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P23109 (AMPD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
AMP deaminase 1

EC=3.5.4.6
Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase
Gene names
Name:AMPD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AMP deaminase plays a critical role in energy metabolism.

Catalytic activity

AMP + H2O = IMP + NH3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.

Subunit structure

Homotetramer.

Tissue specificity

Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.

Involvement in disease

Myopathy due to myoadenylate deaminase deficiency (MMDD) [MIM:615511]: A metabolic disorder resulting in exercise-related myopathy. It is characterized by exercise-induced muscle aches, cramps, and early fatigue.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Caution

It is uncertain whether Met-1 or Met-34 is the initiator.

Sequence caution

The sequence AAA57281.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAG24258.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAF84038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG36918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAI18828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23109-1)

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: P23109-2)

The sequence of this isoform differs from the canonical sequence as follows:
     41-45: AEEKQ → E

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 780780AMP deaminase 1
PRO_0000194403

Regions

Region407 – 4126Substrate binding By similarity
Region683 – 6864Substrate binding By similarity

Sites

Active site6271Proton acceptor By similarity
Metal binding3361Zinc; catalytic By similarity
Metal binding3381Zinc; catalytic By similarity
Metal binding6051Zinc; catalytic By similarity
Metal binding6821Zinc; catalytic By similarity
Binding site3381Substrate By similarity
Binding site6081Substrate By similarity

Natural variations

Alternative sequence41 – 455AEEKQ → E in isoform 2.
VSP_042638
Natural variant551E → K.
Corresponds to variant rs2273268 [ dbSNP | Ensembl ].
VAR_048860
Natural variant811P → L Polymorphism; activity comparable to wild-type. Ref.6
Corresponds to variant rs61752479 [ dbSNP | Ensembl ].
VAR_013270
Natural variant4211R → W in MMDD; loss of activity. Ref.7
Corresponds to variant rs35859650 [ dbSNP | Ensembl ].
VAR_013271
Natural variant4581R → H in MMDD; loss of activity. Ref.7
VAR_013272
Natural variant6661P → H in a colorectal cancer sample; somatic mutation. Ref.8
VAR_035801

Experimental info

Sequence conflict2341P → S in BAF84038. Ref.5
Sequence conflict3061V → A in BAF84038. Ref.5
Sequence conflict4671D → G in BAG36918. Ref.5
Sequence conflict4751W → R in BAF84038. Ref.5
Sequence conflict6591F → S in BAF84038. Ref.5

Sequences

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

Last modified April 18, 2012. Version 2.
Checksum: 2449E96D00312629

FASTA78090,219
        10         20         30         40         50         60 
MNVRIFYSVS QSPHSLLSLL FYCAILESRI SATMPLFKLP AEEKQIDDAM RNFAEKVFAS 

        70         80         90        100        110        120 
EVKDEGGRQE ISPFDVDEIC PISHHEMQAH IFHLETLSTS TEARRKKRFQ GRKTVNLSIP 

       130        140        150        160        170        180 
LSETSSTKLS HIDEYISSSP TYQTVPDFQR VQITGDYASG VTVEDFEIVC KGLYRALCIR 

       190        200        210        220        230        240 
EKYMQKSFQR FPKTPSKYLR NIDGEAWVAN ESFYPVFTPP VKKGEDPFRT DNLPENLGYH 

       250        260        270        280        290        300 
LKMKDGVVYV YPNEAAVSKD EPKPLPYPNL DTFLDDMNFL LALIAQGPVK TYTHRRLKFL 

       310        320        330        340        350        360 
SSKFQVHQML NEMDELKELK NNPHRDFYNC RKVDTHIHAA ACMNQKHLLR FIKKSYQIDA 

       370        380        390        400        410        420 
DRVVYSTKEK NLTLKELFAK LKMHPYDLTV DSLDVHAGRQ TFQRFDKFND KYNPVGASEL 

       430        440        450        460        470        480 
RDLYLKTDNY INGEYFATII KEVGADLVEA KYQHAEPRLS IYGRSPDEWS KLSSWFVCNR 

       490        500        510        520        530        540 
IHCPNMTWMI QVPRIYDVFR SKNFLPHFGK MLENIFMPVF EATINPQADP ELSVFLKHIT 

       550        560        570        580        590        600 
GFDSVDDESK HSGHMFSSKS PKPQEWTLEK NPSYTYYAYY MYANIMVLNS LRKERGMNTF 

       610        620        630        640        650        660 
LFRPHCGEAG ALTHLMTAFM IADDISHGLN LKKSPVLQYL FFLAQIPIAM SPLSNNSLFL 

       670        680        690        700        710        720 
EYAKNPFLDF LQKGLMISLS TDDPMQFHFT KEPLMEEYAI AAQVFKLSTC DMCEVARNSV 

       730        740        750        760        770        780 
LQCGISHEEK VKFLGDNYLE EGPAGNDIRR TNVAQIRMAY RYETWCYELN LIAEGLKSTE 

« Hide

Isoform 2 [UniParc].

Checksum: B831F57E1D7AA491
Show »

FASTA77689,763

References

« Hide 'large scale' references
[1]"Characterization of the human and rat myoadenylate deaminase genes."
Sabina R.L., Morisaki T., Clarke P., Eddy R., Shows T.B., Morton C.C., Holmes E.W.
J. Biol. Chem. 265:9423-9433(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Molecular analysis of the myoadenylate deaminase deficiencies."
Sabina R.L., Fishbein W.N., Pezeshkpour G., Clarke P.R., Holmes E.W.
Neurology 42:170-179(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-780 (ISOFORM 1).
[5]"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] OF 15-780 (ISOFORM 1).
Tissue: Pericardium and Tongue.
[6]"Molecular basis of AMP deaminase deficiency in skeletal muscle."
Morisaki T., Gross M., Morisaki H., Pongratz D., Zoellner N., Holmes E.W.
Proc. Natl. Acad. Sci. U.S.A. 89:6457-6461(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-81.
[7]"First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient."
Morisaki H., Higuchi I., Abe M., Osame M., Morisaki T.
Hum. Mutat. 16:467-472(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMDD TRP-421 AND HIS-458.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-666.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37931 expand/collapse EMBL AC list , M37920, M37921, M37922, M37923, M37924, M37927, M37928, M37929, M37930 Genomic DNA. Translation: AAG24258.1. Different initiation.
AL096773 Genomic DNA. Translation: CAI18828.1. Different initiation.
AL096773 Genomic DNA. Translation: CAI18830.1.
CH471122 Genomic DNA. Translation: EAW56607.1.
M60092 mRNA. Translation: AAA57281.1. Different initiation.
AK314252 mRNA. Translation: BAG36918.1. Different initiation.
AK291349 mRNA. Translation: BAF84038.1. Different initiation.
CCDSCCDS53349.1. [P23109-2]
CCDS876.2. [P23109-1]
PIRI39444.
RefSeqNP_000027.2. NM_000036.2. [P23109-1]
NP_001166097.1. NM_001172626.1. [P23109-2]
UniGeneHs.89570.

3D structure databases

ProteinModelPortalP23109.
SMRP23109. Positions 225-775.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106767. 5 interactions.
IntActP23109. 5 interactions.
STRING9606.ENSP00000316520.

Chemistry

BindingDBP23109.
ChEMBLCHEMBL2869.
DrugBankDB00131. Adenosine monophosphate.

PTM databases

PhosphoSiteP23109.

Polymorphism databases

DMDM384872309.

Proteomic databases

PaxDbP23109.
PRIDEP23109.

Protocols and materials databases

DNASU270.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353928; ENSP00000316520; ENSG00000116748.
ENST00000369538; ENSP00000358551; ENSG00000116748. [P23109-2]
ENST00000520113; ENSP00000430075; ENSG00000116748. [P23109-1]
GeneID270.
KEGGhsa:270.
UCSCuc001efe.2. human. [P23109-1]
uc001eff.2. human. [P23109-2]

Organism-specific databases

CTD270.
GeneCardsGC01M115215.
H-InvDBHIX0199913.
HGNCHGNC:468. AMPD1.
HPAHPA026478.
HPA028080.
MIM102770. gene.
615511. phenotype.
neXtProtNX_P23109.
Orphanet45. Adenosine monophosphate deaminase deficiency.
PharmGKBPA24776.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000092200.
HOVERGENHBG050494.
KOK01490.
OMANMTWMIQ.
OrthoDBEOG70ZZMQ.
PhylomeDBP23109.
TreeFamTF300439.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP23109.
UniPathwayUPA00591; UER00663.

Gene expression databases

ArrayExpressP23109.
BgeeP23109.
CleanExHS_AMPD1.
GenevestigatorP23109.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
PANTHERPTHR11359. PTHR11359. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsTIGR01429. AMP_deaminase. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAMPD1. human.
GeneWikiAMP_deaminase.
GenomeRNAi270.
NextBio1061.
PROP23109.
SOURCESearch...

Entry information

Entry nameAMPD1_HUMAN
AccessionPrimary (citable) accession number: P23109
Secondary accession number(s): A8K5N4 expand/collapse secondary AC list , B2RAM1, F2Z3B3, Q5TF00, Q5TF02
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 18, 2012
Last modified: July 9, 2014
This is version 135 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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