PAM
entrez
5066
canonical
uniprot
P19021
canonical
ensembl
ENSG00000145730
resolver
ensp
ENSP00000282992
resolver
ensp
ENSP00000306100
resolver
ensp
ENSP00000314638
resolver
ensp
ENSP00000369125
resolver
ensp
ENSP00000396493
resolver
ensp
ENSP00000403461
resolver
ensp
ENSP00000506915
resolver
ensp
ENSP00000506966
resolver
ensp
ENSP00000507038
resolver
ensp
ENSP00000507172
resolver
ensp
ENSP00000507990
resolver
ensp
ENSP00000508091
resolver
ensp
ENSP00000560250
resolver
ensp
ENSP00000560251
resolver
ensp
ENSP00000560252
resolver
ensp
ENSP00000560253
resolver
ensp
ENSP00000560255
resolver
ensp
ENSP00000560256
resolver
ensp
ENSP00000560258
resolver
ensp
ENSP00000560259
resolver
ensp
ENSP00000560261
resolver
ensp
ENSP00000560262
resolver
ensp
ENSP00000560263
resolver
ensp
ENSP00000560264
resolver
ensp
ENSP00000560269
resolver
ensp
ENSP00000560273
resolver
ensp
ENSP00000560276
resolver
ensp
ENSP00000560277
resolver
ensp
ENSP00000560278
resolver
ensp
ENSP00000560279
resolver
ensp
ENSP00000560280
resolver
ensp
ENSP00000560281
resolver
ensp
ENSP00000609801
resolver
ensp
ENSP00000627544
resolver
ensp
ENSP00000627554
resolver
ensp
ENSP00000627562
resolver
ensp
ENSP00000627574
resolver
ensp
ENSP00000660415
resolver
ensp
ENSP00000660417
resolver
ensp
ENSP00000727753
resolver
ensp
ENSP00000727768
resolver
ensp
ENSP00000727786
resolver
enst
ENST00000304400
resolver
enst
ENST00000510208
resolver
enst
ENST00000682882
resolver
enst
ENST00000682972
resolver
enst
ENST00000890214
resolver
enst
ENST00000890219
resolver
enst
ENST00000957515
resolver
genesymbol
PAM
resolver
hgnc
HGNC:8596
resolver
uniprot
A0A804HIQ0
resolver
uniprot
A0A804HKM7
resolver
uniprot
A0A804HKV8
resolver
uniprot
A0A8C8KD64
resolver
uniprot
A6NMR0
resolver
uniprot
A8K293
resolver
uniprot
O43211
resolver
uniprot
O43832
resolver
uniprot
O95080
resolver
uniprot
Q16252
resolver
uniprot
Q16253
resolver
uniprot
Q54A45
resolver
uniprot
Q86U53
resolver
uniprot
Q8WVC7
resolver
uniprot
Q9UCG0
resolver
uniprot_entry
A0A804HIQ0_HUMAN
resolver
uniprot_entry
A0A804HKM7_HUMAN
resolver
uniprot_entry
A0A804HKV8_HUMAN
resolver
uniprot_entry
A0A8C8KD64_HUMAN
resolver
uniprot_entry
AMD_HUMAN
resolver
uniprot_entry
O43832_HUMAN
resolver
uniprot_sec
A6NMR0
resolver
uniprot_sec
A8K293
resolver
uniprot_sec
O43211
resolver
uniprot_sec
O95080
resolver
uniprot_sec
Q16252
resolver
uniprot_sec
Q16253
resolver
uniprot_sec
Q54A45
resolver
uniprot_sec
Q86U53
resolver
uniprot_sec
Q8WVC7
resolver
uniprot_sec
Q9UCG0
resolver
activity_regulation
ACTIVITY REGULATION: PAM activity is inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate (PubMed:12699694). PAL activity is stimulated by cadmium and inhibited by mercury (By similarity). {ECO:0000250|UniProtKB:P14925, ECO:0000269|PubMed:12699694}.
uniprot
proteins
amino_acid_sequence
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHEHHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQPPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSFDSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVREIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMENKPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS
uniprot
proteins
ec_number
1.14.17.3
uniprot
proteins
ec_number
4.3.2.5
uniprot
proteins
function
FUNCTION: Bifunctional enzyme that catalyzes amidation of the C-terminus of proteins (PubMed:12699694, PubMed:2357221). Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity (PubMed:1575450). C-terminal amidation also takes place in response to protein fragmentation triggered by oxidative stress, promoting degradation of amidated protein fragments by the proteasome (PubMed:2207077). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme (PubMed:12699694). The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:12699694). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:12699694). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity). {ECO:0000250|UniProtKB:P14925, ECO:0000269|PubMed:12699694, ECO:0000269|PubMed:2357221, ECO:0000303|PubMed:1575450, ECO:0000303|PubMed:2207077}.
uniprot
proteins
mass_dalton
108332
uniprot
proteins
protein_family
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family
uniprot
proteins
pubmed
10574929
uniprot
proteins
pubmed
12699694
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1575450
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
2207077
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2357221
uniprot
proteins
pubmed
7999037
uniprot
proteins
pubmed
8144680
uniprot
proteins
pubmed
9110174
uniprot
proteins
sequence_length
973
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules. {ECO:0000250|UniProtKB:P10731}.; SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Note=Secreted from secretory granules.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted. Note=Secreted from secretory granules.
uniprot
proteins
transmembrane_region
TRANSMEM 864..887; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins