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P19021

- AMD_HUMAN

UniProt

P19021 - AMD_HUMAN

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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

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. 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
Complete GO annotation...

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: UniProtKB
  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
Complete GO annotation...

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

BgeeiP19021.
CleanExiHS_PAM.
ExpressionAtlasiP19021. baseline and differential.
GenevestigatoriP19021.

Organism-specific databases

HPAiCAB026119.
HPA042260.

Interactioni

Subunit structurei

Monomer. Interacts with RASSF9 (By similarity).By similarity

Protein-protein interaction databases

BioGridi111101. 16 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.
GeneTreeiENSGT00730000111058.
HOVERGENiHBG004218.
InParanoidiP19021.
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

        10         20         30         40         50
MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV
60 70 80 90 100
PIDSSDFALD IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT
110 120 130 140 150
VHHMLLFGCN MPSSTGSYWF CDEGTCTDKA NILYAWARNA PPTRLPKGVG
160 170 180 190 200
FRVGGETGSK YFVLQVHYGD ISAFRDNNKD CSGVSLHLTR LPQPLIAGMY
210 220 230 240 250
LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH LGKVVSGYRV
260 270 280 290 300
RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH
310 320 330 340 350
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP
360 370 380 390 400
VKSDMVMMHE HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE
410 420 430 440 450
REDVVHVHKY NPTEKAESES DLVAEIANVV QKKDLGRSDA REGAEHERGN
460 470 480 490 500
AILVRDRIHK FHRLVSTLRP PESRVFSLQQ PPPGEGTWEP EHTGDFHMEE
510 520 530 540 550
ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF DSKFVYQQIG
560 570 580 590 600
LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH
610 620 630 640 650
QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG
660 670 680 690 700
YCNSRIVQFS PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV
710 720 730 740 750
ADRENGRIQC FKTDTKEFVR EIKHSSFGRN VFAISYIPGL LFAVNGKPHF
760 770 780 790 800
GDQEPVQGFV MNFSNGEIID IFKPVRKHFD MPHDIVASED GTVYIGDAHT
810 820 830 840 850
NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN KPTSSELQKM
860 870 880 890 900
QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGDSEH
910 920 930 940 950
KLETSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK
960 970
EDDGSESEEE YSAPLPALAP SSS
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. 16 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.
GeneTreei ENSGT00730000111058.
HOVERGENi HBG004218.
InParanoidi P19021.
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

Bgeei P19021.
CleanExi HS_PAM.
ExpressionAtlasi P19021. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 170 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