Q01433 (AMPD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AMP deaminase 2
EC=3.5.4.6

Alternative name(s):
AMP deaminase isoform L

Gene names

Name:

AMPD2

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	879 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	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.
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	IMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway purine nucleobase metabolic process Traceable author statement. Source: Reactome purine nucleotide metabolic process Non-traceable author statement. Source: UniProtKB purine-containing compound salvage Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	AMP deaminase activity Non-traceable author statement Ref.3. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform Ex1B-2-3 (identifier: Q01433-1)

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 Ex1A-2-3 (identifier: Q01433-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     82-84: AAP → MAS

Isoform Ex1A-3 (identifier: Q01433-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: MRNRGQGLFR...MDGKCKEIAE → MLTFLPSPQ

Isoform Ex1B-3 (identifier: Q01433-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: MRNRGQGLFR...MDGKCKEIAE → MWQSQAPAGA...PACRPPLQLQ

Isoform 5 (identifier: Q01433-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 879	879	AMP deaminase 2		PRO_0000194407
Regions
	Region	489 – 494	6	Substrate binding By similarity
	Region	765 – 768	4	Substrate binding By similarity
Sites
	Active site	709	1	Proton acceptor By similarity
	Metal binding	418	1	Zinc; catalytic By similarity
	Metal binding	420	1	Zinc; catalytic By similarity
	Metal binding	687	1	Zinc; catalytic By similarity
	Metal binding	764	1	Zinc; catalytic By similarity
	Binding site	420	1	Substrate By similarity
	Binding site	690	1	Substrate By similarity
Amino acid modifications
	Modified residue	76	1	Phosphoserine Ref.11
	Modified residue	118	1	Phosphoserine Ref.10
	Modified residue	145	1	Phosphotyrosine By similarity
	Modified residue	151	1	Phosphoserine Ref.10
	Modified residue	168	1	Phosphoserine Ref.8 Ref.12 Ref.14
	Modified residue	188	1	Phosphothreonine Ref.10
	Modified residue	190	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14
	Modified residue	192	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 128	128	MRNRG…KEIAE → MLTFLPSPQ in isoform Ex1A-3.		VSP_001274
	Alternative sequence	1 – 128	128	MRNRG…KEIAE → MWQSQAPAGAAQTPPLSPPW SQPWHPIHLALASPRPNIPL RSGPACRPPLQLQ in isoform Ex1B-3.		VSP_001273
	Alternative sequence	1 – 118	118	Missing in isoform 5.		VSP_045975
	Alternative sequence	1 – 81	81	Missing in isoform Ex1A-2-3.		VSP_001271
	Alternative sequence	82 – 84	3	AAP → MAS in isoform Ex1A-2-3.		VSP_001272
	Natural variant	522	1	I → V. Ref.4 Corresponds to variant rs201254826 [ dbSNP | Ensembl ].		VAR_069105
Experimental info
	Sequence conflict	207	1	R → G in AAA11725. Ref.1
	Sequence conflict	811	1	V → I in BAG59062. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Ex1B-2-3 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 5BD9BBF5AA41BE8F	FASTA	879	100,688
