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Q6DHV7 (ADAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosine deaminase-like protein

EC=3.5.4.-
Gene names
Name:ADAL
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Putative nucleoside deaminase. May catalyze the hydrolytic deamination of adenosine or some similar substrate and play a role in purine metabolism By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6DHV7-1)

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: Q6DHV7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     258-355: ELCLTSNVKS...NHLKPRVLHI → GKAWSFRSSR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Adenosine deaminase-like protein
PRO_0000285090

Sites

Active site2111Proton donor By similarity
Metal binding241Zinc; catalytic By similarity
Metal binding261Zinc; catalytic By similarity
Metal binding2081Zinc; catalytic By similarity
Metal binding2931Zinc; catalytic By similarity
Binding site261Substrate By similarity
Binding site1811Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site2941Substrate By similarity
Site2321Important for catalytic activity By similarity

Natural variations

Alternative sequence258 – 35598ELCLT…RVLHI → GKAWSFRSSR in isoform 2.
VSP_024821

Experimental info

Sequence conflict1191K → E in AK126583. Ref.3
Sequence conflict1391I → T in AK126583. Ref.3

Sequences

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

Last modified May 1, 2007. Version 2.
Checksum: 02810E9BC5F56CD5

FASTA35540,264
        10         20         30         40         50         60 
MIEAEEQQPC KTDFYSELPK VELHAHLNGS ISSHTMKKLI AQKPDLKIHD QMTVIDKGKK 

        70         80         90        100        110        120 
RTLEECFQMF QTIHQLTSSP EDILMVTKDV IKEFADDGVK YLELRSTPRR ENATGMTKKT 

       130        140        150        160        170        180 
YVESILEGIK QSKQENLDID VRYLIAVDRR GGPLVAKETV KLAEEFFLST EGTVLGLDLS 

       190        200        210        220        230        240 
GDPTVGQAKD FLEPLLEAKK AGLKLALHLS EIPNQKKETQ ILLDLLPDRI GHGTFLNSGE 

       250        260        270        280        290        300 
GGSLDLVDFV RQHRIPLELC LTSNVKSQTV PSYDQHHFGF WYSIAHPSVI CTDDKGVFAT 

       310        320        330        340        350 
HLSQEYQLAA ETFNLTQSQV WDLSYESINY IFASDSTRSE LRKKWNHLKP RVLHI 

« Hide

Isoform 2 [UniParc].

Checksum: C4ED476D40B4C512
Show »

FASTA26730,040

References

[1]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed: 16572171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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] OF 92-355 (ISOFORM 1).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC018924 Genomic DNA. No translation available.
AC009852 Genomic DNA. No translation available.
BC075857 mRNA. Translation: AAH75857.1.
AK126583 mRNA. No translation available.
IPIIPI00238031.
IPI00783550.
RefSeqNP_001012987.1. NM_001012969.2.
NP_001152752.1. NM_001159280.1.
UniGeneHs.533913.

3D structure databases

ProteinModelPortalQ6DHV7.
SMRQ6DHV7. Positions 17-348.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6DHV7.

Polymorphism databases

DMDM146286026.

Proteomic databases

PRIDEQ6DHV7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000422466; ENSP00000398744; ENSG00000168803.
GeneID161823.
KEGGhsa:161823.
NMPDRfig|9606.3.peg.10595.
UCSCuc001zrh.1. human.
uc001zri.1. human.

Organism-specific databases

CTD161823.
GeneCardsGC15P043622.
HGNCHGNC:31853. ADAL.
neXtProtNX_Q6DHV7.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11044.
GeneTreeENSGT00510000047133.
HOGENOMHBG630382.
HOVERGENHBG055638.
InParanoidQ6DHV7.
OMAGIKQCKQ.
OrthoDBEOG43N7D3.
PhylomeDBQ6DHV7.

Gene expression databases

ArrayExpressQ6DHV7.
BgeeQ6DHV7.
CleanExHS_ADAL.
GenevestigatorQ6DHV7.

Family and domain databases

InterProIPR001365. A/AMP_deaminase_dom.
[Graphical view]
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
PROSITEPS00485. A_DEAMINASE. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio88114.

Entry information

Entry nameADAL_HUMAN
AccessionPrimary (citable) accession number: Q6DHV7
Secondary accession number(s): A6NHZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: January 25, 2012
This is version 59 of the entry and version 2 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 15

Human chromosome 15: entries, gene names and cross-references to MIM

SIMILARITY comments

Index of protein domains and families