SubmitCancel

Skip Header

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

Q96KP4

- CNDP2_HUMAN

UniProt

Q96KP4 - CNDP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cytosolic non-specific dipeptidase

Gene
CNDP2, CN2, CPGL, PEPA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Isoform 2 may be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells.2 Publications

Catalytic activityi

Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.1 Publication

Cofactori

Binds 2 manganese ions per subunit By similarity.

Enzyme regulationi

Inhibited by p-hydroxymercurybenzoate. The inhibitory concentration 50% (IC50) is 13 µM. Inhibited by bestatin. The inhibitory concentration 50% (IC50) is 7 nM at pH 9.5.1 Publication

Kineticsi

  1. KM=1.04 mM for Ser-Gln (at pH 7.5 and in the presence of 0.1 mM manganese ions)2 Publications
  2. KM=0.6 mM for Cys-Gly (at pH 8.0 and in the presence of 50 µM manganese ions)
  3. KM=15 mM for carnosine (at pH 9.5 and in the presence of 0.1 mM manganese ions)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Manganese 2 By similarity
Active sitei101 – 1011 By similarity
Metal bindingi132 – 1321Manganese 1 By similarity
Metal bindingi132 – 1321Manganese 2 By similarity
Active sitei166 – 1661Proton acceptor By similarity
Metal bindingi167 – 1671Manganese 1 By similarity
Metal bindingi195 – 1951Manganese 2 By similarity
Binding sitei195 – 1951Substrate; via carbonyl oxygen By similarity
Binding sitei228 – 2281Substrate; shared with homodimeric partner By similarity
Sitei228 – 2281Important for catalytic activity By similarity
Binding sitei330 – 3301Substrate; shared with homodimeric partner By similarity
Binding sitei343 – 3431Substrate By similarity
Binding sitei417 – 4171Substrate; via amide nitrogen and carbonyl oxygen By similarity
Metal bindingi445 – 4451Manganese 1 By similarity
Binding sitei445 – 4451Substrate By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: Reactome
  2. dipeptidase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. metallopeptidase activity Source: UniProtKB-KW
  5. tripeptidase activity Source: InterPro

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. glutathione biosynthetic process Source: Reactome
  3. glutathione derivative biosynthetic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. sulfur amino acid metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.13.18. 2681.
ReactomeiREACT_115639. Sulfur amino acid metabolism.
REACT_6960. Glutathione synthesis and recycling.
SABIO-RKQ96KP4.

Protein family/group databases

MEROPSiM20.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic non-specific dipeptidase (EC:3.4.13.18)
Alternative name(s):
CNDP dipeptidase 2
Glutamate carboxypeptidase-like protein 1
Peptidase A
Gene namesi
Name:CNDP2
Synonyms:CN2, CPGL, PEPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:24437. CNDP2.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134975242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 475474Cytosolic non-specific dipeptidasePRO_0000185272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei9 – 91N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96KP4.
PaxDbiQ96KP4.
PRIDEiQ96KP4.

2D gel databases

OGPiQ96KP4.

PTM databases

PhosphoSiteiQ96KP4.

Expressioni

Tissue specificityi

Isoform 1 is ubiquitously expressed with higher levels in kidney and liver (at protein level). Isoform 2 is expressed in fetal tissues, it is only expressed in adult liver and placental tissues.2 Publications

Gene expression databases

ArrayExpressiQ96KP4.
BgeeiQ96KP4.
CleanExiHS_CNDP2.
GenevestigatoriQ96KP4.

Organism-specific databases

HPAiCAB026196.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NDRG1Q925971EBI-1190734,EBI-716486

Protein-protein interaction databases

BioGridi120866. 36 interactions.
IntActiQ96KP4. 2 interactions.
STRINGi9606.ENSP00000325548.

Structurei

3D structure databases

ProteinModelPortaliQ96KP4.
SMRiQ96KP4. Positions 1-474.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 1672Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M20A family.