	10 20 30 40 50 60 MRNRGQGLFR LRSRCFLHQS LPLGAGRRKG LDVAEPGPSR CRSDSPAVAA VVPAMASYPS 70 80 90 100 110 120 GSGKPKAKYP FKKRASLQAS TAAPEARGGL GAPPLQSARS LPGPAPCLKH FPLDLRTSMD 130 140 150 160 170 180 GKCKEIAEEL FTRSLAESEL RSAPYEFPEE SPIEQLEERR QRLERQISQD VKLEPDILLR 190 200 210 220 230 240 AKQDFLKTDS DSDLQLYKEQ GEGQGDRSLR ERDVLEREFQ RVTISGEEKC GVPFTDLLDA 250 260 270 280 290 300 AKSVVRALFI REKYMALSLQ SFCPTTRRYL QQLAEKPLET RTYEQGPDTP VSADAPVHPP 310 320 330 340 350 360 ALEQHPYEHC EPSTMPGDLG LGLRMVRGVV HVYTRREPDE HCSEVELPYP DLQEFVADVN 370 380 390 400 410 420 VLMALIINGP IKSFCYRRLQ YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH 430 440 450 460 470 480 ASSCMNQKHL LRFIKRAMKR HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD 490 500 510 520 530 540 RNTFHRFDKF NAKYNPIGES VLREIFIKTD NRVSGKYFAH IIKEVMSDLE ESKYQNAELR 550 560 570 580 590 600 LSIYGRSRDE WDKLARWAVM HRVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP 610 620 630 640 650 660 LFEATVHPAS HPELHLFLEH VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL 670 680 690 700 710 720 YYTFANMAML NHLRRQRGFH TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ 730 740 750 760 770 780 YLYYLAQIGI AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY 790 800 810 820 830 840 SIATQVWKLS SCDMCELARN SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV 850 860 870 GYRYETLCQE LALITQAVQS EMLETIPEEA GITMSPGPQ
	Isoform Ex1A-2-3 [UniParc]. Checksum: A31876E9F8CC93EB	FASTA	798	92,071
	10 20 30 40 50 60 MASEARGGLG APPLQSARSL PGPAPCLKHF PLDLRTSMDG KCKEIAEELF TRSLAESELR 70 80 90 100 110 120 SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA KQDFLKTDSD SDLQLYKEQG 130 140 150 160 170 180 EGQGDRSLRE RDVLEREFQR VTISGEEKCG VPFTDLLDAA KSVVRALFIR EKYMALSLQS 190 200 210 220 230 240 FCPTTRRYLQ QLAEKPLETR TYEQGPDTPV SADAPVHPPA LEQHPYEHCE PSTMPGDLGL 250 260 270 280 290 300 GLRMVRGVVH VYTRREPDEH CSEVELPYPD LQEFVADVNV LMALIINGPI KSFCYRRLQY 310 320 330 340 350 360 LSSKFQMHVL LNEMKELAAQ KKVPHRDFYN IRKVDTHIHA SSCMNQKHLL RFIKRAMKRH 370 380 390 400 410 420 LEEIVHVEQG REQTLREVFE SMNLTAYDLS VDTLDVHADR NTFHRFDKFN AKYNPIGESV 430 440 450 460 470 480 LREIFIKTDN RVSGKYFAHI IKEVMSDLEE SKYQNAELRL SIYGRSRDEW DKLARWAVMH 490 500 510 520 530 540 RVHSPNVRWL VQVPRLFDVY RTKGQLANFQ EMLENIFLPL FEATVHPASH PELHLFLEHV 550 560 570 580 590 600 DGFDSVDDES KPENHVFNLE SPLPEAWVEE DNPPYAYYLY YTFANMAMLN HLRRQRGFHT 610 620 630 640 650 660 FVLRPHCGEA GPIHHLVSAF MLAENISHGL LLRKAPVLQY LYYLAQIGIA MSPLSNNSLF 670 680 690 700 710 720 LSYHRNPLPE YLSRGLMVSL STDDPLQFHF TKEPLMEEYS IATQVWKLSS CDMCELARNS 730 740 750 760 770 780 VLMSGFSHKV KSHWLGPNYT KEGPEGNDIR RTNVPDIRVG YRYETLCQEL ALITQAVQSE 790 MLETIPEEAG ITMSPGPQ
	Isoform Ex1A-3 [UniParc]. Checksum: AF0EF5DDE5DEBEE3	FASTA	760	88,198
	10 20 30 40 50 60 MLTFLPSPQE LFTRSLAESE LRSAPYEFPE ESPIEQLEER RQRLERQISQ DVKLEPDILL 70 80 90 100 110 120 RAKQDFLKTD SDSDLQLYKE QGEGQGDRSL RERDVLEREF QRVTISGEEK CGVPFTDLLD 130 140 150 160 170 180 AAKSVVRALF IREKYMALSL QSFCPTTRRY LQQLAEKPLE TRTYEQGPDT PVSADAPVHP 190 200 210 220 230 240 PALEQHPYEH CEPSTMPGDL GLGLRMVRGV VHVYTRREPD EHCSEVELPY PDLQEFVADV 250 260 270 280 290 300 NVLMALIING PIKSFCYRRL QYLSSKFQMH VLLNEMKELA AQKKVPHRDF YNIRKVDTHI 310 320 330 340 350 360 HASSCMNQKH LLRFIKRAMK RHLEEIVHVE QGREQTLREV FESMNLTAYD LSVDTLDVHA 370 380 390 400 410 420 DRNTFHRFDK FNAKYNPIGE SVLREIFIKT DNRVSGKYFA HIIKEVMSDL EESKYQNAEL 430 440 450 460 470 480 RLSIYGRSRD EWDKLARWAV MHRVHSPNVR WLVQVPRLFD VYRTKGQLAN FQEMLENIFL 490 500 510 520 530 540 PLFEATVHPA SHPELHLFLE HVDGFDSVDD ESKPENHVFN LESPLPEAWV EEDNPPYAYY 550 560 570 580 590 600 LYYTFANMAM LNHLRRQRGF HTFVLRPHCG EAGPIHHLVS AFMLAENISH GLLLRKAPVL 610 620 630 640 650 660 QYLYYLAQIG IAMSPLSNNS LFLSYHRNPL PEYLSRGLMV SLSTDDPLQF HFTKEPLMEE 670 680 690 700 710 720 YSIATQVWKL SSCDMCELAR NSVLMSGFSH KVKSHWLGPN YTKEGPEGND IRRTNVPDIR 730 740 750 760 VGYRYETLCQ ELALITQAVQ SEMLETIPEE AGITMSPGPQ
	Isoform Ex1B-3 [UniParc]. Checksum: 753154327F2740E4	FASTA	804	92,918
	10 20 30 40 50 60 MWQSQAPAGA AQTPPLSPPW SQPWHPIHLA LASPRPNIPL RSGPACRPPL QLQELFTRSL 70 80 90 100 110 120 AESELRSAPY EFPEESPIEQ LEERRQRLER QISQDVKLEP DILLRAKQDF LKTDSDSDLQ 130 140 150 160 170 180 LYKEQGEGQG DRSLRERDVL EREFQRVTIS GEEKCGVPFT DLLDAAKSVV RALFIREKYM 190 200 210 220 230 240 ALSLQSFCPT TRRYLQQLAE KPLETRTYEQ GPDTPVSADA PVHPPALEQH PYEHCEPSTM 250 260 270 280 290 300 PGDLGLGLRM VRGVVHVYTR REPDEHCSEV ELPYPDLQEF VADVNVLMAL IINGPIKSFC 310 320 330 340 350 360 YRRLQYLSSK FQMHVLLNEM KELAAQKKVP HRDFYNIRKV DTHIHASSCM NQKHLLRFIK 370 380 390 400 410 420 RAMKRHLEEI VHVEQGREQT LREVFESMNL TAYDLSVDTL DVHADRNTFH RFDKFNAKYN 430 440 450 460 470 480 PIGESVLREI FIKTDNRVSG KYFAHIIKEV MSDLEESKYQ NAELRLSIYG RSRDEWDKLA 490 500 510 520 530 540 RWAVMHRVHS PNVRWLVQVP RLFDVYRTKG QLANFQEMLE NIFLPLFEAT VHPASHPELH 550 560 570 580 590 600 LFLEHVDGFD SVDDESKPEN HVFNLESPLP EAWVEEDNPP YAYYLYYTFA NMAMLNHLRR 610 620 630 640 650 660 QRGFHTFVLR PHCGEAGPIH HLVSAFMLAE NISHGLLLRK APVLQYLYYL AQIGIAMSPL 670 680 690 700 710 720 SNNSLFLSYH RNPLPEYLSR GLMVSLSTDD PLQFHFTKEP LMEEYSIATQ VWKLSSCDMC 730 740 750 760 770 780 ELARNSVLMS GFSHKVKSHW LGPNYTKEGP EGNDIRRTNV PDIRVGYRYE TLCQELALIT 790 800 QAVQSEMLET IPEEAGITMS PGPQ
	Isoform 5 [UniParc]. Checksum: A3BD94E9D6226281	FASTA	761	88,288
	10 20 30 40 50 60 MDGKCKEIAE ELFTRSLAES ELRSAPYEFP EESPIEQLEE RRQRLERQIS QDVKLEPDIL 70 80 90 100 110 120 LRAKQDFLKT DSDSDLQLYK EQGEGQGDRS LRERDVLERE FQRVTISGEE KCGVPFTDLL 130 140 150 160 170 180 DAAKSVVRAL FIREKYMALS LQSFCPTTRR YLQQLAEKPL ETRTYEQGPD TPVSADAPVH 190 200 210 220 230 240 PPALEQHPYE HCEPSTMPGD LGLGLRMVRG VVHVYTRREP DEHCSEVELP YPDLQEFVAD 250 260 270 280 290 300 VNVLMALIIN GPIKSFCYRR LQYLSSKFQM HVLLNEMKEL AAQKKVPHRD FYNIRKVDTH 310 320 330 340 350 360 IHASSCMNQK HLLRFIKRAM KRHLEEIVHV EQGREQTLRE VFESMNLTAY DLSVDTLDVH 370 380 390 400 410 420 ADRNTFHRFD KFNAKYNPIG ESVLREIFIK TDNRVSGKYF AHIIKEVMSD LEESKYQNAE 430 440 450 460 470 480 LRLSIYGRSR DEWDKLARWA VMHRVHSPNV RWLVQVPRLF DVYRTKGQLA NFQEMLENIF 490 500 510 520 530 540 LPLFEATVHP ASHPELHLFL EHVDGFDSVD DESKPENHVF NLESPLPEAW VEEDNPPYAY 550 560 570 580 590 600 YLYYTFANMA MLNHLRRQRG FHTFVLRPHC GEAGPIHHLV SAFMLAENIS HGLLLRKAPV 610 620 630 640 650 660 LQYLYYLAQI GIAMSPLSNN SLFLSYHRNP LPEYLSRGLM VSLSTDDPLQ FHFTKEPLME 670 680 690 700 710 720 EYSIATQVWK LSSCDMCELA RNSVLMSGFS HKVKSHWLGP NYTKEGPEGN DIRRTNVPDI 730 740 750 760 RVGYRYETLC QELALITQAV QSEMLETIPE EAGITMSPGP Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA." Bausch-Jurken M.T., Mahnke-Zizelman D.K., Morisaki T., Sabina R.L. J. Biol. Chem. 267:22407-22413(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L." Van den Bergh F., Sabina R.L. Biochem. J. 312:401-410(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
[3]	"Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters." Mahnke-Zizelman D.K., van den Bergh F., Bausch-Jurken M.T., Eddy R., Sait S., Shows T.B., Sabina R.L. Biochim. Biophys. Acta 1308:122-132(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[4]	"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 EX1B-3 AND 5), VARIANT VAL-522. Tissue: Testis and Thalamus.
[5]	"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. , 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].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 EX1A-2-3). Tissue: Brain.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-151; THR-188 AND SER-190, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-76 AND SER-190, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-190, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-190, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M91029 mRNA. Translation: AAA62127.1. M91029 mRNA. Translation: AAA62126.1. S47833 mRNA. Translation: AAA11725.1. U16267 mRNA. Translation: AAC50306.1. U16268 mRNA. Translation: AAC50307.1. U16269 Genomic RNA. Translation: AAB06511.1. U16270 mRNA. Translation: AAC50308.1. U16272, U16271 Genomic DNA. Translation: AAD56302.1. U16272, U16271 Genomic DNA. Translation: AAC50309.2. U16272, U16271 Genomic DNA. Translation: AAD56303.1. AK296394 mRNA. Translation: BAG59062.1. AK302939 mRNA. Translation: BAG64097.1. AL355310 Genomic DNA. Translation: CAI19305.1. AL355310 Genomic DNA. Translation: CAI19307.1. CH471122 Genomic DNA. Translation: EAW56396.1. CH471122 Genomic DNA. Translation: EAW56399.1. CH471122 Genomic DNA. Translation: EAW56401.1. BC007711 mRNA. Translation: AAH07711.1. BC075844 mRNA. Translation: AAH75844.1.
IPI	IPI00184670. IPI00215826. IPI00215827. IPI00942246. IPI00977596.
PIR	A44313. S59994. S59995. S59998. S59999. S60000.
RefSeq	NP_001244289.1. NM_001257360.1. NP_001244290.1. NM_001257361.1. NP_004028.3. NM_004037.7. NP_631895.1. NM_139156.3. NP_981949.1. NM_203404.1.
UniGene	Hs.82927.
3D structure databases
ProteinModelPortal	Q01433.
ModBase	Search...
PTM databases
PhosphoSite	Q01433.
Polymorphism databases
DMDM	12644375.
Proteomic databases
PaxDb	Q01433.
PRIDE	Q01433.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000256578; ENSP00000256578; ENSG00000116337. ENST00000342115; ENSP00000345498; ENSG00000116337. ENST00000358729; ENSP00000351573; ENSG00000116337. ENST00000393688; ENSP00000377292; ENSG00000116337. ENST00000528454; ENSP00000437164; ENSG00000116337. ENST00000528667; ENSP00000436541; ENSG00000116337.
GeneID	271.
KEGG	hsa:271.
UCSC	uc001dyb.1. human. uc001dyc.1. human. uc001dyd.1. human. uc010ovr.1. human. uc010ovs.1. human.
Organism-specific databases
CTD	271.
GeneCards	GC01P110162.
HGNC	HGNC:469. AMPD2.
HPA	HPA027137. HPA045760. HPA050590.
MIM	102771. gene.
neXtProt	NX_Q01433.
PharmGKB	PA24777.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1816.
HOVERGEN	HBG050494.
KO	K01490.
OMA	RYETLCQ.
PhylomeDB	Q01433.
Enzyme and pathway databases
BioCyc	MetaCyc:HS04008-MONOMER.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q01433.
UniPathway	UPA00591; UER00663.
Gene expression databases
ArrayExpress	Q01433.
Bgee	Q01433.
Genevestigator	Q01433.
GermOnline	ENSG00000116337. 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	Q01433.
ChEMBL	CHEMBL2997.
GenomeRNAi	271.
NextBio	1065.
SOURCE	Search...

Entry information

Entry name

AMPD2_HUMAN

Accession

Primary (citable) accession number: Q01433
Secondary accession number(s): B4DK50 , B4DZI5, E9PNG0, Q14856, Q14857, Q16686, Q16687, Q16688, Q16729, Q5T693, Q5T695, Q96IA1, Q9UDX8, Q9UDX9, Q9UMU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 1, 2000
Last modified:	May 29, 2013
This is version 122 of the entry and version 2 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.