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Protein

Aminopeptidase B

Gene

RNPEP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity).By similarity

Catalytic activityi

Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi325 – 3251Zinc; catalyticPROSITE-ProRule annotation
Active sitei326 – 3261Proton acceptorPROSITE-ProRule annotation
Metal bindingi329 – 3291Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi348 – 3481Zinc; catalyticPROSITE-ProRule annotation
Sitei414 – 4141Transition state stabilizerBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. epoxide hydrolase activity Source: UniProtKB
  3. metalloexopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. leukotriene biosynthetic process Source: InterPro
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase B (EC:3.4.11.6)
Short name:
AP-B
Alternative name(s):
Arginine aminopeptidase
Arginyl aminopeptidase
Gene namesi
Name:RNPEP
Synonyms:APB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10078. RNPEP.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: InterPro
  3. extracellular vesicular exosome Source: UniProtKB
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34451.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 650649Aminopeptidase BPRO_0000095088Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei7 – 71Phosphoserine2 Publications
Modified residuei446 – 4461N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H4A4.
PaxDbiQ9H4A4.
PRIDEiQ9H4A4.

PTM databases

PhosphoSiteiQ9H4A4.

Expressioni

Gene expression databases

BgeeiQ9H4A4.
CleanExiHS_RNPEP.
ExpressionAtlasiQ9H4A4. baseline.
GenevestigatoriQ9H4A4.

Organism-specific databases

HPAiHPA036074.
HPA036075.

Interactioni

Protein-protein interaction databases

BioGridi111978. 6 interactions.
IntActiQ9H4A4. 1 interaction.
MINTiMINT-1182309.
STRINGi9606.ENSP00000295640.

Structurei

3D structure databases

ProteinModelPortaliQ9H4A4.
SMRiQ9H4A4. Positions 22-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3025Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00530000063003.
HOVERGENiHBG001274.
InParanoidiQ9H4A4.
KOiK01260.
OMAiAISPWKT.
OrthoDBiEOG7SJD42.
PhylomeDBiQ9H4A4.
TreeFamiTF300758.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015571. Pept_M1_aminopeptidase-B.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF153. PTHR11533:SF153. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H4A4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGEHSPGS GAARRPLHSA QAVDVASASN FRAFELLHLH LDLRAEFGPP
60 70 80 90 100
GPGAGSRGLS GTAVLDLRCL EPEGAAELRL DSHPCLEVTA AALRRERPGS
110 120 130 140 150
EEPPAEPVSF YTQPFSHYGQ ALCVSFPQPC RAAERLQVLL TYRVGEGPGV
160 170 180 190 200
CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP CFDTPAVKYK YSALIEVPDG
210 220 230 240 250
FTAVMSASTW EKRGPNKFFF QMCQPIPSYL IALAIGDLVS AEVGPRSRVW
260 270 280 290 300
AEPCLIDAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM
310 320 330 340 350
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF
360 370 380 390 400
TMYAQRRIST ILFGAAYTCL EAATGRALLR QHMDITGEEN PLNKLRVKIE
410 420 430 440 450
PGVDPDDTYN ETPYEKGFCF VSYLAHLVGD QDQFDSFLKA YVHEFKFRSI
460 470 480 490 500
LADDFLDFYL EYFPELKKKR VDIIPGFEFD RWLNTPGWPP YLPDLSPGDS
510 520 530 540 550
LMKPAEELAQ LWAAEELDMK AIEAVAISPW KTYQLVYFLD KILQKSPLPP
560 570 580 590 600
GNVKKLGDTY PSISNARNAE LRLRWGQIVL KNDHQEDFWK VKEFLHNQGK
610 620 630 640 650
QKYTLPLYHA MMGGSEVAQT LAKETFASTA SQLHSNVVNY VQQIVAPKGS
Length:650
Mass (Da):72,596
Last modified:March 26, 2002 - v2
Checksum:i4C04FE09689F2487
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in CAC14047 (Ref. 2) Curated
Sequence conflicti11 – 144GAAR → ARPGGRCTPRRL in CAC12957 (Ref. 1) Curated
Sequence conflicti149 – 1491G → R in CAC12957 (Ref. 1) Curated
Sequence conflicti153 – 1531L → V in CAC12957 (Ref. 1) Curated
Sequence conflicti208 – 2103STW → RPG in CAC12957 (Ref. 1) Curated
Sequence conflicti262 – 2621Missing in CAC12957 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti579 – 5791V → I.
Corresponds to variant rs3820439 [ dbSNP | Ensembl ].
VAR_051566

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242586 mRNA. Translation: CAC12957.1.
AJ296161 mRNA. Translation: CAC14047.1.
BC001064 mRNA. Translation: AAH01064.1.
BC012166 mRNA. Translation: AAH12166.1.
AL390139 mRNA. Translation: CAB99087.1.
CCDSiCCDS1418.1.
PIRiT51870.
RefSeqiNP_064601.3. NM_020216.3.
XP_005245477.1. XM_005245420.1.
XP_005245478.1. XM_005245421.1.
UniGeneiHs.497391.

Genome annotation databases

EnsembliENST00000295640; ENSP00000295640; ENSG00000176393.
GeneIDi6051.
KEGGihsa:6051.
UCSCiuc001gxd.3. human.

Polymorphism databases

DMDMi20137480.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242586 mRNA. Translation: CAC12957.1.
AJ296161 mRNA. Translation: CAC14047.1.
BC001064 mRNA. Translation: AAH01064.1.
BC012166 mRNA. Translation: AAH12166.1.
AL390139 mRNA. Translation: CAB99087.1.
CCDSiCCDS1418.1.
PIRiT51870.
RefSeqiNP_064601.3. NM_020216.3.
XP_005245477.1. XM_005245420.1.
XP_005245478.1. XM_005245421.1.
UniGeneiHs.497391.

3D structure databases

ProteinModelPortaliQ9H4A4.
SMRiQ9H4A4. Positions 22-647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111978. 6 interactions.
IntActiQ9H4A4. 1 interaction.
MINTiMINT-1182309.
STRINGi9606.ENSP00000295640.

Chemistry

BindingDBiQ9H4A4.
ChEMBLiCHEMBL2432.

Protein family/group databases

MEROPSiM01.014.

PTM databases

PhosphoSiteiQ9H4A4.

Polymorphism databases

DMDMi20137480.

Proteomic databases

MaxQBiQ9H4A4.
PaxDbiQ9H4A4.
PRIDEiQ9H4A4.

Protocols and materials databases

DNASUi6051.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295640; ENSP00000295640; ENSG00000176393.
GeneIDi6051.
KEGGihsa:6051.
UCSCiuc001gxd.3. human.

Organism-specific databases

CTDi6051.
GeneCardsiGC01P201951.
H-InvDBHIX0023896.
HGNCiHGNC:10078. RNPEP.
HPAiHPA036074.
HPA036075.
MIMi602675. gene.
neXtProtiNX_Q9H4A4.
PharmGKBiPA34451.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00530000063003.
HOVERGENiHBG001274.
InParanoidiQ9H4A4.
KOiK01260.
OMAiAISPWKT.
OrthoDBiEOG7SJD42.
PhylomeDBiQ9H4A4.
TreeFamiTF300758.

Miscellaneous databases

ChiTaRSiRNPEP. human.
GeneWikiiRNPEP.
GenomeRNAii6051.
NextBioi23595.
PROiQ9H4A4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4A4.
CleanExiHS_RNPEP.
ExpressionAtlasiQ9H4A4. baseline.
GenevestigatoriQ9H4A4.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015571. Pept_M1_aminopeptidase-B.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF153. PTHR11533:SF153. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human aminopeptidase B on chromosome 1q32.2: cDNA, genomic structure and expression."
    Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S., Foulon T., Cohen P.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human aminopeptidase B cDNA cloning."
    Kristensen T.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-650.
    Tissue: Brain.
  5. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAMPB_HUMAN
AccessioniPrimary (citable) accession number: Q9H4A4
Secondary accession number(s): Q9BVM9, Q9H1D4, Q9NPT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 26, 2002
Last sequence update: March 26, 2002
Last modified: March 31, 2015
This is version 134 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.