Q9H4A4 (AMPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	650 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	leukotriene biosynthetic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred by curator PubMed 12119107. Source: UniProtKB
Cellular_component	extracellular region Inferred from sequence or structural similarity PubMed 9405297. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from sequence or structural similarity PubMed 9405297. Source: UniProtKB
Molecular_function	aminopeptidase activity Inferred from sequence or structural similarity PubMed 9405297. Source: UniProtKB epoxide hydrolase activity Non-traceable author statement PubMed 12119107. Source: UniProtKB metalloexopeptidase activity Non-traceable author statement PubMed 12119107. Source: UniProtKB zinc ion binding Non-traceable author statement PubMed 12119107. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 650	649	Aminopeptidase B		PRO_0000095088
Regions
	Region	298 – 302	5	Substrate binding By similarity
Sites
	Active site	326	1	Proton acceptor By similarity
	Metal binding	325	1	Zinc; catalytic By similarity
	Metal binding	329	1	Zinc; catalytic By similarity
	Metal binding	348	1	Zinc; catalytic By similarity
	Site	414	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7 Ref.9
	Modified residue	7	1	Phosphoserine Ref.7 Ref.9
	Modified residue	446	1	N6-acetyllysine Ref.6
Natural variations
	Natural variant	579	1	V → I. Corresponds to variant rs3820439 [ dbSNP | Ensembl ].		VAR_051566
Experimental info
	Sequence conflict	2	1	A → V in CAC14047. Ref.2
	Sequence conflict	11 – 14	4	GAAR → ARPGGRCTPRRL in CAC12957. Ref.1
	Sequence conflict	149	1	G → R in CAC12957. Ref.1
	Sequence conflict	153	1	L → V in CAC12957. Ref.1
	Sequence conflict	208 – 210	3	STW → RPG in CAC12957. Ref.1
	Sequence conflict	262	1	Missing in CAC12957. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H4A4 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: 4C04FE09689F2487	FASTA	650	72,596
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00642211.
PIR	T51870.
RefSeq	NP_064601.3. NM_020216.3.
UniGene	Hs.497391.
3D structure databases
ProteinModelPortal	Q9H4A4.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1182309.
STRING	9606.ENSP00000295640.
Protein family/group databases
MEROPS	M01.014.
PTM databases
PhosphoSite	Q9H4A4.
Polymorphism databases
DMDM	20137480.
Proteomic databases
PaxDb	Q9H4A4.
PRIDE	Q9H4A4.
Protocols and materials databases
DNASU	6051.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295640; ENSP00000295640; ENSG00000176393.
GeneID	6051.
KEGG	hsa:6051.
UCSC	uc001gxd.3. human.
Organism-specific databases
CTD	6051.
GeneCards	GC01P201951.
H-InvDB	HIX0023896.
HGNC	HGNC:10078. RNPEP.
HPA	HPA036075.
MIM	602675. gene.
neXtProt	NX_Q9H4A4.
PharmGKB	PA34451.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0308.
HOVERGEN	HBG001274.
InParanoid	Q9H4A4.
KO	K01260.
OMA	WGQIVLK.
OrthoDB	EOG4X6C7T.
PhylomeDB	Q9H4A4.
Gene expression databases
ArrayExpress	Q9H4A4.
Bgee	Q9H4A4.
CleanEx	HS_RNPEP.
Genevestigator	Q9H4A4.
GermOnline	ENSG00000176393. Homo sapiens.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR015571. Pept_M1_aminopeptidase-B. IPR001930. Peptidase_M1. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. PTHR11533. 1 hit. PTHR11533:SF5. PTHR11533:SF5. 1 hit.
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9H4A4.
ChEMBL	CHEMBL2432.
ChiTaRS	RNPEP. human.
GenomeRNAi	6051.
NextBio	23595.
SOURCE	Search...

Entry information

Entry name

AMPB_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.