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P49368

- TCPG_HUMAN

UniProt

P49368 - TCPG_HUMAN

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Protein

T-complex protein 1 subunit gamma

Gene

CCT3

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. poly(A) RNA binding Source: UniProtKB
  3. unfolded protein binding Source: ProtInc

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. protein folding Source: Reactome
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 gamma
Short name:
TCP-1-gamma
Alternative name(s):
CCT-gamma
hTRiC5
Gene namesi
Name:CCT3
Synonyms:CCTG, TRIC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1616. CCT3.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. chaperonin-containing T-complex Source: Ensembl
  3. cytoplasm Source: HPA
  4. cytoskeleton Source: ProtInc
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. microtubule Source: UniProtKB
  8. plasma membrane Source: HPA
  9. zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545T-complex protein 1 subunit gammaPRO_0000128321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei222 – 2221N6-acetyllysine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication
Modified residuei252 – 2521Phosphoserine1 Publication
Disulfide bondi366 ↔ 372By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP49368.
PaxDbiP49368.
PRIDEiP49368.

2D gel databases

DOSAC-COBS-2DPAGEP49368.
OGPiP49368.
SWISS-2DPAGEP49368.

PTM databases

PhosphoSiteiP49368.

Expressioni

Gene expression databases

BgeeiP49368.
CleanExiHS_CCT3.
ExpressionAtlasiP49368. baseline and differential.
GenevestigatoriP49368.

Organism-specific databases

HPAiHPA006543.

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. Interacts with DYX1C1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RAF1P040493EBI-356673,EBI-365996

Protein-protein interaction databases

BioGridi113054. 128 interactions.
DIPiDIP-32970N.
IntActiP49368. 63 interactions.
MINTiMINT-260598.
STRINGi9606.ENSP00000357244.

Structurei

3D structure databases

ProteinModelPortaliP49368.
SMRiP49368. Positions 7-526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00570000079224.
HOGENOMiHOG000226732.
HOVERGENiHBG104982.
InParanoidiP49368.
KOiK09495.
OMAiTEMAVSH.
OrthoDBiEOG7DJSKS.
PhylomeDBiP49368.
TreeFamiTF105649.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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.
PTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 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.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49368-1) [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
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML
60 70 80 90 100
LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII
110 120 130 140 150
LAGEMLSVAE HFLEQQMHPT VVISAYRKAL DDMISTLKKI SIPVDISDSD
160 170 180 190 200
MMLNIINSSI TTKAISRWSS LACNIALDAV KMVQFEENGR KEIDIKKYAR
210 220 230 240 250
VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL LDSSLEYKKG
260 270 280 290 300
ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA
310 320 330 340 350
QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL
360 370 380 390 400
EIKKIGDEYF TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN
410 420 430 440 450
VLLDPQLVPG GGASEMAVAH ALTEKSKAMT GVEQWPYRAV AQALEVIPRT
460 470 480 490 500
LIQNCGASTI RLLTSLRAKH TQENCETWGV NGETGTLVDM KELGIWEPLA
510 520 530 540
VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP DAGQE
Length:545
Mass (Da):60,534
Last modified:May 24, 2005 - v4
Checksum:i0A528762EF24F36B
GO
Isoform 2 (identifier: P49368-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-69: Missing.

Note: No experimental confirmation available.

Show »
Length:507
Mass (Da):56,431
Checksum:i7A7F387DF6A76FFE
GO

Sequence cautioni

The sequence AAH08019.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511E → G in CAA52808. (PubMed:8573069)Curated
Sequence conflicti345 – 3451T → A in AAC50068. (PubMed:8001976)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911L → F.
Corresponds to variant rs2230194 [ dbSNP | Ensembl ].
VAR_052265

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 6938Missing in isoform 2. 1 PublicationVSP_042026Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK293477 mRNA. Translation: BAG56968.1.
AL833197 mRNA. Translation: CAI46192.1.
AL589685 Genomic DNA. Translation: CAI14167.1.
BC006501 mRNA. Translation: AAH06501.3.
BC008019 mRNA. Translation: AAH08019.1. Different initiation.
X74801 mRNA. Translation: CAA52808.1.
U17104 mRNA. Translation: AAC50068.1.
CCDSiCCDS1140.2. [P49368-1]
CCDS30888.1. [P49368-2]
PIRiS61529. A38983.
RefSeqiNP_001008800.1. NM_001008800.2. [P49368-2]
NP_005989.3. NM_005998.4. [P49368-1]
UniGeneiHs.491494.

