Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01433

- AMPD2_HUMAN

UniProt

Q01433 - AMPD2_HUMAN

Protein

AMP deaminase 2

Gene

AMPD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. cyclic purine nucleotide metabolic process Source: UniProtKB
    2. energy homeostasis Source: MGI
    3. IMP biosynthetic process Source: MGI
    4. IMP salvage Source: UniProtKB-UniPathway
    5. nucleobase-containing small molecule metabolic process Source: Reactome
    6. purine-containing compound salvage Source: Reactome
    7. purine nucleobase metabolic process Source: Reactome
    8. small molecule metabolic process Source: Reactome

    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

    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.
    Orphaneti369920. 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

    ArrayExpressiQ01433.
    BgeeiQ01433.
    GenevestigatoriQ01433.

    Organism-specific databases

    HPAiHPA027137.
    HPA045760.
    HPA050590.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106768. 11 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.
    HOVERGENiHBG050494.
    KOiK01490.
    OMAiRYETLCQ.
    OrthoDBiEOG70ZZMQ.
    PhylomeDBiQ01433.
    TreeFamiTF300439.

    Family and domain databases

    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view]
    PANTHERiPTHR11359. PTHR11359. 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

    MRNRGQGLFR LRSRCFLHQS LPLGAGRRKG LDVAEPGPSR CRSDSPAVAA    50
    VVPAMASYPS GSGKPKAKYP FKKRASLQAS TAAPEARGGL GAPPLQSARS 100
    LPGPAPCLKH FPLDLRTSMD GKCKEIAEEL FTRSLAESEL RSAPYEFPEE 150
    SPIEQLEERR QRLERQISQD VKLEPDILLR AKQDFLKTDS DSDLQLYKEQ 200
    GEGQGDRSLR ERDVLEREFQ RVTISGEEKC GVPFTDLLDA AKSVVRALFI 250
    REKYMALSLQ SFCPTTRRYL QQLAEKPLET RTYEQGPDTP VSADAPVHPP 300
    ALEQHPYEHC EPSTMPGDLG LGLRMVRGVV HVYTRREPDE HCSEVELPYP 350
    DLQEFVADVN VLMALIINGP IKSFCYRRLQ YLSSKFQMHV LLNEMKELAA 400
    QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL LRFIKRAMKR HLEEIVHVEQ 450
    GREQTLREVF ESMNLTAYDL SVDTLDVHAD RNTFHRFDKF NAKYNPIGES 500
    VLREIFIKTD NRVSGKYFAH IIKEVMSDLE ESKYQNAELR LSIYGRSRDE 550
    WDKLARWAVM HRVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP 600
    LFEATVHPAS HPELHLFLEH VDGFDSVDDE SKPENHVFNL ESPLPEAWVE 650
    EDNPPYAYYL YYTFANMAML NHLRRQRGFH TFVLRPHCGE AGPIHHLVSA 700
    FMLAENISHG LLLRKAPVLQ YLYYLAQIGI AMSPLSNNSL FLSYHRNPLP 750
    EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIATQVWKLS SCDMCELARN 800
    SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV GYRYETLCQE 850
    LALITQAVQS EMLETIPEEA GITMSPGPQ 879
    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. 11 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 369920. Pontocerebellar hypoplasia type 9.
    PharmGKBi PA24777.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1816.
    HOVERGENi HBG050494.
    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

    ArrayExpressi Q01433.
    Bgeei Q01433.
    Genevestigatori Q01433.

    Family and domain databases

    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view ]
    PANTHERi PTHR11359. PTHR11359. 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

    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 1, 2014
    This is version 136 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