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Protein
Submitted name:

Xaa-Pro aminopeptidase 1

Gene

XPNPEP1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:12822. XPNPEP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiQ5T6H7.

Expressioni

Gene expression databases

BgeeiQ5T6H7.
ExpressionAtlasiQ5T6H7. baseline and differential.

Interactioni

Protein-protein interaction databases

MINTiMINT-1382650.
STRINGi9606.ENSP00000421566.

Structurei

3D structure databases

ProteinModelPortaliQ5T6H7.
SMRiQ5T6H7. Positions 1-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24B family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000013970.
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

        10         20         30         40         50
MWTDGRYFLQ AAKQMDSNWT LMKMGLKDTP TQEDWLVSVL PEGSRVGVDP
60 70 80 90 100
LIIPTDYWKK MAKVLRSAGH HLIPVKENLV DKIWTDRPER PCKPLLTLGL
110 120 130 140 150
DYTGISWKDK VADLRLKMAE RNVMWFVVTA LDEIAWLFNL RGSDVEHNPV
160 170 180 190 200
FFSYAIIGLE TIMLFIDGDR IDAPSVKEHL LLDLGLEAEY RIQVHPYKSI
210 220 230 240 250
LSELKALCAD LSPREKVWVS DKASYAVSET IPKDHRCCMP YTPICIAKAV
260 270 280 290 300
KNSAESEGMR RAHIKDAVAL CELFNWLEKE VPKGGVTEIS AADKAEEFRR
310 320 330 340 350
QQADFVDLSF PTISSTGPNG AIIHYAPVPE TNRTLSLDEV YLIDSGAQYK
360 370 380 390 400
DGTTDVTRTM HFGTPTAYEK ECFTYVLKGH IAVSAAVFPT GTKGHLLDSF
410 420 430 440 450
ARSALWDSGL DYLHGTGHGV GSFLNVHEGP CGISYKTFSD EPLEAGMIVT
460 470 480 490 500
DEPGYYEDGA FGIRIENVVL VVPVKTKYNF NNRGSLTFEP LTLVPIQTKM
510 520 530 540 550
IDVDSLTDKE CDWLNNYHLT CRDVIGKELQ KQGRQEALEW LIRETQPISK

QH
Length:552
Mass (Da):62,139
Last modified:December 21, 2004 - v1
Checksum:i627539255505E5CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354951 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000369683; ENSP00000358697; ENSG00000108039.
KEGGihsa:7511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354951 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliQ5T6H7.
SMRiQ5T6H7. Positions 1-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1382650.
STRINGi9606.ENSP00000421566.

Chemistry

BindingDBiQ5T6H7.

Proteomic databases

PRIDEiQ5T6H7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369683; ENSP00000358697; ENSG00000108039.
KEGGihsa:7511.

Organism-specific databases

CTDi7511.
HGNCiHGNC:12822. XPNPEP1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000013970.
HOVERGENiHBG002934.
KOiK01262.
OrthoDBiEOG7BGHK4.

Miscellaneous databases

ChiTaRSiXPNPEP1. human.
GenomeRNAii7511.

Gene expression databases

BgeeiQ5T6H7.
ExpressionAtlasiQ5T6H7. baseline and differential.

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]
ProtoNetiSearch...

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.
  5. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 24, 2015
This is version 91 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, Proteomics identificationCombined sources, Reference proteomeImported

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.