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P19021

- AMD_HUMAN

UniProt

P19021 - AMD_HUMAN

Protein

Peptidyl-glycine alpha-amidating monooxygenase

Gene

PAM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.

    Catalytic activityi

    Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.
    Peptidylamidoglycolate = peptidyl amide + glyoxylate.

    Cofactori

    Zinc; for the lyase reaction.1 Publication
    Binds 2 copper ions per subunit; For the monoxygenase reaction.1 Publication

    Enzyme regulationi

    Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi102 – 1021Copper ABy similarity
    Metal bindingi103 – 1031Copper ABy similarity
    Metal bindingi167 – 1671Copper ABy similarity
    Metal bindingi237 – 2371Copper BBy similarity
    Metal bindingi239 – 2391Copper BBy similarity
    Metal bindingi309 – 3091Copper BBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: Ensembl
    2. copper ion binding Source: InterPro
    3. L-ascorbic acid binding Source: UniProtKB-KW
    4. peptidylamidoglycolate lyase activity Source: UniProt
    5. peptidylglycine monooxygenase activity Source: UniProt
    6. protein binding Source: UniProtKB
    7. zinc ion binding Source: UniProt

    GO - Biological processi

    1. central nervous system development Source: Ensembl
    2. heart development Source: Ensembl
    3. lactation Source: Ensembl
    4. limb development Source: Ensembl
    5. long-chain fatty acid metabolic process Source: Ensembl
    6. maternal process involved in female pregnancy Source: Ensembl
    7. odontogenesis Source: Ensembl
    8. ovulation cycle process Source: Ensembl
    9. peptide amidation Source: UniProt
    10. protein amidation Source: Ensembl
    11. protein homooligomerization Source: Ensembl
    12. regulation of actin cytoskeleton organization Source: Ensembl
    13. regulation of protein secretion Source: Ensembl
    14. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    15. response to copper ion Source: Ensembl
    16. response to drug Source: Ensembl
    17. response to estradiol Source: Ensembl
    18. response to glucocorticoid Source: Ensembl
    19. response to hypoxia Source: Ensembl
    20. response to pH Source: Ensembl
    21. toxin metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Vitamin C, Zinc

    Enzyme and pathway databases

    SignaLinkiP19021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-glycine alpha-amidating monooxygenase
    Short name:
    PAM
    Including the following 2 domains:
    Peptidylglycine alpha-hydroxylating monooxygenase (EC:1.14.17.3)
    Short name:
    PHM
    Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC:4.3.2.5)
    Alternative name(s):
    Peptidylamidoglycolate lyase
    Short name:
    PAL
    Gene namesi
    Name:PAM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:8596. PAM.

    Subcellular locationi

    Isoform 3 : Secreted
    Note: Secreted from secretory granules.
    Isoform 4 : Secreted
    Note: Secreted from secretory granules.

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular space Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: UniProtKB
    6. neuron projection Source: Ensembl
    7. perikaryon Source: Ensembl
    8. perinuclear region of cytoplasm Source: Ensembl
    9. plasma membrane Source: Ensembl
    10. secretory granule membrane Source: Ensembl
    11. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32926.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020CuratedAdd
    BLAST
    Propeptidei21 – 3010CuratedPRO_0000006361
    Chaini31 – 973943Peptidyl-glycine alpha-amidating monooxygenasePRO_0000006362Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 181By similarity
    Disulfide bondi76 ↔ 121By similarity
    Disulfide bondi109 ↔ 126By similarity
    Disulfide bondi222 ↔ 329By similarity
    Disulfide bondi288 ↔ 310By similarity
    Disulfide bondi631 ↔ 652By similarity
    Disulfide bondi699 ↔ 710By similarity
    Glycosylationi762 – 7621N-linked (GlcNAc...)Sequence Analysis
    Modified residuei929 – 9291Phosphoserine1 Publication
    Modified residuei942 – 9421Phosphoserine1 Publication
    Modified residuei943 – 9431Phosphothreonine1 Publication
    Modified residuei946 – 9461Phosphoserine; by UHMK1; in vitro3 Publications
    Modified residuei961 – 9611Sulfotyrosine1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    MaxQBiP19021.
    PaxDbiP19021.
    PRIDEiP19021.

    PTM databases

    PhosphoSiteiP19021.

    Expressioni

    Gene expression databases

    ArrayExpressiP19021.
    BgeeiP19021.
    CleanExiHS_PAM.
    GenevestigatoriP19021.

    Organism-specific databases

    HPAiCAB026119.
    HPA042260.

