Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lysosomal Pro-X carboxypeptidase

Gene

PRCP

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

Functioni

Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

Catalytic activityi

Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791Charge relay system1 Publication
Active sitei430 – 4301Charge relay system1 Publication
Active sitei455 – 4551Charge relay system1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.16.2. 2681.
ReactomeiREACT_326. Intrinsic Pathway of Fibrin Clot Formation.

Protein family/group databases

ESTHERihuman-PRCP. Prolylcarboxypeptidase.
MEROPSiS28.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysosomal Pro-X carboxypeptidase (EC:3.4.16.2)
Alternative name(s):
Angiotensinase C
Lysosomal carboxypeptidase C
Proline carboxypeptidase
Prolylcarboxypeptidase
Short name:
PRCP
Gene namesi
Name:PRCP
Synonyms:PCP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9344. PRCP.

Subcellular locationi

GO - Cellular componenti

  • basal part of cell Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • lysosome Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33705.

Polymorphism and mutation databases

BioMutaiPRCP.
DMDMi1172047.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 4524PRO_0000027308Add
BLAST
Chaini46 – 496451Lysosomal Pro-X carboxypeptidasePRO_0000027309Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
Disulfide bondi215 ↔ 3721 Publication
Disulfide bondi233 ↔ 3101 Publication
Disulfide bondi264 ↔ 3431 Publication
Glycosylationi317 – 3171N-linked (GlcNAc...)2 Publications
Glycosylationi336 – 3361N-linked (GlcNAc...)1 Publication
Glycosylationi345 – 3451N-linked (GlcNAc...)1 Publication
Disulfide bondi364 ↔ 3941 Publication
Glycosylationi415 – 4151N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP42785.
PaxDbiP42785.
PRIDEiP42785.

PTM databases

PhosphoSiteiP42785.

Expressioni

Tissue specificityi

Highest levels in placenta, lung and liver. Also present in heart, brain, pancreas and kidney.

Gene expression databases

BgeeiP42785.
CleanExiHS_PRCP.
ExpressionAtlasiP42785. baseline and differential.
GenevisibleiP42785. HS.

Organism-specific databases

HPAiHPA017065.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GPR37L1O608832EBI-2803892,EBI-2927498

Protein-protein interaction databases

BioGridi111538. 12 interactions.
IntActiP42785. 4 interactions.
MINTiMINT-3015634.
STRINGi9606.ENSP00000377055.

Structurei

Secondary structure

1
496
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 579Combined sources
Beta strandi67 – 759Combined sources
Turni81 – 833Combined sources
Beta strandi85 – 906Combined sources
Helixi96 – 1027Combined sources
Helixi104 – 11310Combined sources
Beta strandi115 – 1206Combined sources
Helixi132 – 1365Combined sources
Turni139 – 1413Combined sources
Helixi147 – 16418Combined sources
Helixi168 – 1703Combined sources
Beta strandi173 – 1786Combined sources
Helixi180 – 19112Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 2026Combined sources
Helixi217 – 22711Combined sources
Helixi233 – 24715Combined sources
Helixi251 – 26010Combined sources
Beta strandi263 – 2653Combined sources
Helixi272 – 28817Combined sources
Beta strandi295 – 3017Combined sources
Helixi305 – 3128Combined sources
Helixi320 – 33617Combined sources
Beta strandi342 – 3443Combined sources
Helixi354 – 36512Combined sources
Beta strandi375 – 3806Combined sources
Helixi387 – 39812Combined sources
Helixi406 – 4116Combined sources
Beta strandi422 – 4298Combined sources
Helixi431 – 4355Combined sources
Beta strandi441 – 45010Combined sources
Helixi457 – 4593Combined sources
Helixi468 – 48922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2ZX-ray2.79B46-491[»]
ProteinModelPortaliP42785.
SMRiP42785. Positions 46-491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42785.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 334141SKS domainAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290141.
GeneTreeiENSGT00530000063027.
HOGENOMiHOG000238311.
HOVERGENiHBG005526.
InParanoidiP42785.
KOiK01285.
OMAiKQWGVRP.
OrthoDBiEOG78WKRN.
PhylomeDBiP42785.
TreeFamiTF314414.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERiPTHR11010. PTHR11010. 1 hit.
PfamiPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P42785-1) [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
MGRRALLLLL LSFLAPWATI ALRPALRALG SLHLPTNPTS LPAVAKNYSV
60 70 80 90 100
LYFQQKVDHF GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC
110 120 130 140 150
NNTGFMWDVA EELKAMLVFA EHRYYGESLP FGDNSFKDSR HLNFLTSEQA
160 170 180 190 200
LADFAELIKH LKRTIPGAEN QPVIAIGGSY GGMLAAWFRM KYPHMVVGAL
210 220 230 240 250
AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIHRS WDAINRLSNT
260 270 280 290 300
GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP
310 320 330 340 350
LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA
360 370 380 390 400
TSSLGTLGWS YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV
410 420 430 440 450
RPRPSWITTM YGGKNISSHT NIVFSNGELD PWSGGGVTKD ITDTLVAVTI
460 470 480 490
SEGAHHLDLR TKNALDPMSV LLARSLEVRH MKNWIRDFYD SAGKQH
Length:496
Mass (Da):55,800
Last modified:November 1, 1995 - v1
Checksum:iFC5DD570D3D3AB4F
GO
Isoform 2 (identifier: P42785-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-56: K → KALAAGQLHICIIQLNHYKTPL

Note: No experimental confirmation available.
Show »
Length:517
Mass (Da):58,100
Checksum:iA2490258A57E6F23
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041G → E in BAG52417 (PubMed:14702039).Curated
Sequence conflicti248 – 2481S → L in BAG52417 (PubMed:14702039).Curated
Sequence conflicti304 – 3041W → R in BAG52417 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121E → D.1 Publication
Corresponds to variant rs2298668 [ dbSNP | Ensembl ].
VAR_020464
Natural varianti444 – 4441T → S.
Corresponds to variant rs2228312 [ dbSNP | Ensembl ].
VAR_029329

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei56 – 561K → KALAAGQLHICIIQLNHYKT PL in isoform 2. 1 PublicationVSP_045799

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13977 mRNA. Translation: AAA99891.1.
AK091786 mRNA. Translation: BAG52417.1.
AK312919 mRNA. Translation: BAG35764.1.
AB451270 mRNA. Translation: BAG70084.1.
AB451397 mRNA. Translation: BAG70211.1.
AP000893 Genomic DNA. No translation available.
AP001646 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75074.1.
CH471076 Genomic DNA. Translation: EAW75075.1.
BC001500 mRNA. Translation: AAH01500.1.
CCDSiCCDS41695.1. [P42785-2]
CCDS8262.1. [P42785-1]
PIRiA47352.
RefSeqiNP_005031.1. NM_005040.2. [P42785-1]
NP_955450.2. NM_199418.2. [P42785-2]
UniGeneiHs.523936.

Genome annotation databases

EnsembliENST00000313010; ENSP00000317362; ENSG00000137509. [P42785-1]
ENST00000393399; ENSP00000377055; ENSG00000137509. [P42785-2]
GeneIDi5547.
KEGGihsa:5547.
UCSCiuc001ozr.3. human.
uc001ozs.3. human. [P42785-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13977 mRNA. Translation: AAA99891.1.
AK091786 mRNA. Translation: BAG52417.1.
AK312919 mRNA. Translation: BAG35764.1.
AB451270 mRNA. Translation: BAG70084.1.
AB451397 mRNA. Translation: BAG70211.1.
AP000893 Genomic DNA. No translation available.
AP001646 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75074.1.
CH471076 Genomic DNA. Translation: EAW75075.1.
BC001500 mRNA. Translation: AAH01500.1.
CCDSiCCDS41695.1. [P42785-2]
CCDS8262.1. [P42785-1]
PIRiA47352.
RefSeqiNP_005031.1. NM_005040.2. [P42785-1]
NP_955450.2. NM_199418.2. [P42785-2]
UniGeneiHs.523936.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2ZX-ray2.79B46-491[»]
ProteinModelPortaliP42785.
SMRiP42785. Positions 46-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111538. 12 interactions.
IntActiP42785. 4 interactions.
MINTiMINT-3015634.
STRINGi9606.ENSP00000377055.

