Q01432 (AMPD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AMP deaminase 3
EC=3.5.4.6

Alternative name(s):
AMP deaminase isoform E
Erythrocyte AMP deaminase

Gene names

Name:

AMPD3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	767 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Isoform 1 is the predominant form in skeletal muscle; Isoform 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; Isoform 3 is found in erythrocytes.
Involvement in disease	Adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE) [MIM:612874]: A metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	AMP catabolic process Traceable author statement PubMed 9291127. Source: ProtInc IMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway purine nucleobase metabolic process Traceable author statement. Source: Reactome purine-containing compound salvage Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	AMP deaminase activity Traceable author statement PubMed 9291127. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1B (identifier: Q01432-1)

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 1A (identifier: Q01432-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM
     208-767: Missing.

Isoform 1C (identifier: Q01432-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM
     652-767: Missing.

Isoform 2 (identifier: Q01432-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM

Isoform 3 (identifier: Q01432-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM

Isoform 4 (identifier: Q01432-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 767	767	AMP deaminase 3		PRO_0000194410
Regions
	Region	388 – 393	6	Substrate binding By similarity
	Region	664 – 667	4	Substrate binding By similarity
Sites
	Active site	608	1	Proton acceptor By similarity
	Metal binding	317	1	Zinc; catalytic By similarity
	Metal binding	319	1	Zinc; catalytic By similarity
	Metal binding	586	1	Zinc; catalytic By similarity
	Metal binding	663	1	Zinc; catalytic By similarity
	Binding site	319	1	Substrate By similarity
	Binding site	589	1	Substrate By similarity
Amino acid modifications
	Modified residue	107	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	1 – 159	159	Missing in isoform 4.		VSP_044230
	Alternative sequence	1	1	M → MALSSEPAEM in isoform 1A and isoform 2.		VSP_001275
	Alternative sequence	1	1	M → MEPGSAEM in isoform 1C and isoform 3.		VSP_001276
	Alternative sequence	208 – 767	560	Missing in isoform 1A.		VSP_001277
	Alternative sequence	652 – 767	116	Missing in isoform 1C.		VSP_001278
	Natural variant	185	1	R → W. Corresponds to variant rs11042836 [ dbSNP | Ensembl ].		VAR_033499
	Natural variant	310	1	N → K in AMPDDE. Ref.10		VAR_042606
	Natural variant	311	1	V → L in AMPDDE. Ref.11		VAR_042607
	Natural variant	320	1	A → V in AMPDDE. Ref.10		VAR_042608
	Natural variant	324	1	M → T in AMPDDE. Ref.10		VAR_042609
	Natural variant	331	1	R → C in AMPDDE. Ref.10		VAR_042610
	Natural variant	402	1	R → C in AMPDDE. Ref.10		VAR_042611
	Natural variant	450	1	W → R in AMPDDE. Ref.10 Ref.12		VAR_042612
	Natural variant	455	1	Y → H. Corresponds to variant rs36003153 [ dbSNP | Ensembl ].		VAR_042613
	Natural variant	573	1	R → C in AMPDDE; enzyme inactive. Ref.4 Corresponds to variant rs3741040 [ dbSNP | Ensembl ].		VAR_009881
	Natural variant	585	1	P → L in AMPDDE. Ref.10		VAR_042614
	Natural variant	712	1	Q → P in AMPDDE. Ref.12		VAR_042615

