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P19021 (AMD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-glycine alpha-amidating monooxygenase

Short name=PAM

Including the following 2 domains:

  1. Peptidylglycine alpha-hydroxylating monooxygenase
    Short name=PHM
    EC=1.14.17.3
  2. Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
    EC=4.3.2.5
    Alternative name(s):
    Peptidylamidoglycolate lyase
    Short name=PAL
Gene names
Name:PAM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length973 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Peptidylamidoglycolate = peptidyl amide + glyoxylate.

Cofactor

Zinc; for the lyase reaction. Ref.3

Binds 2 copper ions per subunit; For the monoxygenase reaction. Ref.3

Enzyme regulation

Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate. Ref.3

Subunit structure

Monomer. Interacts with RASSF9 By similarity.

Subcellular location

Isoform 1: Membrane; Single-pass type I membrane protein.

Isoform 2: Membrane; Single-pass type I membrane protein.

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

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

Sequence similarities

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

Contains 5 NHL repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
Vitamin C
Zinc
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcentral nervous system development

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

limb development

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

odontogenesis

Inferred from electronic annotation. Source: Ensembl

ovulation cycle process

Inferred from electronic annotation. Source: Ensembl

peptide amidation

Inferred from direct assay Ref.3Ref.1. Source: UniProt

protein amidation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

toxin metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

secretory granule membrane

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

copper ion binding

Inferred from electronic annotation. Source: InterPro

peptidylamidoglycolate lyase activity

Inferred from direct assay Ref.3. Source: UniProt

peptidylglycine monooxygenase activity

Inferred from direct assay Ref.3Ref.1. Source: UniProt

zinc ion binding

Inferred from direct assay Ref.3. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P19021-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P19021-2)

The sequence of this isoform differs from the canonical sequence as follows:
     388-494: Missing.
Isoform 3 (identifier: P19021-3)

The sequence of this isoform differs from the canonical sequence as follows:
     829-896: Missing.
Isoform 4 (identifier: P19021-4)

The sequence of this isoform differs from the canonical sequence as follows:
     829-914: Missing.
Isoform 5 (identifier: P19021-5)

The sequence of this isoform differs from the canonical sequence as follows:
     896-896: G → GA
Isoform 6 (identifier: P19021-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Probable
Propeptide21 – 3010 Probable
PRO_0000006361
Chain31 – 973943Peptidyl-glycine alpha-amidating monooxygenase
PRO_0000006362

Regions

Topological domain31 – 863833Intragranular Potential
Transmembrane864 – 88724Helical; Potential
Topological domain888 – 97386Cytoplasmic Potential
Repeat498 – 54144NHL 1
Repeat567 – 60842NHL 2
Repeat617 – 66246NHL 3
Repeat670 – 71445NHL 4
Repeat766 – 80944NHL 5
Region1 – 494494Peptidylglycine alpha-hydroxylating monooxygenase By similarity
Region495 – 817323Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarity
Region925 – 94218Interaction with RASSF9 By similarity

Sites

Metal binding1021Copper A By similarity
Metal binding1031Copper A By similarity
Metal binding1671Copper A By similarity
Metal binding2371Copper B By similarity
Metal binding2391Copper B By similarity
Metal binding3091Copper B By similarity

Amino acid modifications

Modified residue9291Phosphoserine Ref.14
Modified residue9421Phosphoserine Ref.15
Modified residue9431Phosphothreonine Ref.12
Modified residue9461Phosphoserine; by UHMK1; in vitro Ref.12 Ref.13 Ref.15
Modified residue9611Sulfotyrosine Ref.11
Glycosylation7621N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 181 By similarity
Disulfide bond76 ↔ 121 By similarity
Disulfide bond109 ↔ 126 By similarity
Disulfide bond222 ↔ 329 By similarity
Disulfide bond288 ↔ 310 By similarity
Disulfide bond631 ↔ 652 By similarity
Disulfide bond699 ↔ 710 By similarity

Natural variations

Alternative sequence388 – 494107Missing in isoform 2.
VSP_001227
Alternative sequence829 – 91486Missing in isoform 4.
VSP_001229
Alternative sequence829 – 89668Missing in isoform 3.
VSP_001228
Alternative sequence8961G → GA in isoform 5.
VSP_038691
Alternative sequence897 – 91418Missing in isoform 6.
VSP_042209
Natural variant491V → L.
Corresponds to variant rs2230458 [ dbSNP | Ensembl ].
VAR_055694

