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Q5T6H7

- Q5T6H7_HUMAN

UniProt

Q5T6H7 - Q5T6H7_HUMAN

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Protein
Submitted name: Xaa-Pro aminopeptidase 1
Gene
XPNPEP1
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. aminopeptidase activity Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Ligandi

Metal-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Submitted name:
Xaa-Pro aminopeptidase 1Imported
Gene namesi
Name:XPNPEP1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:12822. XPNPEP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Ensembl
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiQ5T6H7.

Expressioni

Gene expression databases

ArrayExpressiQ5T6H7.

Interactioni

Protein-protein interaction databases

MINTiMINT-1382650.

Structurei

3D structure databases

ProteinModelPortaliQ5T6H7.
SMRiQ5T6H7. Positions 1-548.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24B family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG002934.
KOiK01262.
OrthoDBiEOG7BGHK4.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR000587. Creatinase_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5T6H7-1 [UniParc]FASTAAdd to Basket

« Hide

MWTDGRYFLQ AAKQMDSNWT LMKMGLKDTP TQEDWLVSVL PEGSRVGVDP    50
LIIPTDYWKK MAKVLRSAGH HLIPVKENLV DKIWTDRPER PCKPLLTLGL 100
DYTGISWKDK VADLRLKMAE RNVMWFVVTA LDEIAWLFNL RGSDVEHNPV 150
FFSYAIIGLE TIMLFIDGDR IDAPSVKEHL LLDLGLEAEY RIQVHPYKSI 200
LSELKALCAD LSPREKVWVS DKASYAVSET IPKDHRCCMP YTPICIAKAV 250
KNSAESEGMR RAHIKDAVAL CELFNWLEKE VPKGGVTEIS AADKAEEFRR 300
QQADFVDLSF PTISSTGPNG AIIHYAPVPE TNRTLSLDEV YLIDSGAQYK 350
DGTTDVTRTM HFGTPTAYEK ECFTYVLKGH IAVSAAVFPT GTKGHLLDSF 400
ARSALWDSGL DYLHGTGHGV GSFLNVHEGP CGISYKTFSD EPLEAGMIVT 450
DEPGYYEDGA FGIRIENVVL VVPVKTKYNF NNRGSLTFEP LTLVPIQTKM 500
IDVDSLTDKE CDWLNNYHLT CRDVIGKELQ KQGRQEALEW LIRETQPISK 550
QH 552
Length:552
Mass (Da):62,139
Last modified:December 21, 2004 - v1
Checksum:i627539255505E5CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL354951 Genomic DNA. No translation available.
RefSeqiXP_006718026.1. XM_006717963.1.
UniGeneiHs.390623.

Genome annotation databases

EnsembliENST00000369683; ENSP00000358697; ENSG00000108039.
GeneIDi7511.
KEGGihsa:7511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL354951 Genomic DNA. No translation available.
RefSeqi XP_006718026.1. XM_006717963.1.
UniGenei Hs.390623.

3D structure databases

ProteinModelPortali Q5T6H7.
SMRi Q5T6H7. Positions 1-548.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1382650.

Proteomic databases

PRIDEi Q5T6H7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369683 ; ENSP00000358697 ; ENSG00000108039 .
GeneIDi 7511.
KEGGi hsa:7511.

Organism-specific databases

CTDi 7511.
HGNCi HGNC:12822. XPNPEP1.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG002934.
KOi K01262.
OrthoDBi EOG7BGHK4.

Miscellaneous databases

ChiTaRSi XPNPEP1. human.

Gene expression databases

ArrayExpressi Q5T6H7.

Family and domain databases

Gene3Di 3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProi IPR029149. Creatin/AminoP/Spt16_NTD.
IPR000587. Creatinase_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view ]
Pfami PF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
SUPFAMi SSF55920. SSF55920. 1 hit.
PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiQ5T6H7_HUMAN
AccessioniPrimary (citable) accession number: Q5T6H7
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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