AMPB_HUMAN
ID AMPB_HUMAN Reviewed; 650 AA.
AC Q9H4A4; Q9BVM9; Q9H1D4; Q9NPT7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Aminopeptidase B;
DE Short=AP-B;
DE EC=3.4.11.6;
DE AltName: Full=Arginine aminopeptidase;
DE AltName: Full=Arginyl aminopeptidase;
GN Name=RNPEP; Synonyms=APB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S., Foulon T.,
RA Cohen P.;
RT "Human aminopeptidase B on chromosome 1q32.2: cDNA, genomic structure and
RT expression.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Kristensen T.;
RT "Human aminopeptidase B cDNA cloning.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-650.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Exopeptidase which selectively removes arginine and/or lysine
CC residues from the N-terminus of several peptide substrates including
CC Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-
CC somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene
CC B4 (LTB-4) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1'
CC is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AJ242586; CAC12957.1; -; mRNA.
DR EMBL; AJ296161; CAC14047.1; -; mRNA.
DR EMBL; BC001064; AAH01064.1; -; mRNA.
DR EMBL; BC012166; AAH12166.1; -; mRNA.
DR EMBL; AL390139; CAB99087.1; -; mRNA.
DR CCDS; CCDS1418.1; -.
DR PIR; T51870; T51870.
DR RefSeq; NP_001306111.1; NM_001319182.1.
DR RefSeq; NP_001306112.1; NM_001319183.1.
DR RefSeq; NP_001306113.1; NM_001319184.1.
DR RefSeq; NP_064601.3; NM_020216.3.
DR RefSeq; XP_005245478.1; XM_005245421.1.
DR RefSeq; XP_016857511.1; XM_017002022.1.
DR AlphaFoldDB; Q9H4A4; -.
DR SMR; Q9H4A4; -.
DR BioGRID; 111978; 27.
DR IntAct; Q9H4A4; 5.
DR MINT; Q9H4A4; -.
DR STRING; 9606.ENSP00000295640; -.
DR BindingDB; Q9H4A4; -.
DR ChEMBL; CHEMBL2432; -.
DR MEROPS; M01.014; -.
DR GlyGen; Q9H4A4; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9H4A4; -.
DR MetOSite; Q9H4A4; -.
DR PhosphoSitePlus; Q9H4A4; -.
DR SwissPalm; Q9H4A4; -.
DR BioMuta; RNPEP; -.
DR DMDM; 20137480; -.
DR EPD; Q9H4A4; -.
DR jPOST; Q9H4A4; -.
DR MassIVE; Q9H4A4; -.
DR MaxQB; Q9H4A4; -.
DR PaxDb; Q9H4A4; -.
DR PeptideAtlas; Q9H4A4; -.
DR PRIDE; Q9H4A4; -.
DR ProteomicsDB; 80809; -.
DR TopDownProteomics; Q9H4A4; -.
DR Antibodypedia; 34521; 216 antibodies from 25 providers.
DR DNASU; 6051; -.
DR Ensembl; ENST00000295640.9; ENSP00000295640.4; ENSG00000176393.11.
DR GeneID; 6051; -.
DR KEGG; hsa:6051; -.
DR MANE-Select; ENST00000295640.9; ENSP00000295640.4; NM_020216.4; NP_064601.3.
DR UCSC; uc001gxd.4; human.
DR CTD; 6051; -.
DR DisGeNET; 6051; -.
DR GeneCards; RNPEP; -.
DR HGNC; HGNC:10078; RNPEP.
DR HPA; ENSG00000176393; Low tissue specificity.
DR MIM; 602675; gene.
DR neXtProt; NX_Q9H4A4; -.
DR OpenTargets; ENSG00000176393; -.
DR PharmGKB; PA34451; -.
DR VEuPathDB; HostDB:ENSG00000176393; -.
DR eggNOG; KOG1047; Eukaryota.
DR GeneTree; ENSGT00940000160431; -.
DR HOGENOM; CLU_014505_2_1_1; -.
DR InParanoid; Q9H4A4; -.
DR OMA; FEMEKPI; -.
DR OrthoDB; 775595at2759; -.
DR PhylomeDB; Q9H4A4; -.
DR TreeFam; TF300758; -.
DR BRENDA; 3.4.11.6; 2681.
DR PathwayCommons; Q9H4A4; -.
DR SignaLink; Q9H4A4; -.
DR BioGRID-ORCS; 6051; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; RNPEP; human.
DR GeneWiki; RNPEP; -.
DR GenomeRNAi; 6051; -.
DR Pharos; Q9H4A4; Tchem.
DR PRO; PR:Q9H4A4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H4A4; protein.
DR Bgee; ENSG00000176393; Expressed in mucosa of transverse colon and 95 other tissues.
DR ExpressionAtlas; Q9H4A4; baseline and differential.
DR Genevisible; Q9H4A4; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004301; F:epoxide hydrolase activity; NAS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR015571; Pept_M1_aminopeptidase-B.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; PTHR45726; 1.
DR PANTHER; PTHR45726:SF1; PTHR45726:SF1; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Secreted; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..650
FT /note="Aminopeptidase B"
FT /id="PRO_0000095088"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 298..302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 414
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 579
FT /note="V -> I (in dbSNP:rs3820439)"
FT /id="VAR_051566"
FT CONFLICT 2
FT /note="A -> V (in Ref. 2; CAC14047)"
FT /evidence="ECO:0000305"
FT CONFLICT 11..14
FT /note="GAAR -> ARPGGRCTPRRL (in Ref. 1; CAC12957)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="G -> R (in Ref. 1; CAC12957)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="L -> V (in Ref. 1; CAC12957)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..210
FT /note="STW -> RPG (in Ref. 1; CAC12957)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="Missing (in Ref. 1; CAC12957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 72596 MW; 4C04FE09689F2487 CRC64;
MASGEHSPGS GAARRPLHSA QAVDVASASN FRAFELLHLH LDLRAEFGPP GPGAGSRGLS
GTAVLDLRCL EPEGAAELRL DSHPCLEVTA AALRRERPGS EEPPAEPVSF YTQPFSHYGQ
ALCVSFPQPC RAAERLQVLL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP
CFDTPAVKYK YSALIEVPDG FTAVMSASTW EKRGPNKFFF QMCQPIPSYL IALAIGDLVS
AEVGPRSRVW AEPCLIDAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST
ILFGAAYTCL EAATGRALLR QHMDITGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGFCF
VSYLAHLVGD QDQFDSFLKA YVHEFKFRSI LADDFLDFYL EYFPELKKKR VDIIPGFEFD
RWLNTPGWPP YLPDLSPGDS LMKPAEELAQ LWAAEELDMK AIEAVAISPW KTYQLVYFLD
KILQKSPLPP GNVKKLGDTY PSISNARNAE LRLRWGQIVL KNDHQEDFWK VKEFLHNQGK
QKYTLPLYHA MMGGSEVAQT LAKETFASTA SQLHSNVVNY VQQIVAPKGS