    Interactioni

    Subunit structurei

    Monomer. Interacts with RASSF9 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi111101. 6 interactions.
    IntActiP19021. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP19021.
    SMRiP19021. Positions 40-351, 495-817.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 863833IntragranularSequence AnalysisAdd
    BLAST
    Topological domaini888 – 97386CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei864 – 88724HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati498 – 54144NHL 1Add
    BLAST
    Repeati567 – 60842NHL 2Add
    BLAST
    Repeati617 – 66246NHL 3Add
    BLAST
    Repeati670 – 71445NHL 4Add
    BLAST
    Repeati766 – 80944NHL 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 494494Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd
    BLAST
    Regioni495 – 817323Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd
    BLAST
    Regioni925 – 94218Interaction with RASSF9By similarityAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.Curated
    In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.Curated
    Contains 5 NHL repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3391.
    HOVERGENiHBG004218.
    KOiK00504.
    K18200.
    OMAiTVHHMLL.
    OrthoDBiEOG70ZZNT.
    PhylomeDBiP19021.
    TreeFamiTF320698.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR014784. Cu2_ascorb_mOase-like_C.
    IPR020611. Cu2_ascorb_mOase_CS-1.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR001258. NHL_repeat.
    IPR013017. NHL_repeat_subgr.
    IPR000720. Pep_amidat_mOase.
    IPR008977. PHM/PNGase_F_dom.
    [Graphical view]
    PfamiPF01082. Cu2_monooxygen. 1 hit.
    PF01436. NHL. 4 hits.
    [Graphical view]
    PRINTSiPR00790. PAMONOXGNASE.
    SUPFAMiSSF49742. SSF49742. 2 hits.
    PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
    PS00085. CU2_MONOOXYGENASE_2. 1 hit.
    PS51125. NHL. 5 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P19021-1) [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

    MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV    50
    PIDSSDFALD IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT 100
    VHHMLLFGCN MPSSTGSYWF CDEGTCTDKA NILYAWARNA PPTRLPKGVG 150
    FRVGGETGSK YFVLQVHYGD ISAFRDNNKD CSGVSLHLTR LPQPLIAGMY 200
    LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH LGKVVSGYRV 250
    RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 300
    IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP 350
    VKSDMVMMHE HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE 400
    REDVVHVHKY NPTEKAESES DLVAEIANVV QKKDLGRSDA REGAEHERGN 450
    AILVRDRIHK FHRLVSTLRP PESRVFSLQQ PPPGEGTWEP EHTGDFHMEE 500
    ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF DSKFVYQQIG 550
    LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 600
    QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG 650
    YCNSRIVQFS PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV 700
    ADRENGRIQC FKTDTKEFVR EIKHSSFGRN VFAISYIPGL LFAVNGKPHF 750
    GDQEPVQGFV MNFSNGEIID IFKPVRKHFD MPHDIVASED GTVYIGDAHT 800
    NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN KPTSSELQKM 850
    QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGDSEH 900
    KLETSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK 950
    EDDGSESEEE YSAPLPALAP SSS 973
    Length:973
    Mass (Da):108,332
    Last modified:September 19, 2002 - v2
    Checksum:i8A089B657F56EE39
    GO
    Isoform 2 (identifier: P19021-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         388-494: Missing.

    Show »
    Length:866
    Mass (Da):96,258
    Checksum:i41F0822F95AC3B0E
    GO
    Isoform 3 (identifier: P19021-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         829-896: Missing.

    Show »
    Length:905
    Mass (Da):100,818
    Checksum:i5A5EAAC529E267AE
    GO
    Isoform 4 (identifier: P19021-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         829-914: Missing.

    Show »
    Length:887
    Mass (Da):98,762
    Checksum:i5F3E355C256FF35C
    GO
    Isoform 5 (identifier: P19021-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         896-896: G → GA

    Show »
    Length:974
    Mass (Da):108,403
    Checksum:iF6D51C73F6E264A3
    GO
    Isoform 6 (identifier: P19021-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         897-914: Missing.

    Show »
    Length:955
    Mass (Da):106,276
    Checksum:iEE05609B9A7F1772
    GO

    Sequence cautioni

    The sequence AAD01439.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261S → P in BAF82847. (PubMed:14702039)Curated
    Sequence conflicti574 – 5741G → E in AAA36414. (PubMed:2357221)Curated
    Sequence conflicti774 – 7741P → L in BAF82847. (PubMed:14702039)Curated
    Sequence conflicti830 – 8312Missing in AAB32775. (PubMed:7999037)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491V → L.
    Corresponds to variant rs2230458 [ dbSNP | Ensembl ].
    VAR_055694

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei388 – 494107Missing in isoform 2. 2 PublicationsVSP_001227Add
    BLAST
    Alternative sequencei829 – 91486Missing in isoform 4. 1 PublicationVSP_001229Add
    BLAST
    Alternative sequencei829 – 89668Missing in isoform 3. 1 PublicationVSP_001228Add
    BLAST
    Alternative sequencei896 – 8961G → GA in isoform 5. 1 PublicationVSP_038691
    Alternative sequencei897 – 91418Missing in isoform 6. 1 PublicationVSP_042209Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37721 mRNA. Translation: AAA36414.1.
    S75037 mRNA. Translation: AAB32775.1.
    S75038 mRNA. Translation: AAB32776.1.
    AB095007 mRNA. Translation: BAC22594.1.
    AK290158 mRNA. Translation: BAF82847.1.
    BT007419 mRNA. Translation: AAP36087.1.
    AC008779 Genomic DNA. No translation available.
    AC010250 Genomic DNA. No translation available.
    AC113373 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW49085.1.
    BC018127 mRNA. Translation: AAH18127.1.
    AF010472 mRNA. Translation: AAD01439.1. Different initiation.
    AF035320 mRNA. Translation: AAB88190.1.
    CCDSiCCDS4092.1. [P19021-3]
    CCDS4093.1. [P19021-2]
    CCDS4094.1. [P19021-4]
    CCDS43348.1. [P19021-5]
    CCDS54885.1. [P19021-1]
    PIRiA35477. URHUAP.
    RefSeqiNP_000910.2. NM_000919.3. [P19021-5]
    NP_001170777.1. NM_001177306.1. [P19021-1]
    NP_620121.1. NM_138766.2. [P19021-3]
    NP_620176.1. NM_138821.2. [P19021-2]
    NP_620177.1. NM_138822.2. [P19021-4]
    XP_006714695.1. XM_006714632.1. [P19021-5]
    XP_006714696.1. XM_006714633.1. [P19021-5]
    XP_006714697.1. XM_006714634.1. [P19021-1]
    XP_006714701.1. XM_006714638.1. [P19021-3]
    XP_006714703.1. XM_006714640.1. [P19021-2]
    UniGeneiHs.369430.

    Genome annotation databases

    EnsembliENST00000304400; ENSP00000306100; ENSG00000145730. [P19021-5]
    ENST00000346918; ENSP00000282992; ENSG00000145730. [P19021-4]
    ENST00000348126; ENSP00000314638; ENSG00000145730. [P19021-2]
    ENST00000438793; ENSP00000396493; ENSG00000145730. [P19021-1]
    ENST00000455264; ENSP00000403461; ENSG00000145730. [P19021-3]
    GeneIDi5066.
    KEGGihsa:5066.
    UCSCiuc003kns.3. human. [P19021-2]
    uc003knt.3. human. [P19021-5]
    uc003knu.3. human. [P19021-3]
    uc003knv.3. human. [P19021-4]
    uc003knw.3. human. [P19021-1]

    Polymorphism databases

    DMDMi23503036.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37721 mRNA. Translation: AAA36414.1 .
    S75037 mRNA. Translation: AAB32775.1 .
    S75038 mRNA. Translation: AAB32776.1 .
    AB095007 mRNA. Translation: BAC22594.1 .
    AK290158 mRNA. Translation: BAF82847.1 .
    BT007419 mRNA. Translation: AAP36087.1 .
    AC008779 Genomic DNA. No translation available.
    AC010250 Genomic DNA. No translation available.
    AC113373 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW49085.1 .
    BC018127 mRNA. Translation: AAH18127.1 .
    AF010472 mRNA. Translation: AAD01439.1 . Different initiation.
    AF035320 mRNA. Translation: AAB88190.1 .
    CCDSi CCDS4092.1. [P19021-3 ]
    CCDS4093.1. [P19021-2 ]
    CCDS4094.1. [P19021-4 ]
    CCDS43348.1. [P19021-5 ]
    CCDS54885.1. [P19021-1 ]
    PIRi A35477. URHUAP.
    RefSeqi NP_000910.2. NM_000919.3. [P19021-5 ]
    NP_001170777.1. NM_001177306.1. [P19021-1 ]
    NP_620121.1. NM_138766.2. [P19021-3 ]
    NP_620176.1. NM_138821.2. [P19021-2 ]
    NP_620177.1. NM_138822.2. [P19021-4 ]
    XP_006714695.1. XM_006714632.1. [P19021-5 ]
    XP_006714696.1. XM_006714633.1. [P19021-5 ]
    XP_006714697.1. XM_006714634.1. [P19021-1 ]
    XP_006714701.1. XM_006714638.1. [P19021-3 ]
    XP_006714703.1. XM_006714640.1. [P19021-2 ]
    UniGenei Hs.369430.

    3D structure databases

    ProteinModelPortali P19021.
    SMRi P19021. Positions 40-351, 495-817.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111101. 6 interactions.
    IntActi P19021. 2 interactions.

    Chemistry

    BindingDBi P19021.
    ChEMBLi CHEMBL2544.
    DrugBanki DB00126. Vitamin C.

    PTM databases

    PhosphoSitei P19021.

    Polymorphism databases

    DMDMi 23503036.

    Proteomic databases

    MaxQBi P19021.
    PaxDbi P19021.
    PRIDEi P19021.

    Protocols and materials databases

    DNASUi 5066.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304400 ; ENSP00000306100 ; ENSG00000145730 . [P19021-5 ]
    ENST00000346918 ; ENSP00000282992 ; ENSG00000145730 . [P19021-4 ]
    ENST00000348126 ; ENSP00000314638 ; ENSG00000145730 . [P19021-2 ]
    ENST00000438793 ; ENSP00000396493 ; ENSG00000145730 . [P19021-1 ]
    ENST00000455264 ; ENSP00000403461 ; ENSG00000145730 . [P19021-3 ]
    GeneIDi 5066.
    KEGGi hsa:5066.
    UCSCi uc003kns.3. human. [P19021-2 ]
    uc003knt.3. human. [P19021-5 ]
    uc003knu.3. human. [P19021-3 ]
    uc003knv.3. human. [P19021-4 ]
    uc003knw.3. human. [P19021-1 ]

    Organism-specific databases

    CTDi 5066.
    GeneCardsi GC05P102089.
    HGNCi HGNC:8596. PAM.
    HPAi CAB026119.
    HPA042260.
    MIMi 170270. gene.
    neXtProti NX_P19021.
    PharmGKBi PA32926.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3391.
    HOVERGENi HBG004218.
    KOi K00504.
    K18200.
    OMAi TVHHMLL.
    OrthoDBi EOG70ZZNT.
    PhylomeDBi P19021.
    TreeFami TF320698.

    Enzyme and pathway databases

    SignaLinki P19021.

    Miscellaneous databases

    ChiTaRSi PAM. human.
    GeneWikii Peptidylglycine_alpha-amidating_monooxygenase.
    GenomeRNAii 5066.
    NextBioi 19512.
    PROi P19021.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19021.
    Bgeei P19021.
    CleanExi HS_PAM.
    Genevestigatori P19021.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR014784. Cu2_ascorb_mOase-like_C.
    IPR020611. Cu2_ascorb_mOase_CS-1.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR001258. NHL_repeat.
    IPR013017. NHL_repeat_subgr.
    IPR000720. Pep_amidat_mOase.
    IPR008977. PHM/PNGase_F_dom.
    [Graphical view ]
    Pfami PF01082. Cu2_monooxygen. 1 hit.
    PF01436. NHL. 4 hits.
    [Graphical view ]
    PRINTSi PR00790. PAMONOXGNASE.
    SUPFAMi SSF49742. SSF49742. 2 hits.
    PROSITEi PS00084. CU2_MONOOXYGENASE_1. 1 hit.
    PS00085. CU2_MONOOXYGENASE_2. 1 hit.
    PS51125. NHL. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells."
      Glauder J., Ragg H., Rauch J., Engels J.W.
      Biochem. Biophys. Res. Commun. 169:551-558(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Thyroid carcinoma.
    2. "Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase."
      Tateishi K., Arakawa F., Misumi Y., Treston A.M., Vos M., Matsuoka Y.
      Biochem. Biophys. Res. Commun. 205:282-290(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    3. "Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase."
      Satani M., Takahashi K., Sakamoto H., Harada S., Kaida Y., Noguchi M.
      Protein Expr. Purif. 28:293-302(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, ENZYME REGULATION.
      Tissue: Heart.
    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] (ISOFORM 1).
      Tissue: Thalamus.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. 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).
      Tissue: Lung.
    9. "The alpha-amidating monooxygenase gene of human kidney."
      Chung B.H., Oh G.H., Choi E.S.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-973 (ISOFORM 4).
      Tissue: Kidney.
    10. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 707-973 (ISOFORM 6).
      Tissue: Brain.
    11. "Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase."
      Yun H.Y., Keutmann H.T., Eipper B.A.
      J. Biol. Chem. 269:10946-10955(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-961.
    12. "The novel kinase peptidylglycine alpha-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine alpha-amidating monooxygenase."
      Caldwell B.D., Darlington D.N., Penzes P., Johnson R.C., Eipper B.A., Mains R.E.
      J. Biol. Chem. 274:34646-34656(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-943 AND SER-946 BY UHMK1.
    13. "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-946, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-929, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-942 AND SER-946, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMD_HUMAN
    AccessioniPrimary (citable) accession number: P19021
    Secondary accession number(s): A6NMR0
    , A8K293, O43211, O95080, Q16252, Q16253, Q54A45, Q86U53, Q8WVC7, Q9UCG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 169 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3