNP_116248.2. NM_032859.2.
UniGeneiHs.183528.

Genome annotation databases

EnsembliENST00000375898; ENSP00000365063; ENSG00000139826.
GeneIDi84945.
KEGGihsa:84945.
UCSCiuc001vqq.3. human.

Polymorphism and mutation databases

BioMutaiABHD13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027812 mRNA. Translation: BAB55387.1. Different initiation.
AK124864 mRNA. Translation: BAG54109.1.
AK075195 mRNA. No translation available.
AL157762 Genomic DNA. Translation: CAH70630.1.
CH471085 Genomic DNA. Translation: EAX09097.1.
BC022566 mRNA. Translation: AAH22566.2.
BC070226 mRNA. Translation: AAH70226.1. Different initiation.
CCDSiCCDS32007.1.
RefSeqiNP_116248.2. NM_032859.2.
UniGeneiHs.183528.

3D structure databases

ProteinModelPortaliQ7L211.
SMRiQ7L211. Positions 81-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7L211. 1 interaction.
STRINGi9606.ENSP00000365063.

Protein family/group databases

MEROPSiS09.051.

PTM databases

PhosphoSiteiQ7L211.

Polymorphism and mutation databases

BioMutaiABHD13.
DMDMi74749881.

Proteomic databases

MaxQBiQ7L211.
PaxDbiQ7L211.
PeptideAtlasiQ7L211.
PRIDEiQ7L211.

Protocols and materials databases

DNASUi84945.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375898; ENSP00000365063; ENSG00000139826.
GeneIDi84945.
KEGGihsa:84945.
UCSCiuc001vqq.3. human.

Organism-specific databases

CTDi84945.
GeneCardsiGC13P108870.
HGNCiHGNC:20293. ABHD13.
HPAiHPA032143.
HPA032144.
neXtProtiNX_Q7L211.
PharmGKBiPA134862303.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1073.
GeneTreeiENSGT00390000000948.
HOGENOMiHOG000007143.
HOVERGENiHBG080816.
InParanoidiQ7L211.
KOiK06889.
OMAiNKQHARN.
OrthoDBiEOG789CBW.
PhylomeDBiQ7L211.
TreeFamiTF315122.

Miscellaneous databases

GenomeRNAii84945.
NextBioi75418.
PROiQ7L211.

Gene expression databases

BgeeiQ7L211.
CleanExiHS_ABHD13.
ExpressionAtlasiQ7L211. baseline and differential.
GenevestigatoriQ7L211.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
[Graphical view]
PfamiPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].
    Tissue: Hippocampus and Placenta.
  2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain.

Entry informationi

Entry nameiABHDD_HUMAN
AccessioniPrimary (citable) accession number: Q7L211
Secondary accession number(s): B3KWE7, Q8NBW1, Q96JX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2004
Last modified: April 29, 2015
This is version 110 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. 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.