Reviewed, UniProtKB/Swiss-Prot Q96KP4 (CNDP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Cytosolic non-specific dipeptidase
Alternative name(s):
    CNDP dipeptidase 2
    Glutamate carboxypeptidase-like protein 1
    Peptidase A

Gene names

Name:	CNDP2
Synonyms:	CN2, CPGL, PEPA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	475 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)

Cofactor	Binds 2 zinc ions per subunit By similarity.
Sequence similarities	Belongs to the peptidase M20A family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW protein dimerization activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDRG1	Q92597	1	EBI-1190734,EBI-716486

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 475	474	Cytosolic non-specific dipeptidase		PRO_0000185272
Sites
	Active site	101	1	By similarity
	Active site	166	1	Proton acceptor By similarity
	Metal binding	99	1	Zinc 2 By similarity
	Metal binding	132	1	Zinc 1 By similarity
	Metal binding	132	1	Zinc 2 By similarity
	Metal binding	167	1	Zinc 1 By similarity
	Metal binding	195	1	Zinc 2 By similarity
	Metal binding	445	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.4
Natural variations
	Natural variant	126	1	Y → H: dbSNP rs2278161.		VAR_057154
Experimental info
	Sequence conflict	128	1	R → G in BAA91840. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q96KP4-1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: 43FA0668B0587A39	FASTA	475	52,878
	10 20 30 40 50 60 MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA DVKQLGGSVE 70 80 90 100 110 120 LVDIGKQKLP DGSEIPLPPI LLGRLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE 130 140 150 160 170 180 RDGKLYGRGS TDDKGPVAGW INALEAYQKT GQEIPVNVRF CLEGMEESGS EGLDELIFAR 190 200 210 220 230 240 KDTFFKDVDY VCISDNYWLG KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM 250 260 270 280 290 300 TDLILLMGSL VDKRGNILIP GINEAVAAVT EEEHKLYDDI DFDIEEFAKD VGAQILLHSH 310 320 330 340 350 360 KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP EVVGEQVTSY 370 380 390 400 410 420 LTKKFAELRS PNEFKVYMGH GGKPWVSDFS HPHYLAGRRA MKTVFGVEPD LTREGGSIPV 430 440 450 460 470 TLTFQEATGK NVMLLPVGSA DDGAHSQNEK LNRYNYIEGT KMLAAYLYEV SQLKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], VARIANT HIS-126. Tissue: Uterus.
[2]	"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].
[3]	"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]. Tissue: Colon and Kidney.
[4]	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, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ347717 mRNA. Translation: CAC69883.1. AK001692 mRNA. Translation: BAA91840.1. BC001375 mRNA. Translation: AAH01375.1. BC003176 mRNA. Translation: AAH03176.1.
IPI	IPI00177728.
RefSeq	NP_060705.1.
UniGene	Hs.149185
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96KP4. 1 interaction.
Protein family/group databases
MEROPS	M20.005.
PTM databases
PhosphoSite	Q96KP4.
2-D gel databases
OGP	Q96KP4.
Proteomic databases
PRIDE	Q96KP4.
Genome annotation databases
Ensembl	ENSG00000133313. Homo sapiens. [Contig view]
GeneID	55748.
KEGG	hsa:55748.
NMPDR	fig|9606.3.peg.15152.
Organism-specific databases
GeneCards	GC18P070314.
HGNC	HGNC:24437. CNDP2.
MIM	169800. gene.
PharmGKB	PA134975242.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q96KP4.
HOVERGEN	Q96KP4.
OMA	Q96KP4. LIFAQKD.
Gene expression databases
ArrayExpress	Q96KP4.
Bgee	Q96KP4.
CleanEx	HS_CNDP2.
GermOnline	ENSG00000133313. Homo sapiens.
Family and domain databases
InterPro	IPR001261. ArgE/DapE_CS. IPR017153. GSH_degradosome_DUG1. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. False negative. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	60729.
SOURCE	Search...

Entry information

Entry name

CNDP2_HUMAN

Accession

Primary (citable) accession number: Q96KP4
Secondary accession number(s): Q9BQ94, Q9NVB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	September 19, 2002
Last modified:	July 7, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)