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Q5U5Z8 (CBPC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic carboxypeptidase 2

EC=3.4.17.-
Alternative name(s):
ATP/GTP-binding protein-like 2
Gene names
Name:AGBL2
Synonyms:CCP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metallocarboxypeptidase involved in the detyrosination of alpha-tubulin C-terminus. Ref.5

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by RARRES1. Ref.5

Subcellular location

Cytoplasmcytosol By similarity.

Sequence similarities

Belongs to the peptidase M14 family.

Sequence caution

The sequence BAB15707.1 differs from that shown. Reason: Erroneous termination at position 797. Translated as Lys.

The sequence BAD96891.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD96896.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetallocarboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5U5Z8-1)

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: Q5U5Z8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-471: Missing.
Isoform 3 (identifier: Q5U5Z8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-617: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 902902Cytosolic carboxypeptidase 2
PRO_0000283748

Sites

Active site5121Nucleophile By similarity
Metal binding4621Zinc By similarity
Metal binding4651Zinc By similarity
Metal binding5581Zinc By similarity

Natural variations

Alternative sequence1 – 617617Missing in isoform 3.
VSP_024361
Alternative sequence1 – 471471Missing in isoform 2.
VSP_024360
Natural variant901I → R.
Corresponds to variant rs12795414 [ dbSNP | Ensembl ].
VAR_046637
Natural variant3331T → P.
Corresponds to variant rs35898124 [ dbSNP | Ensembl ].
VAR_046638
Natural variant3491R → H.
Corresponds to variant rs7941404 [ dbSNP | Ensembl ].
VAR_031572
Natural variant3681D → G.
Corresponds to variant rs1870545 [ dbSNP | Ensembl ].
VAR_046639
Natural variant6711M → I. Ref.1 Ref.2 Ref.4
Corresponds to variant rs12286721 [ dbSNP | Ensembl ].
VAR_046640

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: C9C5D8260AFBCF65

FASTA902104,194
        10         20         30         40         50         60 
MFPALETHLK QTIPDPYEDF MYRHLQYYGY FKAQRGSLPN SATHQHVRKN NPQCLLNGSL 

        70         80         90        100        110        120 
GEKDDLIPDT LQKEKLLWPI SLSSAVHRQI EAINRDFHSC LGWMQWRGLS SLQPPPPRFK 

       130        140        150        160        170        180 
DSPASAFRVA GITDSHMLSL PHLRSRQLLY DELDEVNPRL REPQELFSIL STKRPLQAPR 

       190        200        210        220        230        240 
WPIECEVIKE NIHHIEWAPP QPEYFYQPKG NEKVPEIVGE KKGTVVYQLD SVPIEGSYFT 

       250        260        270        280        290        300 
SSRVGGKRGI VKELAVTLQG PEDNTLLFES RFESGNLQKA VRVDTYEYEL TLRTDLYTNK 

       310        320        330        340        350        360 
HTQWFYFRVQ NTRKDATYRF TIVNLLKPKS LYTVGMKPLL YSQLDANTRN IGWRREGNEI 

       370        380        390        400        410        420 
KYYKNNTDDG QQPFYCLTWT IQFPYDQDTC FFAHFYPYTY TDLQCYLLSV ANNPIQSQFC 

       430        440        450        460        470        480 
KLQTLCRSLA GNTVYLLTIT NPSQTPQEAA AKKAVVLSAR VHPGESNGSW VMKGFLDFIL 

       490        500        510        520        530        540 
SNSPDAQLLR DIFVFKVLPM LNPDGVIVGN YRCSLAGRDL NRHYKTILKE SFPCIWYTRN 

       550        560        570        580        590        600 
MIKRLLEERE VLLYCDFHGH SRKNNIFLYG CNNNNRKYWL HERVFPLMLC KNAPDKFSFH 

       610        620        630        640        650        660 
SCNFKVQKCK EGTGRVVMWR MGILNSYTME STFGGSTLGN KRDTHFTIED LKSLGYHVCD 

       670        680        690        700        710        720 
TLLDFCDPDQ MKFTQCLAEL KELLRQEIHK KFHELGQDVD LEGSWSDISL SDIESSTSGS 

       730        740        750        760        770        780 
DSSLSDGLPV HLANIADELT QKKKMFKKKK KKSLQTRKQR NEQYQKKNLM QKLKLTEDTS 

       790        800        810        820        830        840 
EKAGFASTLQ KQPTFFKNSE NSSFLPMKNE NPRLNETNLN RRDKDTPLDP SMATLILPKN 

       850        860        870        880        890        900 
KGRMQNKKPG FTVSCSPKRT INSSQEPAPG MKPNWPRSRY PATKRGCAAM AAYPSLHIYT 


YP 

« Hide

Isoform 2 [UniParc].

Checksum: 24C22924E231027A
Show »

FASTA43149,706
Isoform 3 [UniParc].

Checksum: C5D03FEC06B4A594
Show »

FASTA28532,454

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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 2), VARIANT ILE-671.
Tissue: Lung.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-671.
Tissue: Lung.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 3), VARIANT ILE-671.
Tissue: Lung and Testis.
[5]"Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2 to regulate the alpha-tubulin tyrosination cycle."
Sahab Z.J., Hall M.D., Me Sung Y., Dakshanamurthy S., Ji Y., Kumar D., Byers S.W.
Cancer Res. 71:1219-1228(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, 3D-STRUCTURE MODELING, ENZYME REGULATION, INTERACTION WITH RARRES1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027251 mRNA. Translation: BAB15707.1. Sequence problems.
AK223171 mRNA. Translation: BAD96891.1. Different initiation.
AK223176 mRNA. Translation: BAD96896.1. Different initiation.
AC021443 Genomic DNA. No translation available.
BC028200 mRNA. Translation: AAH28200.1.
BC036234 mRNA. Translation: AAH36234.1.
RefSeqNP_079059.2. NM_024783.3.
UniGeneHs.147377.

3D structure databases

ProteinModelPortalQ5U5Z8.
SMRQ5U5Z8. Positions 265-668.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122932. 3 interactions.
STRING9606.ENSP00000298861.

Protein family/group databases

MEROPSM14.029.

PTM databases

PhosphoSiteQ5U5Z8.

Polymorphism databases

DMDM206729855.

Proteomic databases

PaxDbQ5U5Z8.
PRIDEQ5U5Z8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298861; ENSP00000298861; ENSG00000165923. [Q5U5Z8-1]
ENST00000525123; ENSP00000435582; ENSG00000165923. [Q5U5Z8-1]
GeneID79841.
KEGGhsa:79841.
UCSCuc001ngg.3. human. [Q5U5Z8-1]

Organism-specific databases

CTD79841.
GeneCardsGC11M047681.
HGNCHGNC:26296. AGBL2.
HPAHPA007718.
neXtProtNX_Q5U5Z8.
PharmGKBPA142672634.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000111052.
HOVERGENHBG070840.
OrthoDBEOG78H3SB.
PhylomeDBQ5U5Z8.
TreeFamTF313794.

Gene expression databases

ArrayExpressQ5U5Z8.
BgeeQ5U5Z8.
CleanExHS_AGBL2.
GenevestigatorQ5U5Z8.

Family and domain databases

InterProIPR000834. Peptidase_M14.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi79841.
NextBio69520.
PROQ5U5Z8.

Entry information

Entry nameCBPC2_HUMAN
AccessionPrimary (citable) accession number: Q5U5Z8
Secondary accession number(s): A8MPX2 expand/collapse secondary AC list , Q53FV5, Q8IV57, Q9H5C0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM