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Q2TAA2 (IAH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoamyl acetate-hydrolyzing esterase 1 homolog

EC=3.1.-.-
Gene names
Name:IAH1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable lipase By similarity.

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family. IAH1 subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionhydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Isoamyl acetate-hydrolyzing esterase 1 homolog
PRO_0000315723

Sites

Active site241Nucleophile By similarity
Active site1961 By similarity
Active site1991 By similarity
Binding site561Substrate; via amide nitrogen By similarity
Binding site891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2TAA2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: B21C1C0EC9F69778

FASTA24827,599
        10         20         30         40         50         60 
MALCEAAGCG SALLWPRLLL FGDSITQFSF QQGGWGASLA DRLVRKCDVL NRGFSGYNTR 

        70         80         90        100        110        120 
WAKIILPRLI RKGNSLDIPV AVTIFFGAND SALKDENPKQ HIPLEEYAAN LKSMVQYLKS 

       130        140        150        160        170        180 
VDIPENRVIL ITPTPLCETA WEEQCIIQGC KLNRLNSVVG EYANACLQVA QDCGTDVLDL 

       190        200        210        220        230        240 
WTLMQDSQDF SSYLSDGLHL SPKGNEFLFS HLWPLIEKKV SSLPLLLPYW RDVAEAKPEL 


SLLGDGDH 

« Hide

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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK291984 mRNA. Translation: BAF84673.1.
CH471053 Genomic DNA. Translation: EAX00983.1.
BC111025 mRNA. Translation: AAI11026.1.
IPIIPI00419194.
RefSeqNP_001034702.1. NM_001039613.1.
UniGeneHs.570189.

3D structure databases

ProteinModelPortalQ2TAA2.
SMRQ2TAA2. Positions 13-235.
ModBaseSearch...

Polymorphism databases

DMDM121941741.

2D gel databases

REPRODUCTION-2DPAGEIPI00419194.

Proteomic databases

PRIDEQ2TAA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000497473; ENSP00000417580; ENSG00000134330.
GeneID285148.
KEGGhsa:285148.
UCSCuc002qzr.1. human.

Organism-specific databases

CTD285148.
GeneCardsGC02P009533.
HGNCHGNC:27696. IAH1.
neXtProtNX_Q2TAA2.
PharmGKBPA162391893.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00390000008069.
HOGENOMHBG618579.
HOVERGENHBG105140.
InParanoidQ2TAA2.
OMAITQFSFQ.
PhylomeDBQ2TAA2.

Gene expression databases

ArrayExpressQ2TAA2.
BgeeQ2TAA2.
CleanExHS_IAH1.
GenevestigatorQ2TAA2.

Family and domain databases

InterProIPR013830. Esterase_SGNH_hydro-type.
IPR013831. Esterase_SGNH_hydro-type_subgr.
IPR001087. Lipase_GDSL.
[Graphical view]
Gene3DG3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit.
PfamPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
SUPFAMSSF52266. Esterase_SGNH_hydro-type. 1 hit.
PROSITEPS01098. LIPASE_GDSL_SER. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio95297.

Entry information

Entry nameIAH1_HUMAN
AccessionPrimary (citable) accession number: Q2TAA2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: December 14, 2011
This is version 56 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

Human chromosome 2

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

SIMILARITY comments

Index of protein domains and families