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P12955

- PEPD_HUMAN

UniProt

P12955 - PEPD_HUMAN

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Protein
Xaa-Pro dipeptidase
Gene
PEPD, PRD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.

Catalytic activityi

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.

Cofactori

Binds 2 manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi276 – 2761Manganese 1
Metal bindingi287 – 2871Manganese 1
Metal bindingi287 – 2871Manganese 2
Metal bindingi370 – 3701Manganese 2
Metal bindingi412 – 4121Manganese 2
Metal bindingi452 – 4521Manganese 1
Metal bindingi452 – 4521Manganese 2

GO - Molecular functioni

  1. aminopeptidase activity Source: InterPro
  2. dipeptidase activity Source: UniProtKB-KW
  3. manganese ion binding Source: InterPro
  4. metallocarboxypeptidase activity Source: ProtInc

GO - Biological processi

  1. cellular amino acid metabolic process Source: ProtInc
  2. collagen catabolic process Source: UniProtKB-KW
  3. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

MEROPSiM24.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro dipeptidase (EC:3.4.13.9)
Short name:
X-Pro dipeptidase
Alternative name(s):
Imidodipeptidase
Peptidase D
Proline dipeptidase
Short name:
Prolidase
Gene namesi
Name:PEPD
Synonyms:PRD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:8840. PEPD.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Prolidase deficiency (PD) [MIM:170100]: A multisystem disorder associated with massive iminodipeptiduria and lack of or reduced prolidase activity in erythrocytes, leukocytes, or cultured fibroblasts. Clinical features include skin ulcers, developmental delay, recurrent infections, and a characteristic facies.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti184 – 1841R → Q in PD. 1 Publication
VAR_011614
Natural varianti276 – 2761D → N in PD. 1 Publication
VAR_004404
Natural varianti278 – 2781G → D in PD. 1 Publication
VAR_011615
Natural varianti448 – 4481G → R in PD. 3 Publications
VAR_004405
Natural varianti452 – 4521Missing in PD. 2 Publications
VAR_004406

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi170100. phenotype.
Orphaneti742. Prolidase deficiency.
PharmGKBiPA33181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 493492Xaa-Pro dipeptidase
PRO_0000185087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP12955.
PaxDbiP12955.
PeptideAtlasiP12955.
PRIDEiP12955.

2D gel databases

REPRODUCTION-2DPAGEIPI00257882.

PTM databases

PhosphoSiteiP12955.

Expressioni

Gene expression databases

ArrayExpressiP12955.
BgeeiP12955.
CleanExiHS_PEPD.
GenevestigatoriP12955.

Organism-specific databases

HPAiHPA015599.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi111208. 31 interactions.
IntActiP12955. 8 interactions.
MINTiMINT-5000488.
STRINGi9606.ENSP00000244137.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3616
Beta strandi45 – 495
Beta strandi54 – 563
Helixi69 – 757
Beta strandi79 – 813
Beta strandi83 – 875
Turni88 – 903
Beta strandi93 – 975
Helixi102 – 1043
Turni105 – 1073
Helixi114 – 1218
Beta strandi124 – 1285
Helixi129 – 1313
Helixi132 – 1387
Turni152 – 1543
Helixi166 – 1683
Helixi176 – 18510
Helixi189 – 21224
Helixi219 – 23416
Beta strandi238 – 2414
Beta strandi244 – 2474
Helixi248 – 2525
Beta strandi272 – 2776
Beta strandi279 – 2813
Beta strandi288 – 2936
Helixi300 – 31920
Helixi326 – 34318
Helixi351 – 3566
Turni357 – 3593
Helixi360 – 3634
Beta strandi373 – 3775
Helixi394 – 3963
Beta strandi408 – 4114
Beta strandi414 – 4163
Helixi419 – 4279
Helixi429 – 4324
Helixi437 – 4437
Beta strandi448 – 4503
Beta strandi452 – 4576
Beta strandi459 – 4646
Helixi472 – 4798

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IW2X-ray1.82A/B2-493[»]
2OKNX-ray2.45A/B2-493[»]
ProteinModelPortaliP12955.
SMRiP12955. Positions 6-482.

Miscellaneous databases

EvolutionaryTraceiP12955.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0006.
HOGENOMiHOG000008763.
HOVERGENiHBG053562.
InParanoidiP12955.
KOiK14213.
OMAiPIVACGE.
OrthoDBiEOG7FNC76.
PhylomeDBiP12955.
TreeFamiTF313396.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR007865. Aminopep_P_N.
IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SMARTiSM01011. AMP_N. 1 hit.
[Graphical view]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P12955-1) [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

MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG    50
GEETQRYCTD TGVLFRQESF FHWAFGVTEP GCYGVIDVDT GKSTLFVPRL 100
PASHATWMGK IHSKEHFKEK YAVDDVQYVD EIASVLTSQK PSVLLTLRGV 150
NTDSGSVCRE ASFDGISKFE VNNTILHPEI VECRVFKTDM ELEVLRYTNK 200
ISSEAHREVM KAVKVGMKEY ELESLFEHYC YSRGGMRHSS YTCICGSGEN 250
SAVLHYGHAG APNDRTIQNG DMCLFDMGGE YYCFASDITC SFPANGKFTA 300
DQKAVYEAVL RSSRAVMGAM KPGVWWPDMH RLADRIHLEE LAHMGILSGS 350
VDAMVQAHLG AVFMPHGLGH FLGIDVHDVG GYPEGVERID EPGLRSLRTA 400
RHLQPGMVLT VEPGIYFIDH LLDEALADPA RASFLNREVL QRFRGFGGVR 450
IEEDVVVTDS GIELLTCVPR TVEEIEACMA GCDKAFTPFS GPK 493
Length:493
Mass (Da):54,548
Last modified:January 23, 2007 - v3
Checksum:iE8C4A2497E44BA22
GO
Isoform 2 (identifier: P12955-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-224: Missing.

Note: No experimental confirmation available.

Show »
Length:452
Mass (Da):49,691
Checksum:iEA1B0DFBE694A180
GO
Isoform 3 (identifier: P12955-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-131: Missing.

Note: No experimental confirmation available.

Show »
Length:429
Mass (Da):47,261
Checksum:i2D094B4069E39CF5
GO

Mass spectrometryi

Molecular mass is 54251.73 Da from positions 2 - 493. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti184 – 1841R → Q in PD. 1 Publication
VAR_011614
Natural varianti276 – 2761D → N in PD. 1 Publication
VAR_004404
Natural varianti278 – 2781G → D in PD. 1 Publication
VAR_011615
Natural varianti388 – 3881R → H.
Corresponds to variant rs2230062 [ dbSNP | Ensembl ].
VAR_051574
Natural varianti435 – 4351L → F.2 Publications
Corresponds to variant rs17570 [ dbSNP | Ensembl ].
VAR_014723
Natural varianti448 – 4481G → R in PD. 3 Publications
VAR_004405
Natural varianti452 – 4521Missing in PD. 2 Publications
VAR_004406

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 13164Missing in isoform 3.
VSP_045370Add
BLAST
Alternative sequencei184 – 22441Missing in isoform 2.
VSP_042629Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481L → R in BAF84250. 1 Publication
Sequence conflicti66 – 661R → L in AAA60064. 1 Publication
Sequence conflicti107 – 1071W → R in BAF83470. 1 Publication
Sequence conflicti108 – 1081M → I in BAF83445. 1 Publication
Sequence conflicti183 – 1831C → S in AAA60064. 1 Publication
Sequence conflicti221 – 2211E → G in AAA60064. 1 Publication
Sequence conflicti283 – 2842CF → SV in AAA60064. 1 Publication
Sequence conflicti294 – 2941A → R in AAA60064. 1 Publication
Sequence conflicti311 – 3111R → L in AAA60064. 1 Publication
Sequence conflicti324 – 3241V → D in AAA60064. 1 Publication
Sequence conflicti329 – 3302MH → ID in AAA60064. 1 Publication
Sequence conflicti408 – 4081V → A in BAG56678. 1 Publication
Sequence conflicti458 – 4581T → I in AAA60064. 1 Publication
Sequence conflicti478 – 4781C → R in BAF83470. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04605 mRNA. Translation: AAA60064.1.
BT006692 mRNA. Translation: AAP35338.1.
AK290756 mRNA. Translation: BAF83445.1.
AK290781 mRNA. Translation: BAF83470.1.
AK291561 mRNA. Translation: BAF84250.1.
AK293126 mRNA. Translation: BAG56678.1.
AK294619 mRNA. Translation: BAG57802.1.
AC008744 Genomic DNA. No translation available.
AC010485 Genomic DNA. No translation available.
BC004305 mRNA. Translation: AAH04305.1.
BC015027 mRNA. Translation: AAH15027.1.
BC028295 mRNA. Translation: AAH28295.1.
CCDSiCCDS42544.1. [P12955-1]
CCDS54244.1. [P12955-3]
CCDS54245.1. [P12955-2]
PIRiA32454.
RefSeqiNP_000276.2. NM_000285.3. [P12955-1]
NP_001159528.1. NM_001166056.1. [P12955-2]
NP_001159529.1. NM_001166057.1. [P12955-3]
UniGeneiHs.36473.

Genome annotation databases

EnsembliENST00000244137; ENSP00000244137; ENSG00000124299. [P12955-1]
ENST00000397032; ENSP00000380226; ENSG00000124299. [P12955-2]
ENST00000436370; ENSP00000391890; ENSG00000124299. [P12955-3]
GeneIDi5184.
KEGGihsa:5184.
UCSCiuc002nur.4. human. [P12955-1]
uc010xrr.2. human. [P12955-2]

Polymorphism databases

DMDMi50403718.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04605 mRNA. Translation: AAA60064.1 .
BT006692 mRNA. Translation: AAP35338.1 .
AK290756 mRNA. Translation: BAF83445.1 .
AK290781 mRNA. Translation: BAF83470.1 .
AK291561 mRNA. Translation: BAF84250.1 .
AK293126 mRNA. Translation: BAG56678.1 .
AK294619 mRNA. Translation: BAG57802.1 .
AC008744 Genomic DNA. No translation available.
AC010485 Genomic DNA. No translation available.
BC004305 mRNA. Translation: AAH04305.1 .
BC015027 mRNA. Translation: AAH15027.1 .
BC028295 mRNA. Translation: AAH28295.1 .
CCDSi CCDS42544.1. [P12955-1 ]
CCDS54244.1. [P12955-3 ]
CCDS54245.1. [P12955-2 ]
PIRi A32454.
RefSeqi NP_000276.2. NM_000285.3. [P12955-1 ]
NP_001159528.1. NM_001166056.1. [P12955-2 ]
NP_001159529.1. NM_001166057.1. [P12955-3 ]
UniGenei Hs.36473.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IW2 X-ray 1.82 A/B 2-493 [» ]
2OKN X-ray 2.45 A/B 2-493 [» ]
ProteinModelPortali P12955.
SMRi P12955. Positions 6-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111208. 31 interactions.
IntActi P12955. 8 interactions.
MINTi MINT-5000488.
STRINGi 9606.ENSP00000244137.

Chemistry

BindingDBi P12955.
ChEMBLi CHEMBL4185.

Protein family/group databases

MEROPSi M24.007.

PTM databases

PhosphoSitei P12955.

Polymorphism databases

DMDMi 50403718.

2D gel databases

REPRODUCTION-2DPAGE IPI00257882.

Proteomic databases

MaxQBi P12955.
PaxDbi P12955.
PeptideAtlasi P12955.
PRIDEi P12955.

Protocols and materials databases

DNASUi 5184.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244137 ; ENSP00000244137 ; ENSG00000124299 . [P12955-1 ]
ENST00000397032 ; ENSP00000380226 ; ENSG00000124299 . [P12955-2 ]
ENST00000436370 ; ENSP00000391890 ; ENSG00000124299 . [P12955-3 ]
GeneIDi 5184.
KEGGi hsa:5184.
UCSCi uc002nur.4. human. [P12955-1 ]
uc010xrr.2. human. [P12955-2 ]

Organism-specific databases

CTDi 5184.
GeneCardsi GC19M033877.
HGNCi HGNC:8840. PEPD.
HPAi HPA015599.
MIMi 170100. phenotype.
613230. gene.
neXtProti NX_P12955.
Orphaneti 742. Prolidase deficiency.
PharmGKBi PA33181.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0006.
HOGENOMi HOG000008763.
HOVERGENi HBG053562.
InParanoidi P12955.
KOi K14213.
OMAi PIVACGE.
OrthoDBi EOG7FNC76.
PhylomeDBi P12955.
TreeFami TF313396.

Miscellaneous databases

ChiTaRSi PEPD. human.
EvolutionaryTracei P12955.
GeneWikii PEPD.
GenomeRNAii 5184.
NextBioi 20054.
PROi P12955.
SOURCEi Search...

Gene expression databases

ArrayExpressi P12955.
Bgeei P12955.
CleanExi HS_PEPD.
Genevestigatori P12955.

Family and domain databases

Gene3Di 3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProi IPR007865. Aminopep_P_N.
IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view ]
Pfami PF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
SMARTi SM01011. AMP_N. 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. "Primary structure and gene localization of human prolidase."
    Endo F., Tanoue A., Nakai H., Hata A., Indo Y., Titani K., Matsuda I.
    J. Biol. Chem. 264:4476-4481(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver and Placenta.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT PHE-435.
    Tissue: Brain and Kidney.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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), VARIANT PHE-435.
    Tissue: Kidney, Skin and Uterus.
  6. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human prolidase: the molecular basis of PD disease."
    Protein structure factory (PSF)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.
  11. "A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells."
    Tanoue A., Endo F., Kitano A., Matsuda I.
    J. Clin. Invest. 86:351-355(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PD ASN-276.
  12. "Four novel PEPD alleles causing prolidase deficiency."
    Ledoux P., Scriver C.R., Hechtman P.
    Am. J. Hum. Genet. 54:1014-1021(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PD ARG-448 AND GLU-452 DEL.
  13. "Expression and molecular analysis of mutations in prolidase deficiency."
    Ledoux P., Scriver C.R., Hechtman P.
    Am. J. Hum. Genet. 59:1035-1039(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PD GLN-184; ASP-278; ARG-448 AND GLU-452 DEL.
  14. "Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts."
    Forlino A., Lupi A., Vaghi P., Icaro Cornaglia A., Calligaro A., Campari E., Cetta G.
    Hum. Genet. 111:314-322(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PD ARG-448.

Entry informationi

Entry nameiPEPD_HUMAN
AccessioniPrimary (citable) accession number: P12955
Secondary accession number(s): A8K3Z1
, A8K416, A8K696, A8MX47, B4DDB7, B4DGJ1, E9PCE8, Q8TBN9, Q9BT75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 171 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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