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Q9UPW5

- CBPC1_HUMAN

UniProt

Q9UPW5 - CBPC1_HUMAN

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Protein

Cytosolic carboxypeptidase 1

Gene

AGTPBP1

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

Functioni

Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi920 – 9201ZincBy similarity
Metal bindingi923 – 9231ZincBy similarity
Active sitei970 – 9701NucleophileBy similarity
Metal bindingi1017 – 10171ZincBy similarity

GO - Molecular functioni

  1. metallocarboxypeptidase activity Source: UniProtKB
  2. tubulin binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. adult walking behavior Source: Ensembl
  2. cerebellar Purkinje cell differentiation Source: UniProtKB
  3. C-terminal protein deglutamylation Source: UniProtKB
  4. eye photoreceptor cell differentiation Source: UniProtKB
  5. mitochondrion organization Source: UniProtKB
  6. neuromuscular process Source: UniProtKB
  7. neurotransmitter metabolic process Source: Ensembl
  8. olfactory bulb development Source: UniProtKB
  9. protein side chain deglutamylation Source: UniProtKB
  10. retina development in camera-type eye Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM14.028.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic carboxypeptidase 1 (EC:3.4.17.-)
Alternative name(s):
ATP/GTP-binding protein 1
Nervous system nuclear protein induced by axotomy protein 1 homolog
Gene namesi
Name:AGTPBP1
Synonyms:CCP1, KIAA1035, NNA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17258. AGTPBP1.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytosol By similarity. Nucleus 1 Publication. Mitochondrion By similarity
Note: Localizes in both the cytoplasm and nuclei of interphase and dividing cells.1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24630.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12261226Cytosolic carboxypeptidase 1PRO_0000308690Add
BLAST

Proteomic databases

MaxQBiQ9UPW5.
PaxDbiQ9UPW5.
PRIDEiQ9UPW5.

PTM databases

PhosphoSiteiQ9UPW5.

Expressioni

Gene expression databases

BgeeiQ9UPW5.
CleanExiHS_AGTPBP1.
ExpressionAtlasiQ9UPW5. baseline and differential.
GenevestigatoriQ9UPW5.

Organism-specific databases

HPAiHPA057208.

Interactioni

Subunit structurei

Interacts with MYLK.By similarity

Protein-protein interaction databases

BioGridi116885. 11 interactions.
IntActiQ9UPW5. 9 interactions.
MINTiMINT-2858492.
STRINGi9606.ENSP00000338512.