Phylogenomic databases

eggNOGiCOG0624.
HOGENOMiHOG000216709.
HOVERGENiHBG051103.
InParanoidiQ96KP4.
KOiK08660.
OMAiTDGAHSI.
PhylomeDBiQ96KP4.
TreeFamiTF300633.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEiPS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

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. Align

Isoform 1 (identifier: Q96KP4-1) [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

MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA    50
DVKQLGGSVE LVDIGKQKLP DGSEIPLPPI LLGRLGSDPQ KKTVCIYGHL 100
DVQPAALEDG WDSEPFTLVE RDGKLYGRGS TDDKGPVAGW INALEAYQKT 150
GQEIPVNVRF CLEGMEESGS EGLDELIFAR KDTFFKDVDY VCISDNYWLG 200
KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM TDLILLMGSL 250
VDKRGNILIP GINEAVAAVT EEEHKLYDDI DFDIEEFAKD VGAQILLHSH 300
KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP 350
EVVGEQVTSY LTKKFAELRS PNEFKVYMGH GGKPWVSDFS HPHYLAGRRA 400
MKTVFGVEPD LTREGGSIPV TLTFQEATGK NVMLLPVGSA DDGAHSQNEK 450
LNRYNYIEGT KMLAAYLYEV SQLKD 475
Length:475
Mass (Da):52,878
Last modified:September 19, 2002 - v2
Checksum:i43FA0668B0587A39
GO
Isoform 2 (identifier: Q96KP4-2) [UniParc]FASTAAdd to Basket

Also known as: CPGL-B

The sequence of this isoform differs from the canonical sequence as follows:
     69-152: Missing.

Show »
Length:391
Mass (Da):43,833
Checksum:i07E5F4464C8FC179
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261Y → H.1 Publication
Corresponds to variant rs2278161 [ dbSNP | Ensembl ].
VAR_057154

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 15284Missing in isoform 2. VSP_038203Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281R → G in BAA91840. 1 Publication
Sequence conflicti348 – 3481M → T in BAG53426. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AX523938 Unassigned DNA. Translation: CAD56843.1.
AJ347717 mRNA. Translation: CAC69883.1.
AK001692 mRNA. Translation: BAA91840.1.
AK097155 mRNA. Translation: BAG53426.1.
AF258592 mRNA. Translation: AAG23795.1.
AC009704 Genomic DNA. No translation available.
CH471117 Genomic DNA. Translation: EAW66551.1.
BC001375 mRNA. Translation: AAH01375.1.
BC003176 mRNA. Translation: AAH03176.1.
CCDSiCCDS12006.1. [Q96KP4-1]
CCDS54190.1. [Q96KP4-2]
RefSeqiNP_001161971.1. NM_001168499.1. [Q96KP4-2]
NP_060705.2. NM_018235.2. [Q96KP4-1]
XP_005266785.1. XM_005266728.1. [Q96KP4-1]
XP_006722565.1. XM_006722502.1. [Q96KP4-1]
XP_006722566.1. XM_006722503.1. [Q96KP4-1]
UniGeneiHs.149185.

Genome annotation databases

EnsembliENST00000324262; ENSP00000325548; ENSG00000133313. [Q96KP4-1]
ENST00000324301; ENSP00000325756; ENSG00000133313. [Q96KP4-2]
ENST00000579847; ENSP00000462311; ENSG00000133313. [Q96KP4-1]
GeneIDi55748.
KEGGihsa:55748.
UCSCiuc002llm.2. human. [Q96KP4-1]
uc002lln.2. human. [Q96KP4-2]

Polymorphism databases

DMDMi23396498.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AX523938 Unassigned DNA. Translation: CAD56843.1 .
AJ347717 mRNA. Translation: CAC69883.1 .
AK001692 mRNA. Translation: BAA91840.1 .
AK097155 mRNA. Translation: BAG53426.1 .
AF258592 mRNA. Translation: AAG23795.1 .
AC009704 Genomic DNA. No translation available.
CH471117 Genomic DNA. Translation: EAW66551.1 .
BC001375 mRNA. Translation: AAH01375.1 .
BC003176 mRNA. Translation: AAH03176.1 .
CCDSi CCDS12006.1. [Q96KP4-1 ]
CCDS54190.1. [Q96KP4-2 ]
RefSeqi NP_001161971.1. NM_001168499.1. [Q96KP4-2 ]
NP_060705.2. NM_018235.2. [Q96KP4-1 ]
XP_005266785.1. XM_005266728.1. [Q96KP4-1 ]
XP_006722565.1. XM_006722502.1. [Q96KP4-1 ]
XP_006722566.1. XM_006722503.1. [Q96KP4-1 ]
UniGenei Hs.149185.