Chemistry

BindingDBiP42785.
ChEMBLiCHEMBL2335.

Protein family/group databases

ESTHERihuman-PRCP. Prolylcarboxypeptidase.
MEROPSiS28.001.

PTM databases

PhosphoSiteiP42785.

Polymorphism and mutation databases

BioMutaiPRCP.
DMDMi1172047.

Proteomic databases

MaxQBiP42785.
PaxDbiP42785.
PRIDEiP42785.

Protocols and materials databases

DNASUi5547.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313010; ENSP00000317362; ENSG00000137509. [P42785-1]
ENST00000393399; ENSP00000377055; ENSG00000137509. [P42785-2]
GeneIDi5547.
KEGGihsa:5547.
UCSCiuc001ozr.3. human.
uc001ozs.3. human. [P42785-1]

Organism-specific databases

CTDi5547.
GeneCardsiGC11M082535.
HGNCiHGNC:9344. PRCP.
HPAiHPA017065.
MIMi176785. gene.
neXtProtiNX_P42785.
PharmGKBiPA33705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG290141.
GeneTreeiENSGT00530000063027.
HOGENOMiHOG000238311.
HOVERGENiHBG005526.
InParanoidiP42785.
KOiK01285.
OMAiKQWGVRP.
OrthoDBiEOG78WKRN.
PhylomeDBiP42785.
TreeFamiTF314414.

Enzyme and pathway databases

BRENDAi3.4.16.2. 2681.
ReactomeiREACT_326. Intrinsic Pathway of Fibrin Clot Formation.

Miscellaneous databases

ChiTaRSiPRCP. human.
EvolutionaryTraceiP42785.
GeneWikiiPRCP.
GenomeRNAii5547.
NextBioi21494.
PROiP42785.
SOURCEiSearch...

Gene expression databases

BgeeiP42785.
CleanExiHS_PRCP.
ExpressionAtlasiP42785. baseline and differential.
GenevisibleiP42785. HS.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERiPTHR11010. PTHR11010. 1 hit.
PfamiPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families."
    Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
    J. Biol. Chem. 268:16631-16638(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Kidney.
  2. Erratum
    Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
    J. Biol. Chem. 268:26032-26032(1993)
  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 AND 2), VARIANT ASP-112.
    Tissue: Kidney and Lung.
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney."
    Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., Erdos E.G.
    J. Biol. Chem. 253:5927-5931(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Kidney.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-415.
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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].
    Tissue: Liver.
  12. "Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase."
    Soisson S.M., Patel S.B., Abeywickrema P.D., Byrne N.J., Diehl R.E., Hall D.L., Ford R.E., Reid J.C., Rickert K.W., Shipman J.M., Sharma S., Lumb K.J.
    BMC Struct. Biol. 10:16-16(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 46-491, SUBUNIT, DISULFIDE BONDS, ACTIVE SITE, GLYCOSYLATION AT ASN-101; ASN-317; ASN-336; ASN-345 AND ASN-415.

Entry informationi

Entry nameiPCP_HUMAN
AccessioniPrimary (citable) accession number: P42785
Secondary accession number(s): A8MU24
, B2R7B7, B3KRK5, B5BU34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 144 of the entry and version 1 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 11
    Human chromosome 11: 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

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.