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P78371

- TCPB_HUMAN

UniProt

P78371 - TCPB_HUMAN

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Protein

T-complex protein 1 subunit beta

Gene

CCT2

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

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. binding of sperm to zona pellucida Source: Ensembl
  3. cellular protein metabolic process Source: Reactome
  4. chaperone-mediated protein complex assembly Source: MGI
  5. protein folding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_17050. Folding of actin by CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit beta
Short name:
TCP-1-beta
Alternative name(s):
CCT-beta
Gene namesi
Name:CCT2
Synonyms:99D8.1, CCTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1615. CCT2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. chaperonin-containing T-complex Source: Ensembl
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. microtubule Source: UniProtKB
  6. zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed8 Publications
Chaini2 – 535534T-complex protein 1 subunit betaPRO_0000128316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine7 Publications
Modified residuei3 – 31Phosphoserine2 Publications
Modified residuei13 – 131N6-acetyllysine1 Publication
Modified residuei154 – 1541N6-acetyllysine1 Publication
Modified residuei181 – 1811N6-acetyllysine1 Publication
Modified residuei260 – 2601Phosphoserine1 Publication
Modified residuei261 – 2611Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP78371.
PaxDbiP78371.
PeptideAtlasiP78371.
PRIDEiP78371.

2D gel databases

OGPiP78371.
REPRODUCTION-2DPAGEIPI00297779.
SWISS-2DPAGEP78371.
UCD-2DPAGEP78371.

PTM databases

PhosphoSiteiP78371.

Expressioni

Gene expression databases

BgeeiP78371.
CleanExiHS_CCT2.
ExpressionAtlasiP78371. baseline and differential.
GenevestigatoriP78371.

Organism-specific databases

HPAiCAB009850.
HPA003197.
HPA003198.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BBS7Q8IWZ63EBI-357407,EBI-1806001

Protein-protein interaction databases

BioGridi115827. 133 interactions.
DIPiDIP-38123N.
IntActiP78371. 52 interactions.
MINTiMINT-8213815.
STRINGi9606.ENSP00000299300.

Structurei

3D structure databases

ProteinModelPortaliP78371.
SMRiP78371. Positions 14-526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
HOVERGENiHBG001052.
InParanoidiP78371.
KOiK09494.
OMAiESGDNIR.
OrthoDBiEOG7Q5HD3.
PhylomeDBiP78371.
TreeFamiTF105645.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012716. Chap_CCT_beta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02341. chap_CCT_beta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 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: P78371-1) [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
MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK
60 70 80 90 100
ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT
110 120 130 140 150
SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS
160 170 180 190 200
DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH
210 220 230 240 250
IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK
260 270 280 290 300
IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP
310 320 330 340 350
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE
360 370 380 390 400
EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT
410 420 430 440 450
VKDSRTVYGG GCSEMLMAHA VTQLANRTPG KEAVAMESYA KALRMLPTII
460 470 480 490 500
ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM REGTIGDMAI LGITESFQVK
510 520 530
RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
Length:535
Mass (Da):57,488
Last modified:January 23, 2007 - v4
Checksum:i57F9E1720D84A31F
GO
Isoform 2 (identifier: P78371-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: No experimental confirmation available.

Show »
Length:488
Mass (Da):52,718
Checksum:i5947D87827A365E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511I → T in BAH11729. (PubMed:14702039)Curated
Sequence conflicti126 – 1261I → T in CAG33352. 1 PublicationCurated
Sequence conflicti354 – 3541I → T in BAF83456. (PubMed:14702039)Curated
Sequence conflicti438 – 4381S → P in BAH13640. (PubMed:14702039)Curated
Sequence conflicti444 – 4441R → K in BAG70037. (PubMed:19054851)Curated
Sequence conflicti444 – 4441R → K in BAG70160. (PubMed:19054851)Curated
Sequence conflicti504 – 5041L → P in CAG33352. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2. 1 PublicationVSP_042648Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026293 mRNA. Translation: AAC96012.1.
AF026166 mRNA. Translation: AAC98906.1.
BT019966 mRNA. Translation: AAV38769.1.
AK290767 mRNA. Translation: BAF83456.1.
AK294307 mRNA. Translation: BAH11729.1.
AK302157 mRNA. Translation: BAH13640.1.
AK316397 mRNA. Translation: BAH14768.1.
AK316408 mRNA. Translation: BAH14779.1.
CR457071 mRNA. Translation: CAG33352.1.
AB451223 mRNA. Translation: BAG70037.1.
AB451346 mRNA. Translation: BAG70160.1.
AC018921 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97230.1.
BC113514 mRNA. Translation: AAI13515.1.
BC113516 mRNA. Translation: AAI13517.1.
U91327 Genomic DNA. Translation: AAB67249.1.
CCDSiCCDS55843.1. [P78371-2]
CCDS8991.1. [P78371-1]
RefSeqiNP_001185771.1. NM_001198842.1. [P78371-2]
NP_006422.1. NM_006431.2. [P78371-1]
UniGeneiHs.189772.

Genome annotation databases

EnsembliENST00000299300; ENSP00000299300; ENSG00000166226. [P78371-1]
ENST00000543146; ENSP00000445471; ENSG00000166226. [P78371-2]
GeneIDi10576.
KEGGihsa:10576.
UCSCiuc001svb.1. human. [P78371-1]

Polymorphism databases

DMDMi6094436.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026293 mRNA. Translation: AAC96012.1 .
AF026166 mRNA. Translation: AAC98906.1 .
BT019966 mRNA. Translation: AAV38769.1 .
AK290767 mRNA. Translation: BAF83456.1 .
AK294307 mRNA. Translation: BAH11729.1 .
AK302157 mRNA. Translation: BAH13640.1 .
AK316397 mRNA. Translation: BAH14768.1 .
AK316408 mRNA. Translation: BAH14779.1 .
CR457071 mRNA. Translation: CAG33352.1 .
AB451223 mRNA. Translation: BAG70037.1 .
AB451346 mRNA. Translation: BAG70160.1 .
AC018921 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97230.1 .
BC113514 mRNA. Translation: AAI13515.1 .
BC113516 mRNA. Translation: AAI13517.1 .
U91327 Genomic DNA. Translation: AAB67249.1 .
CCDSi CCDS55843.1. [P78371-2 ]
CCDS8991.1. [P78371-1 ]
RefSeqi NP_001185771.1. NM_001198842.1. [P78371-2 ]
NP_006422.1. NM_006431.2. [P78371-1 ]
UniGenei Hs.189772.

3D structure databases

ProteinModelPortali P78371.
SMRi P78371. Positions 14-526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115827. 133 interactions.
DIPi DIP-38123N.
IntActi P78371. 52 interactions.
MINTi MINT-8213815.
STRINGi 9606.ENSP00000299300.

PTM databases

PhosphoSitei P78371.

Polymorphism databases

DMDMi 6094436.

2D gel databases

OGPi P78371.
REPRODUCTION-2DPAGE IPI00297779.
SWISS-2DPAGE P78371.
UCD-2DPAGE P78371.

Proteomic databases

MaxQBi P78371.
PaxDbi P78371.
PeptideAtlasi P78371.
PRIDEi P78371.

Protocols and materials databases

DNASUi 10576.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299300 ; ENSP00000299300 ; ENSG00000166226 . [P78371-1 ]
ENST00000543146 ; ENSP00000445471 ; ENSG00000166226 . [P78371-2 ]
GeneIDi 10576.
KEGGi hsa:10576.
UCSCi uc001svb.1. human. [P78371-1 ]

Organism-specific databases

CTDi 10576.
GeneCardsi GC12P069979.
HGNCi HGNC:1615. CCT2.
HPAi CAB009850.
HPA003197.
HPA003198.
MIMi 605139. gene.
neXtProti NX_P78371.
PharmGKBi PA26179.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0459.
GeneTreei ENSGT00550000074930.
HOGENOMi HOG000226736.
HOVERGENi HBG001052.
InParanoidi P78371.
KOi K09494.
OMAi ESGDNIR.
OrthoDBi EOG7Q5HD3.
PhylomeDBi P78371.
TreeFami TF105645.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_17050. Folding of actin by CCT/TriC.

Miscellaneous databases

ChiTaRSi CCT2. human.
GeneWikii CCT2_(gene).
GenomeRNAii 10576.
NextBioi 40141.
PROi P78371.
SOURCEi Search...

Gene expression databases

Bgeei P78371.
CleanExi HS_CCT2.
ExpressionAtlasi P78371. baseline and differential.
Genevestigatori P78371.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProi IPR012716. Chap_CCT_beta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00304. TCOMPLEXTCP1.
SUPFAMi SSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02341. chap_CCT_beta. 1 hit.
PROSITEi PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT."
    Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.
    Mol. Cell. Biol. 18:7584-7589(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Isolation and expression of a human novel cDNA homologous to the beta subunit of mouse CCT (chaperonin-containing TCP-1)."
    Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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).
    Tissue: Amygdala and Testis.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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).
  7. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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.
  10. Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R., Fuhrmann J., Kim U.J., Kerlavage A.R., Venter J.C.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
  11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
    Tissue: Platelet.
  12. Bienvenut W.V., Potts A., Quadroni M.
    Submitted (MAY-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  13. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 26-40; 58-72; 83-131; 139-154; 157-170; 182-189; 192-203; 205-222; 237-250; 285-342; 348-354; 359-402; 406-427; 432-441; 445-466; 482-500 AND 502-516, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  14. "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
    Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
    J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACRG.
  15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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; LYS-13; LYS-154 AND LYS-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly."
    Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C.
    Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-260 AND THR-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPB_HUMAN
AccessioniPrimary (citable) accession number: P78371
Secondary accession number(s): A8K402
, B5BTY7, B7Z243, B7Z7K4, B7ZAT2, Q14D36, Q6IAT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 142 of the entry and version 4 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3