3D structure databases

ProteinModelPortali Q96KP4.
SMRi Q96KP4. Positions 1-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120866. 36 interactions.
IntActi Q96KP4. 2 interactions.
STRINGi 9606.ENSP00000325548.

Protein family/group databases

MEROPSi M20.005.

PTM databases

PhosphoSitei Q96KP4.

Polymorphism databases

DMDMi 23396498.

2D gel databases

OGPi Q96KP4.

Proteomic databases

MaxQBi Q96KP4.
PaxDbi Q96KP4.
PRIDEi Q96KP4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324262 ; ENSP00000325548 ; ENSG00000133313 . [Q96KP4-1 ]
ENST00000324301 ; ENSP00000325756 ; ENSG00000133313 . [Q96KP4-2 ]
ENST00000579847 ; ENSP00000462311 ; ENSG00000133313 . [Q96KP4-1 ]
GeneIDi 55748.
KEGGi hsa:55748.
UCSCi uc002llm.2. human. [Q96KP4-1 ]
uc002lln.2. human. [Q96KP4-2 ]

Organism-specific databases

CTDi 55748.
GeneCardsi GC18P072163.
H-InvDB HIX0136845.
HGNCi HGNC:24437. CNDP2.
HPAi CAB026196.
MIMi 169800. gene.
neXtProti NX_Q96KP4.
PharmGKBi PA134975242.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0624.
HOGENOMi HOG000216709.
HOVERGENi HBG051103.
InParanoidi Q96KP4.
KOi K08660.
OMAi TDGAHSI.
PhylomeDBi Q96KP4.
TreeFami TF300633.

Enzyme and pathway databases

BRENDAi 3.4.13.18. 2681.
Reactomei REACT_115639. Sulfur amino acid metabolism.
REACT_6960. Glutathione synthesis and recycling.
SABIO-RK Q96KP4.

Miscellaneous databases

ChiTaRSi CNDP2. human.
GenomeRNAii 55748.
NextBioi 60729.
PROi Q96KP4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96KP4.
Bgeei Q96KP4.
CleanExi HS_CNDP2.
Genevestigatori Q96KP4.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR001261. ArgE/DapE_CS.
IPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEi PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase."
    Teufel M., Saudek V., Ledig J.P., Bernhardt A., Boularand S., Carreau A., Cairns N.J., Carter C., Cowley D.J., Duverger D., Ganzhorn A.J., Guenet C., Heintzelmann B., Laucher V., Sauvage C., Smirnova T.
    J. Biol. Chem. 278:6521-6531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 129-137; 276-289; 311-329; 370-375 AND 462-474, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Cloning and sequencing of human glutamate carboxypeptidase homologue in peptidase family M20."
    Chen J.M., Barrett A.J.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-126.
    Tissue: Uterus.
  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] (ISOFORM 1).
    Tissue: Spleen and Teratocarcinoma.
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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: Colon and Kidney.
  8. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-9; 54-66; 255-275 AND 403-430, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  9. "Identification of carboxypeptidase of glutamate like-B as a candidate suppressor in cell growth and metastasis in human hepatocellular carcinoma."
    Zhang P., Chan D.W., Zhu Y., Li J.J., Ng I.-O., Wan D., Gu J.
    Clin. Cancer Res. 12:6617-6625(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
  10. "Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases."
    Kaur H., Kumar C., Junot C., Toledano M.B., Bachhawat A.K.
    J. Biol. Chem. 284:14493-14502(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "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 ALA-2 AND LYS-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCNDP2_HUMAN
AccessioniPrimary (citable) accession number: Q96KP4
Secondary accession number(s): B3KUG4
, Q8WY59, Q9BQ94, Q9NVB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: September 3, 2014
This is version 118 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi