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Q01433

- AMPD2_HUMAN

UniProt

Q01433 - AMPD2_HUMAN

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Protein

AMP deaminase 2

Gene

AMPD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.1 Publication

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi418 – 4181Zinc; catalyticBy similarity
Metal bindingi420 – 4201Zinc; catalyticBy similarity
Binding sitei420 – 4201SubstrateBy similarity
Metal bindingi687 – 6871Zinc; catalyticBy similarity
Binding sitei690 – 6901SubstrateBy similarity
Active sitei709 – 7091Proton acceptorPROSITE-ProRule annotation
Metal bindingi764 – 7641Zinc; catalyticBy similarity

GO - Molecular functioni

  1. AMP deaminase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. cyclic purine nucleotide metabolic process Source: UniProtKB
  3. energy homeostasis Source: MGI
  4. IMP biosynthetic process Source: MGI
  5. IMP salvage Source: UniProtKB-UniPathway
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. purine-containing compound salvage Source: Reactome
  8. purine nucleobase metabolic process Source: Reactome
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS04008-MONOMER.
ReactomeiREACT_1923. Purine salvage.
SABIO-RKQ01433.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 2 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform L
Gene namesi
Name:AMPD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:469. AMPD2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Pontocerebellar hypoplasia 9 (PCH9) [MIM:615809]: A form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum, evident upon brain imaging. PCH9 features include severely delayed psychomotor development, progressive microcephaly, spasticity, seizures, and brain abnormalities, including brain atrophy, thin corpus callosum, and delayed myelination.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti674 – 6741R → H in PCH9. 1 Publication
VAR_071158
Natural varianti778 – 7781E → D in PCH9. 1 Publication
VAR_071193
Natural varianti793 – 7931D → Y in PCH9. 1 Publication
VAR_071159
Spastic paraplegia 63, autosomal recessive (SPG63) [MIM:615686]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Neurodegeneration

Organism-specific databases

MIMi615686. phenotype.
615809. phenotype.
Orphaneti401805. Autosomal recessive spastic paraplegia type 63.
369920. Pontocerebellar hypoplasia type 9.
PharmGKBiPA24777.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 879879AMP deaminase 2PRO_0000194407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Phosphoserine1 Publication
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei145 – 1451PhosphotyrosineBy similarity
Modified residuei151 – 1511Phosphoserine1 Publication
Modified residuei168 – 1681Phosphoserine3 Publications
Modified residuei188 – 1881Phosphothreonine1 Publication
Modified residuei190 – 1901Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01433.
PaxDbiQ01433.
PRIDEiQ01433.

PTM databases

PhosphoSiteiQ01433.

Expressioni

Tissue specificityi

Highly expressed in cerebellum. 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.1 Publication

Gene expression databases

BgeeiQ01433.
ExpressionAtlasiQ01433. baseline.
GenevestigatoriQ01433.

Organism-specific databases

HPAiHPA027137.
HPA045760.
HPA050590.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106768. 13 interactions.
IntActiQ01433. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ01433.
SMRiQ01433. Positions 306-843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni489 – 4946Substrate bindingBy similarity
Regioni765 – 7684Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOVERGENiHBG050494.
InParanoidiQ01433.
KOiK01490.
OMAiRYETLCQ.
OrthoDBiEOG70ZZMQ.
PhylomeDBiQ01433.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform Ex1B-2-3 (identifier: Q01433-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRNRGQGLFR LRSRCFLHQS LPLGAGRRKG LDVAEPGPSR CRSDSPAVAA
60 70 80 90 100
VVPAMASYPS GSGKPKAKYP FKKRASLQAS TAAPEARGGL GAPPLQSARS
110 120 130 140 150
LPGPAPCLKH FPLDLRTSMD GKCKEIAEEL FTRSLAESEL RSAPYEFPEE
160 170 180 190 200
SPIEQLEERR QRLERQISQD VKLEPDILLR AKQDFLKTDS DSDLQLYKEQ
210 220 230 240 250
GEGQGDRSLR ERDVLEREFQ RVTISGEEKC GVPFTDLLDA AKSVVRALFI
260 270 280 290 300
REKYMALSLQ SFCPTTRRYL QQLAEKPLET RTYEQGPDTP VSADAPVHPP
310 320 330 340 350
ALEQHPYEHC EPSTMPGDLG LGLRMVRGVV HVYTRREPDE HCSEVELPYP
360 370 380 390 400
DLQEFVADVN VLMALIINGP IKSFCYRRLQ YLSSKFQMHV LLNEMKELAA
410 420 430 440 450
QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL LRFIKRAMKR HLEEIVHVEQ
460 470 480 490 500
GREQTLREVF ESMNLTAYDL SVDTLDVHAD RNTFHRFDKF NAKYNPIGES
510 520 530 540 550
VLREIFIKTD NRVSGKYFAH IIKEVMSDLE ESKYQNAELR LSIYGRSRDE
560 570 580 590 600
WDKLARWAVM HRVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP
610 620 630 640 650
LFEATVHPAS HPELHLFLEH VDGFDSVDDE SKPENHVFNL ESPLPEAWVE
660 670 680 690 700
EDNPPYAYYL YYTFANMAML NHLRRQRGFH TFVLRPHCGE AGPIHHLVSA
710 720 730 740 750
FMLAENISHG LLLRKAPVLQ YLYYLAQIGI AMSPLSNNSL FLSYHRNPLP
760 770 780 790 800
EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIATQVWKLS SCDMCELARN
810 820 830 840 850
SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV GYRYETLCQE
860 870
LALITQAVQS EMLETIPEEA GITMSPGPQ
Length:879
Mass (Da):100,688
Last modified:December 1, 2000 - v2
Checksum:i5BD9BBF5AA41BE8F
GO
Isoform Ex1A-2-3 (identifier: Q01433-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:798
Mass (Da):92,071
Checksum:iA31876E9F8CC93EB
GO
Isoform Ex1A-3 (identifier: Q01433-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:760
Mass (Da):88,198
Checksum:iAF0EF5DDE5DEBEE3
GO
Isoform Ex1B-3 (identifier: Q01433-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:804
Mass (Da):92,918
Checksum:i753154327F2740E4
GO
Isoform 5 (identifier: Q01433-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:761
Mass (Da):88,288
Checksum:iA3BD94E9D6226281
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071R → G in AAA11725. (PubMed:1429593)Curated
Sequence conflicti811 – 8111V → I in BAG59062. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti522 – 5221I → V.1 Publication
Corresponds to variant rs201254826 [ dbSNP | Ensembl ].
VAR_069105
Natural varianti674 – 6741R → H in PCH9. 1 Publication
VAR_071158
Natural varianti778 – 7781E → D in PCH9. 1 Publication
VAR_071193
Natural varianti793 – 7931D → Y in PCH9. 1 Publication
VAR_071159

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128MRNRG…KEIAE → MLTFLPSPQ in isoform Ex1A-3. CuratedVSP_001274Add
BLAST
Alternative sequencei1 – 128128MRNRG…KEIAE → MWQSQAPAGAAQTPPLSPPW SQPWHPIHLALASPRPNIPL RSGPACRPPLQLQ in isoform Ex1B-3. 1 PublicationVSP_001273Add
BLAST
Alternative sequencei1 – 118118Missing in isoform 5. 1 PublicationVSP_045975Add
BLAST
Alternative sequencei1 – 8181Missing in isoform Ex1A-2-3. 1 PublicationVSP_001271Add
BLAST
Alternative sequencei82 – 843AAP → MAS in isoform Ex1A-2-3. 1 PublicationVSP_001272

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30796.1. [Q01433-3]
CCDS58016.1. [Q01433-5]
CCDS804.1. [Q01433-2]
CCDS805.1. [Q01433-1]
PIRiA44313.
S59994.
S59995.
S59998.
S59999.
S60000.
RefSeqiNP_001244289.1. NM_001257360.1. [Q01433-1]
NP_001244290.1. NM_001257361.1. [Q01433-5]
NP_004028.3. NM_004037.7. [Q01433-1]
NP_631895.1. NM_139156.3. [Q01433-2]
NP_981949.1. NM_203404.1. [Q01433-3]
XP_005270809.1. XM_005270752.1. [Q01433-4]
UniGeneiHs.82927.

Genome annotation databases

EnsembliENST00000256578; ENSP00000256578; ENSG00000116337. [Q01433-1]
ENST00000342115; ENSP00000345498; ENSG00000116337. [Q01433-2]
ENST00000358729; ENSP00000351573; ENSG00000116337. [Q01433-4]
ENST00000393688; ENSP00000377292; ENSG00000116337. [Q01433-3]
ENST00000528454; ENSP00000437164; ENSG00000116337. [Q01433-5]
ENST00000528667; ENSP00000436541; ENSG00000116337. [Q01433-1]
GeneIDi271.
KEGGihsa:271.
UCSCiuc001dyb.2. human. [Q01433-2]
uc001dyc.2. human. [Q01433-1]
uc001dyd.1. human. [Q01433-3]
uc010ovr.1. human. [Q01433-4]

Polymorphism databases

DMDMi12644375.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30796.1. [Q01433-3 ]
CCDS58016.1. [Q01433-5 ]
CCDS804.1. [Q01433-2 ]
CCDS805.1. [Q01433-1 ]
PIRi A44313.
S59994.
S59995.
S59998.
S59999.
S60000.
RefSeqi NP_001244289.1. NM_001257360.1. [Q01433-1 ]
NP_001244290.1. NM_001257361.1. [Q01433-5 ]
NP_004028.3. NM_004037.7. [Q01433-1 ]
NP_631895.1. NM_139156.3. [Q01433-2 ]
NP_981949.1. NM_203404.1. [Q01433-3 ]
XP_005270809.1. XM_005270752.1. [Q01433-4 ]
UniGenei Hs.82927.

3D structure databases

ProteinModelPortali Q01433.
SMRi Q01433. Positions 306-843.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106768. 13 interactions.
IntActi Q01433. 1 interaction.

Chemistry

BindingDBi Q01433.
ChEMBLi CHEMBL2997.

PTM databases

PhosphoSitei Q01433.

Polymorphism databases

DMDMi 12644375.

Proteomic databases

MaxQBi Q01433.
PaxDbi Q01433.
PRIDEi Q01433.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256578 ; ENSP00000256578 ; ENSG00000116337 . [Q01433-1 ]
ENST00000342115 ; ENSP00000345498 ; ENSG00000116337 . [Q01433-2 ]
ENST00000358729 ; ENSP00000351573 ; ENSG00000116337 . [Q01433-4 ]
ENST00000393688 ; ENSP00000377292 ; ENSG00000116337 . [Q01433-3 ]
ENST00000528454 ; ENSP00000437164 ; ENSG00000116337 . [Q01433-5 ]
ENST00000528667 ; ENSP00000436541 ; ENSG00000116337 . [Q01433-1 ]
GeneIDi 271.
KEGGi hsa:271.
UCSCi uc001dyb.2. human. [Q01433-2 ]
uc001dyc.2. human. [Q01433-1 ]
uc001dyd.1. human. [Q01433-3 ]
uc010ovr.1. human. [Q01433-4 ]

Organism-specific databases

CTDi 271.
GeneCardsi GC01P110162.
HGNCi HGNC:469. AMPD2.
HPAi HPA027137.
HPA045760.
HPA050590.
MIMi 102771. gene.
615686. phenotype.
615809. phenotype.
neXtProti NX_Q01433.
Orphaneti 401805. Autosomal recessive spastic paraplegia type 63.
369920. Pontocerebellar hypoplasia type 9.
PharmGKBi PA24777.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1816.
GeneTreei ENSGT00390000008190.
HOVERGENi HBG050494.
InParanoidi Q01433.
KOi K01490.
OMAi RYETLCQ.
OrthoDBi EOG70ZZMQ.
PhylomeDBi Q01433.
TreeFami TF300439.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .
BioCyci MetaCyc:HS04008-MONOMER.
Reactomei REACT_1923. Purine salvage.
SABIO-RK Q01433.

Miscellaneous databases

GeneWikii AMPD2.
GenomeRNAii 271.
NextBioi 1065.
PROi Q01433.
SOURCEi Search...

Gene expression databases

Bgeei Q01433.
ExpressionAtlasi Q01433. baseline.
Genevestigatori Q01433.

Family and domain databases

InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view ]
PANTHERi PTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 1 hit.
Pfami PF00962. A_deaminase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
PROSITEi PS00485. A_DEAMINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-151; THR-188 AND SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANTS PCH9 HIS-674; ASP-778 AND TYR-793.
  16. Cited for: INVOLVEMENT IN SPG63.

Entry informationi

Entry nameiAMPD2_HUMAN
AccessioniPrimary (citable) accession number: Q01433
Secondary accession number(s): B4DK50
, B4DZI5, E9PNG0, Q14856, Q14857, Q16686, Q16687, Q16688, Q16729, Q5T693, Q5T695, Q96IA1, Q9UDX8, Q9UDX9, Q9UMU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3