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Q9NQW7

- XPP1_HUMAN

UniProt

Q9NQW7 - XPP1_HUMAN

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Protein

Xaa-Pro aminopeptidase 1

Gene

XPNPEP1

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

Functioni

Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.

Catalytic activityi

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.2 Publications

Cofactori

Mn2+2 PublicationsNote: Binds 2 manganese ions per subunit.2 Publications

Enzyme regulationi

Inhibited by apstatin and the metal ion chelators EDTA and 1,10-phenanthroline. Partially inhibited by dithiothreitol. Not inhibited by enalaprilat or amastatin.1 Publication

Kineticsi

  1. KM=100.6 µM for bradykinin2 Publications
  2. KM=308 µM for the tripeptide Arg-Pro-Pro2 Publications

pH dependencei

Optimum pH is 8.2.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi415 – 4151Manganese 1
Metal bindingi426 – 4261Manganese 1
Metal bindingi426 – 4261Manganese 2
Metal bindingi489 – 4891Manganese 2
Metal bindingi523 – 5231Manganese 2
Metal bindingi537 – 5371Manganese 1
Metal bindingi537 – 5371Manganese 2

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. manganese ion binding Source: UniProtKB
  3. metalloaminopeptidase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. bradykinin catabolic process Source: UniProtKB
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.11.9. 2681.

Protein family/group databases

MEROPSiM24.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro aminopeptidase 1 (EC:3.4.11.9)
Alternative name(s):
Aminoacylproline aminopeptidase
Cytosolic aminopeptidase P
Soluble aminopeptidase P
Short name:
sAmp
X-Pro aminopeptidase 1
X-prolyl aminopeptidase 1, soluble
Gene namesi
Name:XPNPEP1Imported
Synonyms:XPNPEPLImported, XPNPEPL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:12822. XPNPEP1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411E → A: Reduces activity by 10%. 1 Publication
Mutagenesisi477 – 4771W → E: Interferes with dimerization and reduces activity by 94%. 1 Publication

Organism-specific databases

PharmGKBiPA37415.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 623622Xaa-Pro aminopeptidase 1PRO_0000185083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NQW7.
PaxDbiQ9NQW7.
PRIDEiQ9NQW7.

PTM databases

PhosphoSiteiQ9NQW7.

Expressioni

Tissue specificityi

Expressed in all tissues tested, including pancreas, heart, muscle, kidney, liver, lung and brain. Highest levels in pancreas.1 Publication

Gene expression databases

BgeeiQ9NQW7.
CleanExiHS_XPNPEP1.
ExpressionAtlasiQ9NQW7. baseline and differential.
GenevestigatoriQ9NQW7.

Organism-specific databases

HPAiCAB025196.
HPA030419.
HPA030420.
HPA030422.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi113346. 41 interactions.
IntActiQ9NQW7. 7 interactions.
MINTiMINT-3039782.
STRINGi9606.ENSP00000358694.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1610Combined sources
Turni20 – 223Combined sources
Beta strandi28 – 325Combined sources
Helixi45 – 473Combined sources
Helixi49 – 546Combined sources
Beta strandi62 – 687Combined sources
Beta strandi70 – 745Combined sources
Helixi76 – 783Combined sources
Helixi79 – 857Combined sources
Beta strandi90 – 945Combined sources
Helixi103 – 1108Combined sources
Beta strandi116 – 1194Combined sources
Helixi121 – 1233Combined sources
Helixi126 – 13813Combined sources
Beta strandi142 – 1454Combined sources
Helixi150 – 1545Combined sources
Helixi171 – 1744Combined sources
Helixi178 – 19013Combined sources
Turni191 – 1933Combined sources
Beta strandi194 – 1996Combined sources
Helixi202 – 2098Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi233 – 2364Combined sources
Helixi240 – 2434Combined sources
Helixi245 – 2506Combined sources
Turni251 – 2544Combined sources
Helixi259 – 2613Combined sources
Beta strandi263 – 2664Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28010Combined sources
Beta strandi287 – 2915Combined sources
Helixi296 – 3016Combined sources
Helixi304 – 3063Combined sources
Beta strandi307 – 3126Combined sources
Helixi314 – 3207Combined sources
Helixi324 – 35128Combined sources
Helixi352 – 3543Combined sources
Helixi359 – 37113Combined sources
Beta strandi376 – 3816Combined sources
Beta strandi384 – 3874Combined sources
Helixi388 – 3925Combined sources
Helixi400 – 4023Combined sources
Beta strandi412 – 4165Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi427 – 4315Combined sources
Helixi438 – 45518Combined sources
Helixi465 – 4728Combined sources
Helixi474 – 4785Combined sources
Beta strandi487 – 4904Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi519 – 5224Combined sources
Beta strandi525 – 5284Combined sources
Turni529 – 5313Combined sources
Beta strandi532 – 5354Combined sources
Beta strandi537 – 5459Combined sources
Beta strandi552 – 5543Combined sources
Beta strandi556 – 5616Combined sources
Helixi569 – 5713Combined sources
Helixi574 – 5763Combined sources
Helixi579 – 60224Combined sources
Helixi606 – 6149Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CTZX-ray1.60A1-623[»]
ProteinModelPortaliQ9NQW7.
SMRiQ9NQW7. Positions 3-619.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQW7.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24B family.Sequence Analysis

Phylogenomic databases

eggNOGiCOG0006.
GeneTreeiENSGT00390000013970.
HOGENOMiHOG000255713.
HOVERGENiHBG002934.
InParanoidiQ9NQW7.
KOiK01262.
OMAiKWLEREC.
PhylomeDBiQ9NQW7.
TreeFamiTF314183.

Family and domain databases

Gene3Di3.40.350.10. 2 hits.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
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]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9NQW7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPKVTSELL RQLRQAMRNS EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR
60 70 80 90 100
AFVSGFDGSA GTAIITEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT
110 120 130 140 150
PTQEDWLVSV LPEGSRVGVD PLIIPTDYWK KMAKVLRSAG HHLIPVKENL
160 170 180 190 200
VDKIWTDRPE RPCKPLLTLG LDYTGISWKD KVADLRLKMA ERNVMWFVVT
210 220 230 240 250
ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ETIMLFIDGD RIDAPSVKEH
260 270 280 290 300
LLLDLGLEAE YRIQVHPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE
310 320 330 340 350
TIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK
360 370 380 390 400
EVPKGGVTEI SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP
410 420 430 440 450
ETNRTLSLDE VYLIDSGAQY KDGTTDVTRT MHFGTPTAYE KECFTYVLKG
460 470 480 490 500
HIAVSAAVFP TGTKGHLLDS FARSALWDSG LDYLHGTGHG VGSFLNVHEG
510 520 530 540 550
PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV LVVPVKTKYN
560 570 580 590 600
FNNRGSLTFE PLTLVPIQTK MIDVDSLTDK ECDWLNNYHL TCRDVIGKEL
610 620
QKQGRQEALE WLIRETQPIS KQH
Length:623
Mass (Da):69,918
Last modified:January 23, 2007 - v3
Checksum:iDF4F5AF41E2F3876
GO
Isoform 2 (identifier: Q9NQW7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     398-421: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:599
Mass (Da):67,227
Checksum:i6F6A7D909E1CC84D
GO
Isoform 3 (identifier: Q9NQW7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAASRKPPRVRVNHQDFQLRNLRIIEPNEVTHSGDTGVETDGRM

Note: No experimental confirmation available.

Show »
Length:666
Mass (Da):74,798
Checksum:i59D0596A49C93B17
GO
Isoform 4 (identifier: Q9NQW7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAASRKPPRVRVNHQDFQLRNLRIIEPNEVTHSGDTGVETDGRM
     398-421: Missing.

Show »
Length:642
Mass (Da):72,107
Checksum:i0119CDC61051D1C2
GO

Sequence cautioni

The sequence CAD38640.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901W → C in AAH13417. (PubMed:15489334)Curated
Sequence conflicti131 – 1311K → R in BAF82125. (PubMed:14702039)Curated
Sequence conflicti332 – 3321R → P in CAA65068. (PubMed:9465902)Curated
Sequence conflicti332 – 3321R → P in AAF97866. (PubMed:10871044)Curated
Sequence conflicti496 – 4961N → D in BAD97233. (PubMed:17974005)Curated
Sequence conflicti498 – 4981H → R in BAD97233. (PubMed:17974005)Curated
Sequence conflicti572 – 5721I → T in BAF82125. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAASRKPPRVRVNHQDFQLR NLRIIEPNEVTHSGDTGVET DGRM in isoform 3 and isoform 4. 1 PublicationVSP_045250
Alternative sequencei398 – 42124Missing in isoform 2 and isoform 4. 1 PublicationVSP_051752Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95762 mRNA. Translation: CAA65068.1.
AF195530 mRNA. Translation: AAF97866.1.
AF272981 mRNA. Translation: AAF75795.1.
AK289436 mRNA. Translation: BAF82125.1.
CR456922 mRNA. Translation: CAG33203.1.
AK223513 mRNA. Translation: BAD97233.1.
AL833411 mRNA. Translation: CAD38640.1. Different initiation.
AL354951 Genomic DNA. Translation: CAI14248.1.
CH471066 Genomic DNA. Translation: EAW49577.1.
BC005126 mRNA. Translation: AAH05126.1.
BC007579 mRNA. Translation: AAH07579.1.
BC013417 mRNA. Translation: AAH13417.4.
CCDSiCCDS7560.2. [Q9NQW7-3]
RefSeqiNP_001161076.1. NM_001167604.1. [Q9NQW7-4]
NP_065116.3. NM_020383.3. [Q9NQW7-3]
UniGeneiHs.390623.

Genome annotation databases

EnsembliENST00000322238; ENSP00000324011; ENSG00000108039. [Q9NQW7-4]
ENST00000502935; ENSP00000421566; ENSG00000108039. [Q9NQW7-3]
GeneIDi7511.
KEGGihsa:7511.
UCSCiuc001kyp.2. human.
uc001kyq.2. human. [Q9NQW7-1]

Polymorphism databases

DMDMi68566146.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95762 mRNA. Translation: CAA65068.1 .
AF195530 mRNA. Translation: AAF97866.1 .
AF272981 mRNA. Translation: AAF75795.1 .
AK289436 mRNA. Translation: BAF82125.1 .
CR456922 mRNA. Translation: CAG33203.1 .
AK223513 mRNA. Translation: BAD97233.1 .
AL833411 mRNA. Translation: CAD38640.1 . Different initiation.
AL354951 Genomic DNA. Translation: CAI14248.1 .
CH471066 Genomic DNA. Translation: EAW49577.1 .
BC005126 mRNA. Translation: AAH05126.1 .
BC007579 mRNA. Translation: AAH07579.1 .
BC013417 mRNA. Translation: AAH13417.4 .
CCDSi CCDS7560.2. [Q9NQW7-3 ]
RefSeqi NP_001161076.1. NM_001167604.1. [Q9NQW7-4 ]
NP_065116.3. NM_020383.3. [Q9NQW7-3 ]
UniGenei Hs.390623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CTZ X-ray 1.60 A 1-623 [» ]
ProteinModelPortali Q9NQW7.
SMRi Q9NQW7. Positions 3-619.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113346. 41 interactions.
IntActi Q9NQW7. 7 interactions.
MINTi MINT-3039782.
STRINGi 9606.ENSP00000358694.

Chemistry

BindingDBi Q9NQW7.
ChEMBLi CHEMBL3782.

Protein family/group databases

MEROPSi M24.009.

PTM databases

PhosphoSitei Q9NQW7.

Polymorphism databases

DMDMi 68566146.

Proteomic databases

MaxQBi Q9NQW7.
PaxDbi Q9NQW7.
PRIDEi Q9NQW7.

Protocols and materials databases

DNASUi 7511.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322238 ; ENSP00000324011 ; ENSG00000108039 . [Q9NQW7-4 ]
ENST00000502935 ; ENSP00000421566 ; ENSG00000108039 . [Q9NQW7-3 ]
GeneIDi 7511.
KEGGi hsa:7511.
UCSCi uc001kyp.2. human.
uc001kyq.2. human. [Q9NQW7-1 ]

Organism-specific databases

CTDi 7511.
GeneCardsi GC10M111614.
HGNCi HGNC:12822. XPNPEP1.
HPAi CAB025196.
HPA030419.
HPA030420.
HPA030422.
MIMi 602443. gene.
neXtProti NX_Q9NQW7.
PharmGKBi PA37415.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0006.
GeneTreei ENSGT00390000013970.
HOGENOMi HOG000255713.
HOVERGENi HBG002934.
InParanoidi Q9NQW7.
KOi K01262.
OMAi KWLEREC.
PhylomeDBi Q9NQW7.
TreeFami TF314183.

Enzyme and pathway databases

BRENDAi 3.4.11.9. 2681.

Miscellaneous databases

ChiTaRSi XPNPEP1. human.
EvolutionaryTracei Q9NQW7.
GeneWikii XPNPEP1.
GenomeRNAii 7511.
NextBioi 29395.
PROi Q9NQW7.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQW7.
CleanExi HS_XPNPEP1.
ExpressionAtlasi Q9NQW7. baseline and differential.
Genevestigatori Q9NQW7.

Family and domain databases

Gene3Di 3.40.350.10. 2 hits.
3.90.230.10. 1 hit.
InterProi IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
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 SSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)."
    Vanhoof G., Goossens F., Juliano M.A., Juliano L., Hendriks D., Schatteman K., Lin A.H., Scharpe S.
    Cytogenet. Cell Genet. 78:275-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Lymphocyte.
  2. "Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with XPNPEP2."
    Sprinkle T.J., Caldwell C., Ryan J.W.
    Arch. Biochem. Biophys. 378:51-56(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme."
    Cottrell G.S., Hooper N.M., Turner A.J.
    Biochemistry 39:15121-15128(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Tissue: Pancreatic adenocarcinoma1 Publication.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adipose tissue.
  8. "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.M., 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].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 1).
    Tissue: ColonImported, OvaryImported and PlacentaImported.
  11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Platelet1 Publication.
  12. "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-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit."
    Li X., Lou Z., Li X., Zhou W., Ma M., Cao Y., Geng Y., Bartlam M., Zhang X.C., Rao Z.
    J. Biol. Chem. 283:22858-22866(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-41 AND TRP-477, SUBUNIT.

Entry informationi

Entry nameiXPP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NQW7
Secondary accession number(s): A8K071
, G5E9Y2, G8JLB2, O15250, Q53EX6, Q8N3Q0, Q96D23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 124 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3