Structurei

3D structure databases

ProteinModelPortaliQ9UPW5.
SMRiQ9UPW5. Positions 710-1032.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00550000074405.
HOVERGENiHBG107587.
InParanoidiQ9UPW5.
OMAiDVLCETL.
OrthoDBiEOG712TVD.
PhylomeDBiQ9UPW5.
TreeFamiTF313794.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UPW5-1) [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
MSKLKVIPEK SLTNNSRIVG LLAQLEKINA EPSESDTARY VTSKILHLAQ
60 70 80 90 100
SQEKTRREMT AKGSTGMEIL LSTLENTKDL QTTLNILSIL VELVSAGGGR
110 120 130 140 150
RVSFLVTKGG SQILLQLLMN ASKESPPHED LMVQIHSILA KIGPKDKKFG
160 170 180 190 200
VKARINGALN ITLNLVKQNL QNHRLVLPCL QLLRVYSANS VNSVSLGKNG
210 220 230 240 250
VVELMFKIIG PFSKKNSSLI KVALDTLAAL LKSKTNARRA VDRGYVQVLL
260 270 280 290 300
TIYVDWHRHD NRHRNMLIRK GILQSLKSVT NIKLGRKAFI DANGMKILYN
310 320 330 340 350
TSQECLAVRT LDPLVNTSSL IMRKCFPKNR LPLPTIKSSF HFQLPVIPVT
360 370 380 390 400
GPVAQLYSLP PEVDDVVDES DDNDDIDVEA ENETENEDDL DQNFKNDDIE
410 420 430 440 450
TDINKLKPQQ EPGRTIEDLK MYEHLFPELV DDFQDYDLIS KEPKPFVFEG
460 470 480 490 500
KVRGPIVVPT AGEETSGNSG NLRKVVMKEN ISSKGDEGEK KSTFMDLAKE
510 520 530 540 550
DIKDNDRTLQ QQPGDQNRTI SSVHGLNNDI VKALDRITLQ NIPSQTAPGF
560 570 580 590 600
TAEMKKDCSL PLTVLTCAKA CPHMATCGNV LFEGRTVQLG KLCCTGVETE
610 620 630 640 650
DDEDTESNSS VEQASVEVPD GPTLHDPDLY IEIVKNTKSV PEYSEVAYPD
660 670 680 690 700
YFGHIPPPFK EPILERPYGV QRTKIAQDIE RLIHQSDIID RVVYDLDNPN
710 720 730 740 750
YTIPEEGDIL KFNSKFESGN LRKVIQIRKN EYDLILNSDI NSNHYHQWFY
760 770 780 790 800
FEVSGMRPGV AYRFNIINCE KSNSQFNYGM QPLMYSVQEA LNARPWWIRM
810 820 830 840 850
GTDICYYKNH FSRSSVAAGG QKGKSYYTIT FTVNFPHKDD VCYFAYHYPY
860 870 880 890 900
TYSTLQMHLQ KLESAHNPQQ IYFRKDVLCE TLSGNSCPLV TITAMPESNY
910 920 930 940 950
YEHICHFRNR PYVFLSARVH PGETNASWVM KGTLEYLMSN NPTAQSLRES
960 970 980 990 1000
YIFKIVPMLN PDGVINGNHR CSLSGEDLNR QWQSPSPDLH PTIYHAKGLL
1010 1020 1030 1040 1050
QYLAAVKRLP LVYCDYHGHS RKKNVFMYGC SIKETVWHTN DNATSCDVVE
1060 1070 1080 1090 1100
DTGYRTLPKI LSHIAPAFCM SSCSFVVEKS KESTARVVVW REIGVQRSYT
1110 1120 1130 1140 1150
MESTLCGCDQ GKYKGLQIGT RELEEMGAKF CVGLLRLKRL TSPLEYNLPS
1160 1170 1180 1190 1200
SLLDFENDLI ESSCKVTSPT TYVLDEDEPR FLEEVDYSAE SNDELDIELA
1210 1220
ENVGDYEPSA QEEVLSDSEL SRTYLP
Length:1,226
Mass (Da):138,448
Last modified:October 23, 2007 - v3
Checksum:iA6D598D11D2BD1F8
GO
Isoform 2 (identifier: Q9UPW5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     304-343: Missing.

Show »
Length:1,186
Mass (Da):133,864
Checksum:iD5361B66224C04BE
GO
Isoform 3 (identifier: Q9UPW5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MSKLKVIPEKS → MRTGSAASSAAAAAAAAAASASPATGVCMKTPGGGRRGIRRDPGAEPGAAALRGPRQRPILSR
     304-343: Missing.

Note: No experimental confirmation available.

Show »
Length:1,238
Mass (Da):138,647
Checksum:i8119980498634DDF
GO

Sequence cautioni

The sequence BAA82987.2 differs from that shown. Reason: Frameshift at position 10. Curated
The sequence BAB14100.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14505.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG61460.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH56222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW62697.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741Q → R in BAA91749. (PubMed:14702039)Curated
Sequence conflicti398 – 3992DI → KK in CAH56222. (PubMed:17974005)Curated
Sequence conflicti464 – 4641E → G in BAA91749. (PubMed:14702039)Curated
Sequence conflicti495 – 4951M → V in BAB14505. (PubMed:14702039)Curated
Sequence conflicti574 – 5741M → V in BAB14100. (PubMed:14702039)Curated
Sequence conflicti598 – 5981E → G in BAA91749. (PubMed:14702039)Curated
Sequence conflicti712 – 7121F → I in CAH56222. (PubMed:17974005)Curated
Sequence conflicti756 – 7561M → T in BAB14100. (PubMed:14702039)Curated
Sequence conflicti812 – 8121S → P in BAB14505. (PubMed:14702039)Curated
Sequence conflicti830 – 8301T → A in CAH56158. (PubMed:17974005)Curated
Sequence conflicti909 – 9091N → D in BAB14505. (PubMed:14702039)Curated
Sequence conflicti975 – 9751G → R in BAG58598. (PubMed:14702039)Curated
Sequence conflicti1054 – 10541Y → F in BAB14505. (PubMed:14702039)Curated
Sequence conflicti1153 – 11531L → P in CAH56158. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti423 – 4231E → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036884

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111MSKLKVIPEKS → MRTGSAASSAAAAAAAAAAS ASPATGVCMKTPGGGRRGIR RDPGAEPGAAALRGPRQRPI LSR in isoform 3. 1 PublicationVSP_040422Add
BLAST
Alternative sequencei304 – 34340Missing in isoform 2 and isoform 3. 2 PublicationsVSP_029044Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028958 mRNA. Translation: BAA82987.2. Frameshift.
AK001544 mRNA. Translation: BAA91749.1.
AK022562 mRNA. Translation: BAB14100.1. Different initiation.
AK023280 mRNA. Translation: BAB14505.1. Different initiation.
AK295774 mRNA. Translation: BAG58598.1.
AK299506 mRNA. Translation: BAG61460.1. Different initiation.
AL157882, AL451131 Genomic DNA. Translation: CAH71213.1.
AL157882, AL451131 Genomic DNA. Translation: CAH71214.1.
AL451131, AL157882 Genomic DNA. Translation: CAH72317.1.
AL451131, AL157882 Genomic DNA. Translation: CAH72318.1.
CH471089 Genomic DNA. Translation: EAW62694.1.
CH471089 Genomic DNA. Translation: EAW62698.1.
CH471089 Genomic DNA. Translation: EAW62697.1. Sequence problems.
BC060815 mRNA. Translation: AAH60815.1.
BX648366 mRNA. Translation: CAH56158.1.
AL833359 mRNA. Translation: CAH56222.1. Different initiation.
CCDSiCCDS6672.1. [Q9UPW5-2]
RefSeqiNP_001273644.1. NM_001286715.1.
NP_001273646.1. NM_001286717.1. [Q9UPW5-3]
NP_056054.2. NM_015239.2. [Q9UPW5-2]
XP_005251904.1. XM_005251847.2. [Q9UPW5-1]
XP_005251905.1. XM_005251848.2. [Q9UPW5-1]
UniGeneiHs.719980.

Genome annotation databases

EnsembliENST00000357081; ENSP00000349592; ENSG00000135049. [Q9UPW5-1]
ENST00000376083; ENSP00000365251; ENSG00000135049. [Q9UPW5-2]
GeneIDi23287.
KEGGihsa:23287.
UCSCiuc004aod.4. human. [Q9UPW5-1]
uc010mqc.3. human. [Q9UPW5-2]
uc011lte.2. human. [Q9UPW5-3]

Polymorphism databases

DMDMi160019039.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028958 mRNA. Translation: BAA82987.2 . Frameshift.
AK001544 mRNA. Translation: BAA91749.1 .
AK022562 mRNA. Translation: BAB14100.1 . Different initiation.
AK023280 mRNA. Translation: BAB14505.1 . Different initiation.
AK295774 mRNA. Translation: BAG58598.1 .
AK299506 mRNA. Translation: BAG61460.1 . Different initiation.
AL157882 , AL451131 Genomic DNA. Translation: CAH71213.1 .
AL157882 , AL451131 Genomic DNA. Translation: CAH71214.1 .
AL451131 , AL157882 Genomic DNA. Translation: CAH72317.1 .
AL451131 , AL157882 Genomic DNA. Translation: CAH72318.1 .
CH471089 Genomic DNA. Translation: EAW62694.1 .
CH471089 Genomic DNA. Translation: EAW62698.1 .
CH471089 Genomic DNA. Translation: EAW62697.1 . Sequence problems.
BC060815 mRNA. Translation: AAH60815.1 .
BX648366 mRNA. Translation: CAH56158.1 .
AL833359 mRNA. Translation: CAH56222.1 . Different initiation.
CCDSi CCDS6672.1. [Q9UPW5-2 ]
RefSeqi NP_001273644.1. NM_001286715.1.
NP_001273646.1. NM_001286717.1. [Q9UPW5-3 ]
NP_056054.2. NM_015239.2. [Q9UPW5-2 ]
XP_005251904.1. XM_005251847.2. [Q9UPW5-1 ]
XP_005251905.1. XM_005251848.2. [Q9UPW5-1 ]
UniGenei Hs.719980.

3D structure databases

ProteinModelPortali Q9UPW5.
SMRi Q9UPW5. Positions 710-1032.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116885. 11 interactions.
IntActi Q9UPW5. 9 interactions.
MINTi MINT-2858492.
STRINGi 9606.ENSP00000338512.

Protein family/group databases

MEROPSi M14.028.

PTM databases

PhosphoSitei Q9UPW5.

Polymorphism databases

DMDMi 160019039.

Proteomic databases

MaxQBi Q9UPW5.
PaxDbi Q9UPW5.
PRIDEi Q9UPW5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357081 ; ENSP00000349592 ; ENSG00000135049 . [Q9UPW5-1 ]
ENST00000376083 ; ENSP00000365251 ; ENSG00000135049 . [Q9UPW5-2 ]
GeneIDi 23287.
KEGGi hsa:23287.
UCSCi uc004aod.4. human. [Q9UPW5-1 ]
uc010mqc.3. human. [Q9UPW5-2 ]
uc011lte.2. human. [Q9UPW5-3 ]

Organism-specific databases

CTDi 23287.
GeneCardsi GC09M088161.
HGNCi HGNC:17258. AGTPBP1.
HPAi HPA057208.
MIMi 606830. gene.
neXtProti NX_Q9UPW5.
PharmGKBi PA24630.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2866.
GeneTreei ENSGT00550000074405.
HOVERGENi HBG107587.
InParanoidi Q9UPW5.
OMAi DVLCETL.
OrthoDBi EOG712TVD.
PhylomeDBi Q9UPW5.
TreeFami TF313794.

Miscellaneous databases

ChiTaRSi AGTPBP1. human.
GenomeRNAii 23287.
NextBioi 45098.
PROi Q9UPW5.
SOURCEi Search...

Gene expression databases

Bgeei Q9UPW5.
CleanExi HS_AGTPBP1.
ExpressionAtlasi Q9UPW5. baseline and differential.
Genevestigatori Q9UPW5.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000834. Peptidase_M14.
[Graphical view ]
Pfami PF00246. Peptidase_M14. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  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 2 AND 3).
    Tissue: Brain and Hippocampus.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 396-1226.
    Tissue: Esophageal carcinoma and Lymph node.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Functional segregation and emerging role of cilia-related cytosolic carboxypeptidases (CCPs)."
    Rodriguez de la Vega Otazo M., Lorenzo J., Tort O., Aviles F.X., Bautista J.M.
    FASEB J. 27:424-431(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-423.

Entry informationi

Entry nameiCBPC1_HUMAN
AccessioniPrimary (citable) accession number: Q9UPW5
Secondary accession number(s): B4DIT6
, B4DRZ8, Q5VV80, Q63HM7, Q658P5, Q6P9D6, Q9H8U6, Q9H9W8, Q9NVK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: November 26, 2014
This is version 102 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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