Genome annotation databases

EnsembliENST00000295688; ENSP00000295688; ENSG00000163468. [P49368-1]
ENST00000368259; ENSP00000357242; ENSG00000163468. [P49368-2]
GeneIDi7203.
KEGGihsa:7203.
UCSCiuc001fol.2. human. [P49368-1]
uc001fon.2. human. [P49368-2]

Polymorphism databases

DMDMi66774185.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK293477 mRNA. Translation: BAG56968.1 .
AL833197 mRNA. Translation: CAI46192.1 .
AL589685 Genomic DNA. Translation: CAI14167.1 .
BC006501 mRNA. Translation: AAH06501.3 .
BC008019 mRNA. Translation: AAH08019.1 . Different initiation.
X74801 mRNA. Translation: CAA52808.1 .
U17104 mRNA. Translation: AAC50068.1 .
CCDSi CCDS1140.2. [P49368-1 ]
CCDS30888.1. [P49368-2 ]
PIRi S61529. A38983.
RefSeqi NP_001008800.1. NM_001008800.2. [P49368-2 ]
NP_005989.3. NM_005998.4. [P49368-1 ]
UniGenei Hs.491494.

3D structure databases

ProteinModelPortali P49368.
SMRi P49368. Positions 7-526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113054. 128 interactions.
DIPi DIP-32970N.
IntActi P49368. 63 interactions.
MINTi MINT-260598.
STRINGi 9606.ENSP00000357244.

PTM databases

PhosphoSitei P49368.

Polymorphism databases

DMDMi 66774185.

2D gel databases

DOSAC-COBS-2DPAGE P49368.
OGPi P49368.
SWISS-2DPAGE P49368.

Proteomic databases

MaxQBi P49368.
PaxDbi P49368.
PRIDEi P49368.

Protocols and materials databases

DNASUi 7203.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295688 ; ENSP00000295688 ; ENSG00000163468 . [P49368-1 ]
ENST00000368259 ; ENSP00000357242 ; ENSG00000163468 . [P49368-2 ]
GeneIDi 7203.
KEGGi hsa:7203.
UCSCi uc001fol.2. human. [P49368-1 ]
uc001fon.2. human. [P49368-2 ]

Organism-specific databases

CTDi 7203.
GeneCardsi GC01M156278.
HGNCi HGNC:1616. CCT3.
HPAi HPA006543.
MIMi 600114. gene.
neXtProti NX_P49368.
PharmGKBi PA26180.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0459.
GeneTreei ENSGT00570000079224.
HOGENOMi HOG000226732.
HOVERGENi HBG104982.
InParanoidi P49368.
KOi K09495.
OMAi TEMAVSH.
OrthoDBi EOG7DJSKS.
PhylomeDBi P49368.
TreeFami TF105649.

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 CCT3. human.
GeneWikii CCT3.
GenomeRNAii 7203.
NextBioi 28226.
PROi P49368.
SOURCEi Search...

Gene expression databases

Bgeei P49368.
CleanExi HS_CCT3.
ExpressionAtlasi P49368. baseline and differential.
Genevestigatori P49368.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProi IPR012719. Chap_CCT_gamma.
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.
PTHR11353:SF63. PTHR11353:SF63. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00304. TCOMPLEXTCP1.
SUPFAMi SSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02344. chap_CCT_gamma. 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. "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 2).
    Tissue: Cerebellum.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph node.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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] (ISOFORM 1).
    Tissue: Lung.
  5. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-15; 32-38; 49-85; 129-138; 182-191; 238-248; 295-306; 382-389; 428-449 AND 508-528, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  6. "Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma."
    Walkley N.A., Demaine A.G., Malik A.N.
    Biochem. J. 313:381-389(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-545.
    Tissue: Kidney.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 204-216; 331-353 AND 508-518, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization."
    Sevigny G., Joly E., Bibor-Hardy V., Lemieux N.
    Genomics 22:634-636(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 345-544.
  9. "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.
  10. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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 LYS-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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, IDENTIFICATION IN BBS/CCT COMPLEX.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPG_HUMAN
AccessioniPrimary (citable) accession number: P49368
Secondary accession number(s): A6NE14, Q5SZY1, Q9BR64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 24, 2005
Last modified: October 29, 2014
This is version 153 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 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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