CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004280
UniProt Accession
Genbank Protein ID
 U52650; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52653; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52651; U52652; U52664; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52651; U52652; U52653; U52654; U52655; U52656; U52657; U52658; U52659; U52660; U52661; U52662; U52663; U52664; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52651; U52652; U52654; U52655; U52656; U52657; U52658; U52659; U52660; U52661; U52662; U52663; U52664; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52651; U52652; U52654; U52655; U52656; U52657; U52658; U52659; U52660; U52661; U52662; U52664; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52651; U52652; U52654; U52655; U52656; U52657; U52658; U52659; U52660; U52661; U52664; U52639; U52640; U52641; U52642; U52643; U52644; U52645; U52646; U52647; U52648; U52649; U52651; U52652; U52654; U52655; U52656; U52657; U52658; U52659; U52660; U52661; U52663; M25732; M25719; M63662; X59685; X59686; X59687; X59688; X59689; M82845 
Genbank Nucleotide ID
 AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05602.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05603.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05607.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05605.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05604.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05608.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAC05606.1; AAA41803.1; AAA41804.1; AAA42068.1; CAA42206.1; CAA42207.1; CAA42208.1; CAA42209.1; CAA42210.1; AAB00162.1 
Protein Name
 Peptidyl-glycine alpha-amidating monooxygenase 
Protein Synonyms/Alias
 PAM; Peptidylglycine alpha-hydroxylating monooxygenase; PHM; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidylamidoglycolate lyase; PAL 
Gene Name
 Pam 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
904AFGDHDRKLESSSGRubiquitination[1]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 501 544 NHL 1.
 REPEAT 570 611 NHL 2.
 REPEAT 620 665 NHL 3.
 REPEAT 673 717 NHL 4.
 REPEAT 769 812 NHL 5.
 REGION 1 497 Peptidylglycine alpha-hydroxylating
 REGION 498 820 Peptidyl-alpha-hydroxyglycine alpha-
 REGION 928 945 Interaction with RASSF9.
 METAL 107 107 Copper A.
 METAL 108 108 Copper A.
 METAL 172 172 Copper A.
 METAL 242 242 Copper B.
 METAL 244 244 Copper B.
 METAL 314 314 Copper B.
 MOD_RES 921 921 Phosphoserine (By similarity).
 MOD_RES 932 932 Phosphoserine (By similarity).
 MOD_RES 945 945 Phosphoserine (By similarity).
 MOD_RES 946 946 Phosphothreonine (By similarity).
 MOD_RES 949 949 Phosphoserine; by UHMK1 (By similarity).
 MOD_RES 965 965 Sulfotyrosine (By similarity).
 CARBOHYD 765 765 N-linked (GlcNAc...).
 DISULFID 47 186
 DISULFID 81 126
 DISULFID 114 131
 DISULFID 227 334
 DISULFID 293 315
 DISULFID 634 655
 DISULFID 702 713  
Keyword
 3D-structure; Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Copper; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Signal; Sulfation; Transmembrane; Transmembrane helix; Vitamin C; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 976 AA 
Protein Sequence
MAGRARSGLL LLLLGLLALQ SSCLAFRSPL SVFKRFKETT RSFSNECLGT IGPVTPLDAS 60
DFALDIRMPG VTPKESDTYF CMSMRLPVDE EAFVIDFKPR ASMDTVHHML LFGCNMPSST 120
GSYWFCDEGT CTDKANILYA WARNAPPTRL PKGVGFRVGG ETGSKYFVLQ VHYGDISAFR 180
DNHKDCSGVS VHLTRVPQPL IAGMYLMMSV DTVIPPGEKV VNADISCQYK MYPMHVFAYR 240
VHTHHLGKVV SGYRVRNGQW TLIGRQNPQL PQAFYPVEHP VDVTFGDILA ARCVFTGEGR 300
TEATHIGGTS SDEMCNLYIM YYMEAKYALS FMTCTKNVAP DMFRTIPAEA NIPIPVKPDM 360
VMMHGHHKEA ENKEKSALMQ QPKQGEEEVL EQGDFYSLLS KLLGEREDVH VHKYNPTEKT 420
ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEWGNAILVR DRIHRFHQLE STLRPAESRA 480
FSFQQPGEGP WEPEPSGDFH VEEELDWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG 540
NSFDSKFVYQ QRGLGPIEED TILVIDPNNA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 600
ALHQVFKLDP HSKEGPLLIL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV 660
QFSPSGKFVT QWGEESSGSS PRPGQFSVPH SLALVPHLDQ LCVADRENGR IQCFKTDTKE 720
FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK 780
HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTEKMEHRSV KKAGIEVQEI KEAEAVVEPK 840
VENKPTSSEL QKMQEKQKLS TEPGSGVSVV LITTLLVIPV LVLLAIVMFI RWKKSRAFGD 900
HDRKLESSSG RVLGRFRGKG SGGLNLGNFF ASRKGYSRKG FDRVSTEGSD QEKDEDDGTE 960
SEEEYSAPLP KPAPSS 976 
Gene Ontology
 GO:0009986; C:cell surface; IDA:RGD.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043005; C:neuron projection; IDA:RGD.
 GO:0043204; C:perikaryon; IDA:RGD.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO:0005886; C:plasma membrane; IDA:RGD.
 GO:0030667; C:secretory granule membrane; IDA:RGD.
 GO:0005802; C:trans-Golgi network; IDA:RGD.
 GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IDA:RGD.
 GO:0005507; F:copper ion binding; IDA:RGD.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0004598; F:peptidylamidoglycolate lyase activity; IDA:RGD.
 GO:0004504; F:peptidylglycine monooxygenase activity; IDA:RGD.
 GO:0008270; F:zinc ion binding; IDA:RGD.
 GO:0007417; P:central nervous system development; IEP:RGD.
 GO:0007507; P:heart development; IEP:RGD.
 GO:0007595; P:lactation; IEP:RGD.
 GO:0060173; P:limb development; IEP:RGD.
 GO:0001676; P:long-chain fatty acid metabolic process; IDA:RGD.
 GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
 GO:0042476; P:odontogenesis; IEP:RGD.
 GO:0022602; P:ovulation cycle process; IEP:RGD.
 GO:0001519; P:peptide amidation; IDA:RGD.
 GO:0018032; P:protein amidation; IDA:RGD.
 GO:0051260; P:protein homooligomerization; IDA:RGD.
 GO:0032956; P:regulation of actin cytoskeleton organization; IMP:RGD.
 GO:0050708; P:regulation of protein secretion; IMP:RGD.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:RGD.
 GO:0046688; P:response to copper ion; IEP:RGD.
 GO:0042493; P:response to drug; IDA:RGD.
 GO:0032355; P:response to estradiol stimulus; IEP:RGD.
 GO:0051384; P:response to glucocorticoid stimulus; IEP:RGD.
 GO:0001666; P:response to hypoxia; IEP:RGD.
 GO:0009268; P:response to pH; IDA:RGD.
 GO:0009404; P:toxin metabolic process; IDA:RGD. 
Interpro
 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. 
Pfam
 PF01082; Cu2_monooxygen
 PF01436; NHL 
SMART
  
PROSITE
 PS00084; CU2_MONOOXYGENASE_1
 PS00085; CU2_MONOOXYGENASE_2
 PS51125; NHL 
PRINTS
 PR00790; PAMONOXGNASE.