Q9NQW7 (XPP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	XPNPEP1
Synonyms:	XPNPEPL, XPNPEPL1

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	623 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	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 activity	Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Ref.3 Ref.14
Cofactor	Binds 2 manganese ions per subunit. Ref.3 Ref.14
Enzyme regulation	Inhibited by apstatin and the metal ion chelators EDTA and 1,10-phenanthroline. Partially inhibited by dithiothreitol. Not inhibited by enalaprilat or amastatin. Ref.3
Subunit structure	Homodimer. Ref.3 Ref.14
Subcellular location	Cytoplasm By similarity UniProtKB O54975.
Tissue specificity	Expressed in all tissues tested, including pancreas, heart, muscle, kidney, liver, lung and brain. Highest levels in pancreas. Ref.1
Sequence similarities	Belongs to the peptidase M24B family.
Biophysicochemical properties	Kinetic parameters: KM=100.6 µM for bradykinin Ref.3 Ref.14 KM=308 µM for the tripeptide Arg-Pro-Pro pH dependence: Optimum pH is 8.2. Ref.3
Sequence caution	The sequence CAD38640.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bradykinin catabolic process Inferred from direct assay Ref.14. Source: UniProtKB proteolysis Inferred from direct assay Ref.3. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	manganese ion binding Inferred from direct assay Ref.14. Source: UniProtKB metalloaminopeptidase activity Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q9NQW7-1)

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.

Isoform 2 Ref.4 (identifier: Q9NQW7-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NQW7-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 623

622

Xaa-Pro aminopeptidase 1

PRO_0000185083

Sites

Metal binding

415

1

Manganese 1

Metal binding

426

1

Manganese 1

Metal binding

426

1

Manganese 2

Metal binding

489

1

Manganese 2

Metal binding

523

1

Manganese 2

Metal binding

537

1

Manganese 1

Metal binding

537

1

Manganese 2

Amino acid modifications

Modified residue

304

1

N6-acetyllysine Ref.12

Natural variations

Alternative sequence

1

1

M → MAASRKPPRVRVNHQDFQLR NLRIIEPNEVTHSGDTGVET DGRM in isoform 3.

VSP_045250

Alternative sequence

398 – 421

24

Missing in isoform 2. Ref.4

VSP_051752

Experimental info

Mutagenesis

41

1

E → A: Reduces activity by 10%. Ref.14

Mutagenesis

477

1

W → E: Interferes with dimerization and reduces activity by 94%. Ref.14

Sequence conflict

90

1

W → C in AAH13417. Ref.10

Sequence conflict

131

1

K → R in BAF82125. Ref.4

Sequence conflict

332

1

R → P Ref.1

Sequence conflict

332

1

R → P Ref.2

Sequence conflict

496

1

N → D Ref.7

Sequence conflict

498

1

H → R Ref.7

Sequence conflict

572

1

I → T in BAF82125. Ref.4

Secondary structure

1

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623

Helix Strand Turn

Details...

Helix

7 – 16

10

Turn

20 – 22

3

Beta strand

28 – 32

5

Helix

45 – 47

3

Helix

49 – 54

6

Beta strand

62 – 68

7

Beta strand

70 – 74

5

Helix

76 – 78

3

Helix

79 – 85

7

Beta strand

90 – 94

5

Helix

103 – 110

8

Beta strand

116 – 119

4

Helix

121 – 123

3

Helix

126 – 138

13

Beta strand

142 – 145

4

Helix

150 – 154

5

Helix

171 – 174

4

Helix

178 – 190

13

Turn

191 – 193

3

Beta strand

194 – 199

6

Helix

202 – 209

8

Beta strand

215 – 219

5

Beta strand

225 – 231

7

Beta strand

233 – 236

4

Helix

240 – 243

4

Helix

245 – 250

6

Turn

251 – 254

4

Helix

259 – 261

3

Beta strand

263 – 266

4

Helix

268 – 270

3

Helix

271 – 280

10

Beta strand

287 – 291

5

Helix

296 – 301

6

Helix

304 – 306

3

Beta strand

307 – 312

6

Helix

314 – 320

7

Helix

324 – 351

28

Helix

352 – 354

3

Helix

359 – 371

13

Beta strand

376 – 381

6

Beta strand

384 – 387

4

Helix

388 – 392

5

Helix

400 – 402

3

Beta strand

412 – 416

5

Beta strand

418 – 420

3

Beta strand

427 – 431

5

Helix

438 – 455

18

Helix

465 – 472

8

Helix

474 – 478

5

Beta strand

487 – 490

4

Beta strand

493 – 495

3

Beta strand

519 – 522

4

Beta strand

525 – 528

4

Turn

529 – 531

3

Beta strand

532 – 535

4

Beta strand

537 – 545

9

Beta strand

552 – 554

3

Beta strand

556 – 561

6

Helix

569 – 571

3

Helix

574 – 576

3

Helix

579 – 602

24

Helix

606 – 614

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DF4F5AF41E2F3876	FASTA	623	69,918
	10 20 30 40 50 60 MPPKVTSELL RQLRQAMRNS EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA 70 80 90 100 110 120 GTAIITEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD 130 140 150 160 170 180 PLIIPTDYWK KMAKVLRSAG HHLIPVKENL VDKIWTDRPE RPCKPLLTLG LDYTGISWKD 190 200 210 220 230 240 KVADLRLKMA ERNVMWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ETIMLFIDGD 250 260 270 280 290 300 RIDAPSVKEH LLLDLGLEAE YRIQVHPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE 310 320 330 340 350 360 TIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK EVPKGGVTEI 370 380 390 400 410 420 SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP ETNRTLSLDE VYLIDSGAQY 430 440 450 460 470 480 KDGTTDVTRT MHFGTPTAYE KECFTYVLKG HIAVSAAVFP TGTKGHLLDS FARSALWDSG 490 500 510 520 530 540 LDYLHGTGHG VGSFLNVHEG PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV 550 560 570 580 590 600 LVVPVKTKYN FNNRGSLTFE PLTLVPIQTK MIDVDSLTDK ECDWLNNYHL TCRDVIGKEL 610 620 QKQGRQEALE WLIRETQPIS KQH
	Isoform 2 [UniParc]. Checksum: 6F6A7D909E1CC84D	FASTA	599	67,227
	10 20 30 40 50 60 MPPKVTSELL RQLRQAMRNS EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA 70 80 90 100 110 120 GTAIITEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD 130 140 150 160 170 180 PLIIPTDYWK KMAKVLRSAG HHLIPVKENL VDKIWTDRPE RPCKPLLTLG LDYTGISWKD 190 200 210 220 230 240 KVADLRLKMA ERNVMWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ETIMLFIDGD 250 260 270 280 290 300 RIDAPSVKEH LLLDLGLEAE YRIQVHPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE 310 320 330 340 350 360 TIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK EVPKGGVTEI 370 380 390 400 410 420 SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYADGT TDVTRTMHFG TPTAYEKECF 430 440 450 460 470 480 TYVLKGHIAV SAAVFPTGTK GHLLDSFARS ALWDSGLDYL HGTGHGVGSF LNVHEGPCGI 490 500 510 520 530 540 SYKTFSDEPL EAGMIVTDEP GYYEDGAFGI RIENVVLVVP VKTKYNFNNR GSLTFEPLTL 550 560 570 580 590 VPIQTKMIDV DSLTDKECDW LNNYHLTCRD VIGKELQKQG RQEALEWLIR ETQPISKQH
	Isoform 3 [UniParc]. Checksum: 59D0596A49C93B17	FASTA	666	74,798
	10 20 30 40 50 60 MAASRKPPRV RVNHQDFQLR NLRIIEPNEV THSGDTGVET DGRMPPKVTS ELLRQLRQAM 70 80 90 100 110 120 RNSEYVTEPI QAYIIPSGDA HQSEYIAPCD CRRAFVSGFD GSAGTAIITE EHAAMWTDGR 130 140 150 160 170 180 YFLQAAKQMD SNWTLMKMGL KDTPTQEDWL VSVLPEGSRV GVDPLIIPTD YWKKMAKVLR 190 200 210 220 230 240 SAGHHLIPVK ENLVDKIWTD RPERPCKPLL TLGLDYTGIS WKDKVADLRL KMAERNVMWF 250 260 270 280 290 300 VVTALDEIAW LFNLRGSDVE HNPVFFSYAI IGLETIMLFI DGDRIDAPSV KEHLLLDLGL 310 320 330 340 350 360 EAEYRIQVHP YKSILSELKA LCADLSPREK VWVSDKASYA VSETIPKDHR CCMPYTPICI 370 380 390 400 410 420 AKAVKNSAES EGMRRAHIKD AVALCELFNW LEKEVPKGGV TEISAADKAE EFRRQQADFV 430 440 450 460 470 480 DLSFPTISST GPNGAIIHYA PVPETNRTLS LDEVYLIDSG AQYKDGTTDV TRTMHFGTPT 490 500 510 520 530 540 AYEKECFTYV LKGHIAVSAA VFPTGTKGHL LDSFARSALW DSGLDYLHGT GHGVGSFLNV 550 560 570 580 590 600 HEGPCGISYK TFSDEPLEAG MIVTDEPGYY EDGAFGIRIE NVVLVVPVKT KYNFNNRGSL 610 620 630 640 650 660 TFEPLTLVPI QTKMIDVDSL TDKECDWLNN YHLTCRDVIG KELQKQGRQE ALEWLIRETQ PISKQH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 adenocarcinoma.
[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]	"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] (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]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: Colon, Ovary and Placenta.
[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: Platelet.
[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, MASS SPECTROMETRY.
[13]	"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].
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00607814.
IPI00793375.
IPI01011873.

