Q9NQH7 (XPP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Xaa-Pro aminopeptidase 3
Short name=X-Pro aminopeptidase 3
EC=3.4.11.9

Alternative name(s):
Aminopeptidase P3
Short name=APP3

Gene names

Name:

XPNPEP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Subcellular location	Mitochondrion Ref.10.
Tissue specificity	Isoform 1 and isoform 2 are widely expressed, with isoform 1 being more abundant. Ref.8
Involvement in disease	Defects in XPNPEP3 are the cause of nephronophthisis-like nephropathy type 1 (NPHPL1) [MIM:613159]. A disorder with features of nephronophthisis, a cystic kidney disease leading to end-stage renal failure. Nephronophthisis is histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. Typical clinical manifestation are chronic renal failure, anemia, polyuria, polydipsia, isosthenuria, and growth retardation. Associations with extrarenal symptoms are frequent. In NPHPL1 patients, extrarenal symptoms include hypertension, essential tremor, sensorineural hearing loss and gout. Severely affected individuals can manifest a mitochondrial disorder with isolated complex I deficiency activity in muscle, seizures, mental retardation and hypertrophic dilated cardiomyopathy. Ref.10
Sequence similarities	Belongs to the peptidase M24B family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ciliopathy Disease mutation Nephronophthisis
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NQH7-1)

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 (identifier: Q9NQH7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Isoform 3 (identifier: Q9NQH7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     265-278: AFIETMFTSKAPVE → RQGFSVLSRLVSNS
     279-507: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9NQH7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q9NQH7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     265-288: AFIETMFTSKAPVEEAFLYAKFEF → KSVLLARHGGSRLYSHHFGRPRLS
     289-507: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 507	507	Probable Xaa-Pro aminopeptidase 3		PRO_0000255654
Sites
	Metal binding	331	1	Manganese 2 By similarity
	Metal binding	342	1	Manganese 1 By similarity
	Metal binding	342	1	Manganese 2 By similarity
	Metal binding	424	1	Manganese 1 By similarity
	Metal binding	451	1	Manganese 1 By similarity
	Metal binding	475	1	Manganese 1 By similarity
	Metal binding	475	1	Manganese 2 By similarity
Natural variations
	Alternative sequence	1 – 79	79	Missing in isoform 2.		VSP_021296
	Alternative sequence	1 – 23	23	Missing in isoform 4.		VSP_040142
	Alternative sequence	265 – 288	24	AFIET…AKFEF → KSVLLARHGGSRLYSHHFGR PRLS in isoform 5.		VSP_040143
	Alternative sequence	265 – 278	14	AFIET…KAPVE → RQGFSVLSRLVSNS in isoform 3.		VSP_021297
	Alternative sequence	279 – 507	229	Missing in isoform 3.		VSP_021298
	Alternative sequence	289 – 507	219	Missing in isoform 5.		VSP_040144
	Natural variant	450	1	I → L. Corresponds to variant rs17002243 [ dbSNP | Ensembl ].		VAR_051573
	Natural variant	453	1	G → C in NPHPL1. Ref.10		VAR_063820
Experimental info
	Sequence conflict	340	1	V → A in CAG33677. Ref.1
	Sequence conflict	486	1	L → F in AAH01681. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 82D886736ABD0B5B	FASTA	507	57,034
	10 20 30 40 50 60 MPWLLSAPKL VPAVANVRGL SGCMLCSQRR YSLQPVPERR IPNRYLGQPS PFTHPHLLRP 70 80 90 100 110 120 GEVTPGLSQV EYALRRHKLM SLIQKEAQGQ SGTDQTVVVL SNPTYYMSND IPYTFHQDNN 130 140 150 160 170 180 FLYLCGFQEP DSILVLQSLP GKQLPSHKAI LFVPRRDPSR ELWDGPRSGT DGAIALTGVD 190 200 210 220 230 240 EAYTLEEFQH LLPKMKAETN MVWYDWMRPS HAQLHSDYMQ PLTEAKAKSK NKVRGVQQLI 250 260 270 280 290 300 QRLRLIKSPA EIERMQIAGK LTSQAFIETM FTSKAPVEEA FLYAKFEFEC RARGADILAY 310 320 330 340 350 360 PPVVAGGNRS NTLHYVKNNQ LIKDGEMVLL DGGCESSCYV SDITRTWPVN GRFTAPQAEL 370 380 390 400 410 420 YEAVLEIQRD CLALCFPGTS LENIYSMMLT LIGQKLKDLG IMKNIKENNA FKAARKYCPH 430 440 450 460 470 480 HVGHYLGMDV HDTPDMPRSL PLQPGMVITI EPGIYIPEDD KDAPEKFRGL GVRIEDDVVV 490 500 TQDSPLILSA DCPKEMNDIE QICSQAS
	Isoform 2 [UniParc]. Checksum: E95AFE73A5D94D49	FASTA	428	48,112
	10 20 30 40 50 60 MSLIQKEAQG QSGTDQTVVV LSNPTYYMSN DIPYTFHQDN NFLYLCGFQE PDSILVLQSL 70 80 90 100 110 120 PGKQLPSHKA ILFVPRRDPS RELWDGPRSG TDGAIALTGV DEAYTLEEFQ HLLPKMKAET 130 140 150 160 170 180 NMVWYDWMRP SHAQLHSDYM QPLTEAKAKS KNKVRGVQQL IQRLRLIKSP AEIERMQIAG 190 200 210 220 230 240 KLTSQAFIET MFTSKAPVEE AFLYAKFEFE CRARGADILA YPPVVAGGNR SNTLHYVKNN 250 260 270 280 290 300 QLIKDGEMVL LDGGCESSCY VSDITRTWPV NGRFTAPQAE LYEAVLEIQR DCLALCFPGT 310 320 330 340 350 360 SLENIYSMML TLIGQKLKDL GIMKNIKENN AFKAARKYCP HHVGHYLGMD VHDTPDMPRS 370 380 390 400 410 420 LPLQPGMVIT IEPGIYIPED DKDAPEKFRG LGVRIEDDVV VTQDSPLILS ADCPKEMNDI EQICSQAS
	Isoform 3 [UniParc]. Checksum: B4AD5CEB13853823	FASTA	278	31,529
	10 20 30 40 50 60 MPWLLSAPKL VPAVANVRGL SGCMLCSQRR YSLQPVPERR IPNRYLGQPS PFTHPHLLRP 70 80 90 100 110 120 GEVTPGLSQV EYALRRHKLM SLIQKEAQGQ SGTDQTVVVL SNPTYYMSND IPYTFHQDNN 130 140 150 160 170 180 FLYLCGFQEP DSILVLQSLP GKQLPSHKAI LFVPRRDPSR ELWDGPRSGT DGAIALTGVD 190 200 210 220 230 240 EAYTLEEFQH LLPKMKAETN MVWYDWMRPS HAQLHSDYMQ PLTEAKAKSK NKVRGVQQLI 250 260 270 QRLRLIKSPA EIERMQIAGK LTSQRQGFSV LSRLVSNS
	Isoform 4 [UniParc]. Checksum: 6320B2E5975918BB	FASTA	484	54,672
	10 20 30 40 50 60 MLCSQRRYSL QPVPERRIPN RYLGQPSPFT HPHLLRPGEV TPGLSQVEYA LRRHKLMSLI 70 80 90 100 110 120 QKEAQGQSGT DQTVVVLSNP TYYMSNDIPY TFHQDNNFLY LCGFQEPDSI LVLQSLPGKQ 130 140 150 160 170 180 LPSHKAILFV PRRDPSRELW DGPRSGTDGA IALTGVDEAY TLEEFQHLLP KMKAETNMVW 190 200 210 220 230 240 YDWMRPSHAQ LHSDYMQPLT EAKAKSKNKV RGVQQLIQRL RLIKSPAEIE RMQIAGKLTS 250 260 270 280 290 300 QAFIETMFTS KAPVEEAFLY AKFEFECRAR GADILAYPPV VAGGNRSNTL HYVKNNQLIK 310 320 330 340 350 360 DGEMVLLDGG CESSCYVSDI TRTWPVNGRF TAPQAELYEA VLEIQRDCLA LCFPGTSLEN 370 380 390 400 410 420 IYSMMLTLIG QKLKDLGIMK NIKENNAFKA ARKYCPHHVG HYLGMDVHDT PDMPRSLPLQ 430 440 450 460 470 480 PGMVITIEPG IYIPEDDKDA PEKFRGLGVR IEDDVVVTQD SPLILSADCP KEMNDIEQIC SQAS
	Isoform 5 [UniParc]. Checksum: E245C092422567ED	FASTA	288	32,712
	10 20 30 40 50 60 MPWLLSAPKL VPAVANVRGL SGCMLCSQRR YSLQPVPERR IPNRYLGQPS PFTHPHLLRP 70 80 90 100 110 120 GEVTPGLSQV EYALRRHKLM SLIQKEAQGQ SGTDQTVVVL SNPTYYMSND IPYTFHQDNN 130 140 150 160 170 180 FLYLCGFQEP DSILVLQSLP GKQLPSHKAI LFVPRRDPSR ELWDGPRSGT DGAIALTGVD 190 200 210 220 230 240 EAYTLEEFQH LLPKMKAETN MVWYDWMRPS HAQLHSDYMQ PLTEAKAKSK NKVRGVQQLI 250 260 270 280 QRLRLIKSPA EIERMQIAGK LTSQKSVLLA RHGGSRLYSH HFGRPRLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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).
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5). Tissue: Oesophageal carcinoma and Testis.
[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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Lung.
[8]	"Aminopeptidase P isozyme expression in human tissues and peripheral blood mononuclear cell fractions." Ersahin C., Szpaderska A.M., Orawski A.T., Simmons W.H. Arch. Biochem. Biophys. 435:303-310(2005) [PubMed: 15708373] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy." O'Toole J.F., Liu Y., Davis E.E., Westlake C.J., Attanasio M., Otto E.A., Seelow D., Nurnberg G., Becker C., Nuutinen M., Karppa M., Ignatius J., Uusimaa J., Pakanen S., Jaakkola E., van den Heuvel L.P., Fehrenbach H., Wiggins R. , Goyal M., Zhou W., Wolf M.T., Wise E., Helou J., Allen S.J., Murga-Zamalloa C.A., Ashraf S., Chaki M., Heeringa S., Chernin G., Hoskins B.E., Chaib H., Gleeson J., Kusakabe T., Suzuki T., Isaac R.E., Quarmby L.M., Tennant B., Fujioka H., Tuominen H., Hassinen I., Lohi H., van Houten J.L., Rotig A., Sayer J.A., Rolinski B., Freisinger P., Madhavan S.M., Herzer M., Madignier F., Prokisch H., Nurnberg P., Jackson P.K., Khanna H., Katsanis N., Hildebrandt F. J. Clin. Invest. 120:791-802(2010) [PubMed: 20179356] [Abstract] Cited for: VARIANT NPHPL1 CYS-453, SUBCELLULAR LOCATION.
[11]	Erratum O'Toole J.F., Liu Y., Davis E.E., Westlake C.J., Attanasio M., Otto E.A., Seelow D., Nurnberg G., Becker C., Nuutinen M., Karppa M., Ignatius J., Uusimaa J., Pakanen S., Jaakkola E., van den Heuvel L.P., Fehrenbach H., Wiggins R. , Goyal M., Zhou W., Wolf M.T., Wise E., Helou J., Allen S.J., Murga-Zamalloa C.A., Ashraf S., Chaki M., Heeringa S., Chernin G., Hoskins B.E., Chaib H., Gleeson J., Kusakabe T., Suzuki T., Isaac R.E., Quarmby L.M., Tennant B., Fujioka H., Tuominen H., Hassinen I., Lohi H., van Houten J.L., Rotig A., Sayer J.A., Rolinski B., Freisinger P., Madhavan S.M., Herzer M., Madignier F., Prokisch H., Nurnberg P., Jackson P.K., Khanna H., Katsanis N., Hildebrandt F. J. Clin. Invest. 120:1362-1362(2010)
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR457396 mRNA. Translation: CAG33677.1. AL365514 mRNA. Translation: CAB97210.1. CR456442 mRNA. Translation: CAG30328.1. AK301635 mRNA. Translation: BAH13526.1. AK301758 mRNA. Translation: BAH13548.1. AK313770 mRNA. Translation: BAG36508.1. AL834310 mRNA. Translation: CAD38980.1. Z98048, AL035450 Genomic DNA. Translation: CAI20492.1. AL035450, Z98048 Genomic DNA. Translation: CAI19023.1. CH471095 Genomic DNA. Translation: EAW60399.1. BC001208 mRNA. Translation: AAH01208.1. BC001681 mRNA. Translation: AAH01681.1. BC004989 mRNA. Translation: AAH04989.1.
IPI	IPI00550192. IPI00794503. IPI00795212. IPI00922067. IPI00922407.
RefSeq	NP_071381.1. NM_022098.3.
UniGene	Hs.529163.
3D structure databases
HSSP	HSSP built from PDB template 1PV9 based on UniProtKB P81535.
ProteinModelPortal	Q9NQH7.
SMR	Q9NQH7. Positions 58-505.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NQH7. 4 interactions.
MINT	MINT-1142970.
STRING	Q9NQH7.
Protein family/group databases
MEROPS	M24.026.
Polymorphism databases
DMDM	74761652.
Proteomic databases
PRIDE	Q9NQH7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357137; ENSP00000349658; ENSG00000196236.
GeneID	63929.
KEGG	hsa:63929.
NMPDR	fig|9606.3.peg.21772.
UCSC	uc003azh.1. human. uc003azi.1. human.
Organism-specific databases
CTD	63929.
GeneCards	GC22P041253.
HGNC	HGNC:28052. XPNPEP3.
HPA	HPA000527.
MIM	613159. phenotype. 613553. gene.
neXtProt	NX_Q9NQH7.
Orphanet	655. Autosomal recessive medullary cystic kidney disease.
PharmGKB	PA147357130.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07556.
GeneTree	ENSGT00550000074909.
HOGENOM	HBG545079.
HOVERGEN	HBG057305.
InParanoid	Q9NQH7.
OMA	SHKAILF.
PhylomeDB	Q9NQH7.
Gene expression databases
ArrayExpress	Q9NQH7.
Bgee	Q9NQH7.
CleanEx	HS_XPNPEP3.
Genevestigator	Q9NQH7.
Family and domain databases
InterPro	IPR007865. Aminopep_P_N. IPR000994. Pept_M24_structural-domain. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01262.
Pfam	PF05195. AMP_N. 1 hit. PF00557. Peptidase_M24. 1 hit. [Graphical view]
SMART	SM01011. AMP_N. 1 hit. [Graphical view]
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
ProtoNet	Search...
Other
NextBio	65674.
SOURCE	Search...

Entry information

Entry name

XPP3_HUMAN

Accession

Primary (citable) accession number: Q9NQH7
Secondary accession number(s): B2R9G1 , B7Z790, B7Z7B2, Q6I9V9, Q8NDA6, Q9BV27, Q9BVH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 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.