Experimental info

Sequence conflict261S → P in BAF82847. Ref.4
Sequence conflict5741G → E in AAA36414. Ref.1
Sequence conflict7741P → L in BAF82847. Ref.4
Sequence conflict830 – 8312Missing in AAB32775. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 8A089B657F56EE39

FASTA973108,332
        10         20         30         40         50         60 
MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 

        70         80         90        100        110        120 
IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 

       130        140        150        160        170        180 
CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 

       190        200        210        220        230        240 
CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 

       250        260        270        280        290        300 
LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 

       310        320        330        340        350        360 
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 

       370        380        390        400        410        420 
HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 

       430        440        450        460        470        480 
DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 

       490        500        510        520        530        540 
PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 

       550        560        570        580        590        600 
DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 

       610        620        630        640        650        660 
QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 

       670        680        690        700        710        720 
PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 

       730        740        750        760        770        780 
EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 

       790        800        810        820        830        840 
MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN 

       850        860        870        880        890        900 
KPTSSELQKM QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGDSEH 

       910        920        930        940        950        960 
KLETSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK EDDGSESEEE 

       970 
YSAPLPALAP SSS 

« Hide

Isoform 2 [UniParc].

Checksum: 41F0822F95AC3B0E
Show »

FASTA86696,258
Isoform 3 [UniParc].

Checksum: 5A5EAAC529E267AE
Show »

FASTA905100,818
Isoform 4 [UniParc].

Checksum: 5F3E355C256FF35C
Show »

FASTA88798,762
Isoform 5 [UniParc].

Checksum: F6D51C73F6E264A3
Show »

FASTA974108,403
Isoform 6 [UniParc].

Checksum: EE05609B9A7F1772
Show »

FASTA955106,276

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRURHUAP. A35477.
RefSeqNP_000910.2. NM_000919.3.
NP_001170777.1. NM_001177306.1.
NP_620121.1. NM_138766.2.
NP_620176.1. NM_138821.2.
NP_620177.1. NM_138822.2.
UniGeneHs.369430.

3D structure databases

ProteinModelPortalP19021.
SMRP19021. Positions 40-351, 495-817.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111101. 6 interactions.
IntActP19021. 2 interactions.

Chemistry

BindingDBP19021.
ChEMBLCHEMBL2544.
DrugBankDB00126. Vitamin C.

PTM databases

PhosphoSiteP19021.

Polymorphism databases

DMDM23503036.

Proteomic databases

PaxDbP19021.
PRIDEP19021.

Protocols and materials databases

DNASU5066.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304400; ENSP00000306100; ENSG00000145730. [P19021-5]
ENST00000346918; ENSP00000282992; ENSG00000145730. [P19021-4]
ENST00000348126; ENSP00000314638; ENSG00000145730. [P19021-2]
ENST00000438793; ENSP00000396493; ENSG00000145730. [P19021-1]
ENST00000455264; ENSP00000403461; ENSG00000145730. [P19021-3]
GeneID5066.
KEGGhsa:5066.
UCSCuc003kns.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

CTD5066.
GeneCardsGC05P102089.
HGNCHGNC:8596. PAM.
HPACAB026119.
HPA042260.
MIM170270. gene.
neXtProtNX_P19021.
PharmGKBPA32926.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3391.
HOVERGENHBG004218.
KOK00504.
OMATVHHMLL.
OrthoDBEOG70ZZNT.
TreeFamTF320698.

Enzyme and pathway databases

SignaLinkP19021.

Gene expression databases

ArrayExpressP19021.
BgeeP19021.
CleanExHS_PAM.
GenevestigatorP19021.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProIPR011042. 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]
PfamPF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]
PRINTSPR00790. PAMONOXGNASE.
SUPFAMSSF49742. SSF49742. 2 hits.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAM. human.
GeneWikiPeptidylglycine_alpha-amidating_monooxygenase.
GenomeRNAi5066.
NextBio19512.
PROP19021.
SOURCESearch...

Entry information

Entry nameAMD_HUMAN
AccessionPrimary (citable) accession number: P19021
Secondary accession number(s): A6NMR0 expand/collapse secondary AC list , A8K293, O43211, O95080, Q16252, Q16253, Q54A45, Q86U53, Q8WVC7, Q9UCG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 19, 2002
Last modified: March 19, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM