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Q9H4A4 (AMPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase B

Short name=AP-B
EC=3.4.11.6
Alternative name(s):
Arginine aminopeptidase
Arginyl aminopeptidase
Gene names
Name:RNPEP
Synonyms:APB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 650649Aminopeptidase B
PRO_0000095088

Regions

Region298 – 3025Substrate binding By similarity

Sites

Active site3261Proton acceptor By similarity
Metal binding3251Zinc; catalytic By similarity
Metal binding3291Zinc; catalytic By similarity
Metal binding3481Zinc; catalytic By similarity
Site4141Transition state stabilizer By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.9
Modified residue71Phosphoserine Ref.7 Ref.9
Modified residue4461N6-acetyllysine Ref.6

Natural variations

Natural variant5791V → I.
Corresponds to variant rs3820439 [ dbSNP | Ensembl ].
VAR_051566

Experimental info

Sequence conflict21A → V in CAC14047. Ref.2
Sequence conflict11 – 144GAAR → ARPGGRCTPRRL in CAC12957. Ref.1
Sequence conflict1491G → R in CAC12957. Ref.1
Sequence conflict1531L → V in CAC12957. Ref.1
Sequence conflict208 – 2103STW → RPG in CAC12957. Ref.1
Sequence conflict2621Missing in CAC12957. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9H4A4 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 4C04FE09689F2487

FASTA65072,596
        10         20         30         40         50         60 
MASGEHSPGS GAARRPLHSA QAVDVASASN FRAFELLHLH LDLRAEFGPP GPGAGSRGLS 

        70         80         90        100        110        120 
GTAVLDLRCL EPEGAAELRL DSHPCLEVTA AALRRERPGS EEPPAEPVSF YTQPFSHYGQ 

       130        140        150        160        170        180 
ALCVSFPQPC RAAERLQVLL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP 

       190        200        210        220        230        240 
CFDTPAVKYK YSALIEVPDG FTAVMSASTW EKRGPNKFFF QMCQPIPSYL IALAIGDLVS 

       250        260        270        280        290        300 
AEVGPRSRVW AEPCLIDAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM 

       310        320        330        340        350        360 
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST 

       370        380        390        400        410        420 
ILFGAAYTCL EAATGRALLR QHMDITGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGFCF 

       430        440        450        460        470        480 
VSYLAHLVGD QDQFDSFLKA YVHEFKFRSI LADDFLDFYL EYFPELKKKR VDIIPGFEFD 

       490        500        510        520        530        540 
RWLNTPGWPP YLPDLSPGDS LMKPAEELAQ LWAAEELDMK AIEAVAISPW KTYQLVYFLD 

       550        560        570        580        590        600 
KILQKSPLPP GNVKKLGDTY PSISNARNAE LRLRWGQIVL KNDHQEDFWK VKEFLHNQGK 

       610        620        630        640        650 
QKYTLPLYHA MMGGSEVAQT LAKETFASTA SQLHSNVVNY VQQIVAPKGS 

« Hide

References

« Hide 'large scale' references
[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 (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human aminopeptidase B cDNA cloning."
Kristensen T.
Submitted (OCT-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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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(2006) [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(2009) [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(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].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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(2011) [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1418.1.
PIRT51870.
RefSeqNP_064601.3. NM_020216.3.
XP_005245477.1. XM_005245420.1.
XP_005245478.1. XM_005245421.1.
UniGeneHs.497391.

3D structure databases

ProteinModelPortalQ9H4A4.
SMRQ9H4A4. Positions 8-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111978. 4 interactions.
IntActQ9H4A4. 1 interaction.
MINTMINT-1182309.
STRING9606.ENSP00000295640.

Chemistry

BindingDBQ9H4A4.
ChEMBLCHEMBL2432.

Protein family/group databases

MEROPSM01.014.

PTM databases

PhosphoSiteQ9H4A4.

Polymorphism databases

DMDM20137480.

Proteomic databases

MaxQBQ9H4A4.
PaxDbQ9H4A4.
PRIDEQ9H4A4.

Protocols and materials databases

DNASU6051.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295640; ENSP00000295640; ENSG00000176393.
GeneID6051.
KEGGhsa:6051.
UCSCuc001gxd.3. human.

Organism-specific databases

CTD6051.
GeneCardsGC01P201951.
H-InvDBHIX0023896.
HGNCHGNC:10078. RNPEP.
HPAHPA036074.
HPA036075.
MIM602675. gene.
neXtProtNX_Q9H4A4.
PharmGKBPA34451.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0308.
HOVERGENHBG001274.
InParanoidQ9H4A4.
KOK01260.
OMAPPGNVKK.
OrthoDBEOG7SJD42.
PhylomeDBQ9H4A4.
TreeFamTF300758.

Gene expression databases

ArrayExpressQ9H4A4.
BgeeQ9H4A4.
CleanExHS_RNPEP.
GenevestigatorQ9H4A4.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR015571. Pept_M1_aminopeptidase-B.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF153. PTHR11533:SF153. 1 hit.
PfamPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNPEP. human.
GeneWikiRNPEP.
GenomeRNAi6051.
NextBio23595.
PROQ9H4A4.
SOURCESearch...

Entry information

Entry nameAMPB_HUMAN
AccessionPrimary (citable) accession number: Q9H4A4
Secondary accession number(s): Q9BVM9, Q9H1D4, Q9NPT7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: July 9, 2014
This is version 127 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

Peptidase families

Classification of peptidase families and list of entries

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 1

Human chromosome 1: entries, gene names and cross-references to MIM