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1B [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 2E0A2C629003B98C	FASTA	767	88,812
	10 20 30 40 50 60 MPRQFPKLNI SEVDEQVRLL AEKVFAKVLR EEDSKDALSL FTVPEDCPIG QKEAKERELQ 70 80 90 100 110 120 KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PPQQDWKGPP AASPAMSPTT PVVTGATSLP 130 140 150 160 170 180 TPAPYAMPEF QRVTISGDYC AGITLEDYEQ AAKSLAKALM IREKYARLAY HRFPRITSQY 190 200 210 220 230 240 LGHPRADTAP PEEGLPDFHP PPLPQEDPYC LDDAPPNLDY LVHMQGGILF VYDNKKMLEH 250 260 270 280 290 300 QEPHSLPYPD LETYTVDMSH ILALITDGPT KTYCHRRLNF LESKFSLHEM LNEMSEFKEL 310 320 330 340 350 360 KSNPHRDFYN VRKVDTHIHA AACMNQKHLL RFIKHTYQTE PDRTVAEKRG RKITLRQVFD 370 380 390 400 410 420 GLHMDPYDLT VDSLDVHAGR QTFHRFDKFN SKYNPVGASE LRDLYLKTEN YLGGEYFARM 430 440 450 460 470 480 VKEVARELEE SKYQYSEPRL SIYGRSPEEW PNLAYWFIQH KVYSPNMRWI IQVPRIYDIF 490 500 510 520 530 540 RSKKLLPNFG KMLENIFLPL FKATINPQDH RELHLFLKYV TGFDSVDDES KHSDHMFSDK 550 560 570 580 590 600 SPNPDVWTSE QNPPYSYYLY YMYANIMVLN NLRRERGLST FLFRPHCGEA GSITHLVSAF 610 620 630 640 650 660 LTADNISHGL LLKKSPVLQY LYYLAQIPIA MSPLSNNSLF LEYSKNPLRE FLHKGLHVSL 670 680 690 700 710 720 STDDPMQFHY TKEALMEEYA IAAQVWKLST CDLCEIARNS VLQSGLSHQE KQKFLGQNYY 730 740 750 760 KEGPEGNDIR KTNVAQIRMA FRYETLCNEL SFLSDAMKSE EITALTN
	Isoform 1A [UniParc]. Checksum: 77821100D9737811	FASTA	216	24,119
	10 20 30 40 50 60 MALSSEPAEM PRQFPKLNIS EVDEQVRLLA EKVFAKVLRE EDSKDALSLF TVPEDCPIGQ 70 80 90 100 110 120 KEAKERELQK ELAEQKSVET AKRKKSFKMI RSQSLSLQMP PQQDWKGPPA ASPAMSPTTP 130 140 150 160 170 180 VVTGATSLPT PAPYAMPEFQ RVTISGDYCA GITLEDYEQA AKSLAKALMI REKYARLAYH 190 200 210 RFPRITSQYL GHPRADTAPP EEGLPDFHPP PLPQED
	Isoform 1C [UniParc]. Checksum: 0FDFC779DC4996F2	FASTA	658	76,269
	10 20 30 40 50 60 MEPGSAEMPR QFPKLNISEV DEQVRLLAEK VFAKVLREED SKDALSLFTV PEDCPIGQKE 70 80 90 100 110 120 AKERELQKEL AEQKSVETAK RKKSFKMIRS QSLSLQMPPQ QDWKGPPAAS PAMSPTTPVV 130 140 150 160 170 180 TGATSLPTPA PYAMPEFQRV TISGDYCAGI TLEDYEQAAK SLAKALMIRE KYARLAYHRF 190 200 210 220 230 240 PRITSQYLGH PRADTAPPEE GLPDFHPPPL PQEDPYCLDD APPNLDYLVH MQGGILFVYD 250 260 270 280 290 300 NKKMLEHQEP HSLPYPDLET YTVDMSHILA LITDGPTKTY CHRRLNFLES KFSLHEMLNE 310 320 330 340 350 360 MSEFKELKSN PHRDFYNVRK VDTHIHAAAC MNQKHLLRFI KHTYQTEPDR TVAEKRGRKI 370 380 390 400 410 420 TLRQVFDGLH MDPYDLTVDS LDVHAGRQTF HRFDKFNSKY NPVGASELRD LYLKTENYLG 430 440 450 460 470 480 GEYFARMVKE VARELEESKY QYSEPRLSIY GRSPEEWPNL AYWFIQHKVY SPNMRWIIQV 490 500 510 520 530 540 PRIYDIFRSK KLLPNFGKML ENIFLPLFKA TINPQDHREL HLFLKYVTGF DSVDDESKHS 550 560 570 580 590 600 DHMFSDKSPN PDVWTSEQNP PYSYYLYYMY ANIMVLNNLR RERGLSTFLF RPHCGEAGSI 610 620 630 640 650 THLVSAFLTA DNISHGLLLK KSPVLQYLYY LAQIPIAMSP LSNNSLFLEY SKNPLREF
	Isoform 2 [UniParc]. Checksum: 53FFE0714FC9BC45	FASTA	776	89,728
	10 20 30 40 50 60 MALSSEPAEM PRQFPKLNIS EVDEQVRLLA EKVFAKVLRE EDSKDALSLF TVPEDCPIGQ 70 80 90 100 110 120 KEAKERELQK ELAEQKSVET AKRKKSFKMI RSQSLSLQMP PQQDWKGPPA ASPAMSPTTP 130 140 150 160 170 180 VVTGATSLPT PAPYAMPEFQ RVTISGDYCA GITLEDYEQA AKSLAKALMI REKYARLAYH 190 200 210 220 230 240 RFPRITSQYL GHPRADTAPP EEGLPDFHPP PLPQEDPYCL DDAPPNLDYL VHMQGGILFV 250 260 270 280 290 300 YDNKKMLEHQ EPHSLPYPDL ETYTVDMSHI LALITDGPTK TYCHRRLNFL ESKFSLHEML 310 320 330 340 350 360 NEMSEFKELK SNPHRDFYNV RKVDTHIHAA ACMNQKHLLR FIKHTYQTEP DRTVAEKRGR 370 380 390 400 410 420 KITLRQVFDG LHMDPYDLTV DSLDVHAGRQ TFHRFDKFNS KYNPVGASEL RDLYLKTENY 430 440 450 460 470 480 LGGEYFARMV KEVARELEES KYQYSEPRLS IYGRSPEEWP NLAYWFIQHK VYSPNMRWII 490 500 510 520 530 540 QVPRIYDIFR SKKLLPNFGK MLENIFLPLF KATINPQDHR ELHLFLKYVT GFDSVDDESK 550 560 570 580 590 600 HSDHMFSDKS PNPDVWTSEQ NPPYSYYLYY MYANIMVLNN LRRERGLSTF LFRPHCGEAG 610 620 630 640 650 660 SITHLVSAFL TADNISHGLL LKKSPVLQYL YYLAQIPIAM SPLSNNSLFL EYSKNPLREF 670 680 690 700 710 720 LHKGLHVSLS TDDPMQFHYT KEALMEEYAI AAQVWKLSTC DLCEIARNSV LQSGLSHQEK 730 740 750 760 770 QKFLGQNYYK EGPEGNDIRK TNVAQIRMAF RYETLCNELS FLSDAMKSEE ITALTN
	Isoform 3 [UniParc]. Checksum: 208BFD79F9053BA2	FASTA	774	89,514
	10 20 30 40 50 60 MEPGSAEMPR QFPKLNISEV DEQVRLLAEK VFAKVLREED SKDALSLFTV PEDCPIGQKE 70 80 90 100 110 120 AKERELQKEL AEQKSVETAK RKKSFKMIRS QSLSLQMPPQ QDWKGPPAAS PAMSPTTPVV 130 140 150 160 170 180 TGATSLPTPA PYAMPEFQRV TISGDYCAGI TLEDYEQAAK SLAKALMIRE KYARLAYHRF 190 200 210 220 230 240 PRITSQYLGH PRADTAPPEE GLPDFHPPPL PQEDPYCLDD APPNLDYLVH MQGGILFVYD 250 260 270 280 290 300 NKKMLEHQEP HSLPYPDLET YTVDMSHILA LITDGPTKTY CHRRLNFLES KFSLHEMLNE 310 320 330 340 350 360 MSEFKELKSN PHRDFYNVRK VDTHIHAAAC MNQKHLLRFI KHTYQTEPDR TVAEKRGRKI 370 380 390 400 410 420 TLRQVFDGLH MDPYDLTVDS LDVHAGRQTF HRFDKFNSKY NPVGASELRD LYLKTENYLG 430 440 450 460 470 480 GEYFARMVKE VARELEESKY QYSEPRLSIY GRSPEEWPNL AYWFIQHKVY SPNMRWIIQV 490 500 510 520 530 540 PRIYDIFRSK KLLPNFGKML ENIFLPLFKA TINPQDHREL HLFLKYVTGF DSVDDESKHS 550 560 570 580 590 600 DHMFSDKSPN PDVWTSEQNP PYSYYLYYMY ANIMVLNNLR RERGLSTFLF RPHCGEAGSI 610 620 630 640 650 660 THLVSAFLTA DNISHGLLLK KSPVLQYLYY LAQIPIAMSP LSNNSLFLEY SKNPLREFLH 670 680 690 700 710 720 KGLHVSLSTD DPMQFHYTKE ALMEEYAIAA QVWKLSTCDL CEIARNSVLQ SGLSHQEKQK 730 740 750 760 770 FLGQNYYKEG PEGNDIRKTN VAQIRMAFRY ETLCNELSFL SDAMKSEEIT ALTN
	Isoform 4 [UniParc]. Checksum: 04814500471AE377	FASTA	608	71,222
	10 20 30 40 50 60 MIREKYARLA YHRFPRITSQ YLGHPRADTA PPEEGLPDFH PPPLPQEDPY CLDDAPPNLD 70 80 90 100 110 120 YLVHMQGGIL FVYDNKKMLE HQEPHSLPYP DLETYTVDMS HILALITDGP TKTYCHRRLN 130 140 150 160 170 180 FLESKFSLHE MLNEMSEFKE LKSNPHRDFY NVRKVDTHIH AAACMNQKHL LRFIKHTYQT 190 200 210 220 230 240 EPDRTVAEKR GRKITLRQVF DGLHMDPYDL TVDSLDVHAG RQTFHRFDKF NSKYNPVGAS 250 260 270 280 290 300 ELRDLYLKTE NYLGGEYFAR MVKEVARELE ESKYQYSEPR LSIYGRSPEE WPNLAYWFIQ 310 320 330 340 350 360 HKVYSPNMRW IIQVPRIYDI FRSKKLLPNF GKMLENIFLP LFKATINPQD HRELHLFLKY 370 380 390 400 410 420 VTGFDSVDDE SKHSDHMFSD KSPNPDVWTS EQNPPYSYYL YYMYANIMVL NNLRRERGLS 430 440 450 460 470 480 TFLFRPHCGE AGSITHLVSA FLTADNISHG LLLKKSPVLQ YLYYLAQIPI AMSPLSNNSL 490 500 510 520 530 540 FLEYSKNPLR EFLHKGLHVS LSTDDPMQFH YTKEALMEEY AIAAQVWKLS TCDLCEIARN 550 560 570 580 590 600 SVLQSGLSHQ EKQKFLGQNY YKEGPEGNDI RKTNVAQIRM AFRYETLCNE LSFLSDAMKS EEITALTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase." Yamada Y., Goto H., Ogasawara N. Biochim. Biophys. Acta 1171:125-128(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1B).
[2]	"Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons." Mahnke-Zizelman D.K., Sabina R.L. J. Biol. Chem. 267:20866-20877(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C). Tissue: Keratinocyte.
[3]	"Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing." Mahnke-Zizelman D.K., Eddy R., Shows T.B., Sabina R.L. Biochim. Biophys. Acta 1306:75-92(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1B; 2 AND 3), ALTERNATIVE SPLICING.
[4]	"A point mutation responsible for human erythrocyte AMP deaminase deficiency." Yamada Y., Goto H., Ogasawara N. Hum. Mol. Genet. 3:331-334(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1B), VARIANT AMPDDE CYS-573.
[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. , 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 1B; 2; 3 AND 4). Tissue: Brain, Synovium and Testis.
[6]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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. , 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].
[8]	"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 2).
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations." Yamada Y., Goto H., Murase T., Ogasawara N. Hum. Mol. Genet. 3:2243-2245(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMPDDE LYS-310; VAL-320; THR-324; CYS-331; CYS-402; ARG-450 AND LEU-585.
[11]	"Gene mutations responsible for human erythrocyte AMP deaminase deficiency in Poles." Yamada Y., Makarewicz W., Goto H., Nomura N., Kitoh H., Ogasawara N. Adv. Exp. Med. Biol. 431:347-350(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMPDDE LEU-311.
[12]	"A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3." Yamada Y., Goto H., Wakamatsu N., Ogasawara N. Hum. Mutat. 17:78-78(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMPDDE ARG-450 AND PRO-712.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D12775 mRNA. Translation: BAA02240.1. M84720 mRNA. Translation: AAA58365.1. M84721 mRNA. Translation: AAA58366.1. M84722 mRNA. Translation: AAA58367.1. U29926 , U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60410.1. U29926 , U29912, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60408.1. U29926 , U29927, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60409.1. D31646 Genomic DNA. Translation: BAA06505.1. AK289998 mRNA. Translation: BAF82687.1. AK295046 mRNA. Translation: BAH11958.1. AK301507 mRNA. Translation: BAH13499.1. AK302970 mRNA. Translation: BAH13863.1. AC084117 Genomic DNA. No translation available. CH471064 Genomic DNA. Translation: EAW68567.1. CH471064 Genomic DNA. Translation: EAW68568.1. CH471064 Genomic DNA. Translation: EAW68569.1. BC126118 mRNA. Translation: AAI26119.1.
IPI	IPI00300573. IPI00619970. IPI01010843.
PIR	S68146. S68147.
RefSeq	NP_000471.1. NM_000480.2. NP_001020560.1. NM_001025389.1. NP_001020561.1. NM_001025390.1. NP_001165901.1. NM_001172430.1. NP_001165902.1. NM_001172431.1.
UniGene	Hs.501890.
3D structure databases
ProteinModelPortal	Q01432.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01432. 2 interactions.
STRING	9606.ENSP00000256183.
PTM databases
PhosphoSite	Q01432.
Polymorphism databases
DMDM	399033.
Proteomic databases
PaxDb	Q01432.
PRIDE	Q01432.
Protocols and materials databases
DNASU	272.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396553; ENSP00000379801; ENSG00000133805. ENST00000396554; ENSP00000379802; ENSG00000133805. ENST00000444303; ENSP00000396000; ENSG00000133805. ENST00000528723; ENSP00000436987; ENSG00000133805. ENST00000529507; ENSP00000431648; ENSG00000133805.
GeneID	272.
KEGG	hsa:272.
UCSC	uc001min.1. human. uc001mio.1. human. uc001mip.1. human.
Organism-specific databases
CTD	272.
GeneCards	GC11P010329.
HGNC	HGNC:470. AMPD3.
HPA	HPA047408.
MIM	102772. gene. 612874. phenotype.
neXtProt	NX_Q01432.
Orphanet	45. Adenosine monophosphate deaminase deficiency.
PharmGKB	PA24778.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1816.
HOGENOM	HOG000092200.
HOVERGEN	HBG050494.
InParanoid	Q01432.
KO	K01490.
OMA	FSLHEML.
OrthoDB	EOG4J9MZC.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q01432.
UniPathway	UPA00591; UER00663.
Gene expression databases
ArrayExpress	Q01432.
Bgee	Q01432.
CleanEx	HS_AMPD3.
Genevestigator	Q01432.
GermOnline	ENSG00000133805. Homo sapiens.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006329. AMP_deaminase. [Graphical view]
PANTHER	PTHR11359. PTHR11359. 1 hit.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
PIRSF	PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMs	TIGR01429. AMP_deaminase. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q01432.
ChEMBL	CHEMBL2912.
ChiTaRS	AMPD3. human.
GenomeRNAi	272.
NextBio	1073.
SOURCE	Search...

Entry information

Entry name

AMPD3_HUMAN

Accession

Primary (citable) accession number: Q01432
Secondary accession number(s): A0AUX0 , B7Z2S2, B7Z763, B7Z877

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 29, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.