RefSeq

NP_001161076.1. NM_001167604.1.
NP_065116.3. NM_020383.3.

UniGene

Hs.390623.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CTZ	X-ray	1.60	A	1-623	[»]

ProteinModelPortal

Q9NQW7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NQW7. 4 interactions.

STRING

9606.ENSP00000358694.

Protein family/group databases

MEROPS

M24.009.

PTM databases

PhosphoSite

Q9NQW7.

Polymorphism databases

DMDM

68566146.

Proteomic databases

PaxDb

Q9NQW7.

PRIDE

Q9NQW7.

Protocols and materials databases

DNASU

7511.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369680; ENSP00000358694; ENSG00000108039.
ENST00000502935; ENSP00000421566; ENSG00000108039.

GeneID

7511.

KEGG

hsa:7511.

UCSC

uc001kyp.2. human.
uc009xxt.2. human.

Organism-specific databases

CTD

7511.

GeneCards

GC10M111614.

HGNC

HGNC:12822. XPNPEP1.

HPA

CAB025196.
HPA030419.
HPA030420.
HPA030422.

MIM

602443. gene.

neXtProt

NX_Q9NQW7.

PharmGKB

PA37415.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0006.

HOGENOM

HOG000255713.

HOVERGEN

HBG002934.

InParanoid

Q9NQW7.

KO

K01262.

OMA

SRYWEQA.

OrthoDB

EOG4BZN23.

Enzyme and pathway databases

BRENDA

3.4.11.9. 2681.

Gene expression databases

ArrayExpress

Q9NQW7.

Bgee

Q9NQW7.

CleanEx

HS_XPNPEP1.

Genevestigator

Q9NQW7.

GermOnline

ENSG00000108039. Homo sapiens.

Family and domain databases

Gene3D

3.90.230.10. 1 hit.

InterPro

IPR000587. Creatinase.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]

Pfam

PF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

PROSITE

PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9NQW7.

ChEMBL

CHEMBL3782.

ChiTaRS

XPNPEP1. human.

EvolutionaryTrace

Q9NQW7.

GenomeRNAi

7511.

NextBio

29395.

SOURCE

Search...

Entry information

Entry name

XPP1_HUMAN

Accession

Primary (citable) accession number: Q9NQW7
Secondary accession number(s): A8K071 , G5E9Y2, O15250, Q53EX6, Q8N3Q0, Q96D23

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 106 of the entry and version 3 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.