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P11983 (TCPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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:
T-complex protein 1 subunit alpha
Short name=TCP-1-alpha
Alternative name(s):
CCT-alpha
Tailless complex polypeptide 1A
Short name=TCP-1-A
Tailless complex polypeptide 1B
Short name=TCP-1-B
Gene names
Name:Tcp1
Synonyms:Cct1, Ccta
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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 By similarity.

Subcellular location

Cytoplasm. Cytoplasm › cytoskeleton › centrosome By similarity.

Sequence similarities

Belongs to the TCP-1 chaperonin family.

Sequence caution

The sequence AAA40337.1 differs from that shown. Reason: Frameshift at position 528.

The sequence AAA40338.1 differs from that shown. Reason: Frameshift at position 528.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11983-1)

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: P11983-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.
     50-50: G → M
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556T-complex protein 1 subunit alpha
PRO_0000128305

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue1811Phosphotyrosine By similarity
Modified residue1821Phosphothreonine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue4001N6-acetyllysine By similarity
Modified residue5441Phosphoserine Ref.10
Modified residue5511Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 4949Missing in isoform 2.
VSP_024734
Alternative sequence501G → M in isoform 2.
VSP_024735

Experimental info

Sequence conflict171V → I in AAA40337. Ref.1
Sequence conflict171V → I in BAA14356. Ref.3
Sequence conflict171V → I in BAE30084. Ref.5
Sequence conflict361F → L in AAA40337. Ref.1
Sequence conflict361F → L in BAA14356. Ref.3
Sequence conflict1401T → A in AAA40337. Ref.1
Sequence conflict1401T → A in BAA14356. Ref.3
Sequence conflict149 – 1513INA → TNT in AAA40337. Ref.1
Sequence conflict149 – 1513INA → TNT in BAA14356. Ref.3
Sequence conflict1511A → T in AAA40338. Ref.1
Sequence conflict1771L → H in BAE31381. Ref.5
Sequence conflict1921V → I in AAA40337. Ref.1
Sequence conflict1921V → I in BAA14356. Ref.3
Sequence conflict2171N → D in BAE39599. Ref.5
Sequence conflict2591K → E in BAE31381. Ref.5
Sequence conflict2961Y → C in AAA40337. Ref.1
Sequence conflict2961Y → C in BAA14356. Ref.3
Sequence conflict3181H → C in AAA40337. Ref.1
Sequence conflict3181H → C in BAA14356. Ref.3
Sequence conflict3261S → T in AAA40337. Ref.1
Sequence conflict3261S → T in BAA14356. Ref.3
Sequence conflict3781R → Q in BAE30084. Ref.5
Sequence conflict4021V → I in BAE30407. Ref.5
Sequence conflict4021V → I in BAE31988. Ref.5
Sequence conflict4051L → S in AAA40337. Ref.1
Sequence conflict4051L → S in BAA14356. Ref.3
Sequence conflict4291S → N in AAA40338. Ref.1
Sequence conflict4391A → V in BAE31381. Ref.5
Sequence conflict4541V → M in BAE39052. Ref.5
Sequence conflict4941K → N in BAE30407. Ref.5
Sequence conflict5371S → C in AAA40337. Ref.1
Sequence conflict5371S → C in BAA14356. Ref.3

Sequences

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

Last modified October 1, 1996. Version 3.
Checksum: 48F2387BE0F909A4

FASTA55660,449
        10         20         30         40         50         60 
MEGPLSVFGD RSTGEAVRSQ NVMAAASIAN IVKSSFGPVG LDKMLVDDIG DVTITNDGAT 

        70         80         90        100        110        120 
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG 

       130        140        150        160        170        180 
YRLACKEAVR YINENLIINT DELGRDCLIN AAKTSMSSKI IGINGDYFAN MVVDAVLAVK 

       190        200        210        220        230        240 
YTDARGQPRY PVNSVNILKA HGRSQIESML INGYALNCVV GSQGMPKRIV NAKIACLDFS 

       250        260        270        280        290        300 
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMYLKYF 

       310        320        330        340        350        360 
VEAGAMAVRR VLKRDLKHVA KASGASILST LANLEGEETF EVTMLGQAEE VVQERICDDE 

       370        380        390        400        410        420 
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLELKSVVP GGGAVEAALS 

       430        440        450        460        470        480 
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER 

       490        500        510        520        530        540 
KNLKWIGLDL VHGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD 

       550 
KHGSYENAVH SGALDD

« Hide

Isoform 2 [UniParc].

Checksum: 1E169BE37404520B
Show »

FASTA50755,459

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1."
Willison K.R., Dudley K., Potter J.
Cell 44:727-738(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"Nucleotide and amino-acid sequence of human testis-derived TCP1."
Kirchhoff C., Willison K.R.
Nucleic Acids Res. 18:4247-4247(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Nucleotide sequence of mouse Tcp-1a cDNA."
Kubota H., Morita T., Nagata T., Takemoto Y., Nozaki M., Gachelin G., Matsushiro A.
Gene 105:269-273(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Structure and expression of the gene encoding mouse T-complex polypeptide (Tcp-1)."
Kubota H., Willison K., Ashworth A., Nozaki M., Miyamoto H., Yamamoto H., Matsushiro A., Morita T.
Gene 120:207-215(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Bone marrow and Placenta.
[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 1).
Strain: FVB/N.
Tissue: Mammary gland.
[7]Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-11; 34-43; 64-73; 190-199; 234-243; 371-378; 434-466 AND 485-496, ACETYLATION AT MET-1, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
[8]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-63; 112-122; 131-145; 190-199; 234-243; 248-259; 299-309; 434-443; 469-480; 500-510 AND 516-526, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[9]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 485-496.
Tissue: Brain.
[10]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M20130 mRNA. Translation: AAA40337.1. Frameshift.
M12899 mRNA. Translation: AAA40338.1. Frameshift.
D90344 mRNA. Translation: BAA14356.1.
D10606 Genomic DNA. Translation: BAA01461.1.
S46763 Genomic DNA. Translation: AAB23855.1.
AK149611 mRNA. Translation: BAE28989.1.
AK149755 mRNA. Translation: BAE29063.1.
AK151068 mRNA. Translation: BAE30084.1.
AK151445 mRNA. Translation: BAE30407.1.
AK152641 mRNA. Translation: BAE31381.1.
AK153430 mRNA. Translation: BAE31988.1.
AK165665 mRNA. Translation: BAE38327.1.
AK166828 mRNA. Translation: BAE39052.1.
AK166966 mRNA. Translation: BAE39149.1.
AK167529 mRNA. Translation: BAE39599.1.
BC003809 mRNA. Translation: AAH03809.1.
IPIIPI00459493.
IPI00845611.
PIRB24059.
JC1443.
RefSeqNP_038714.2. NM_013686.3.
UniGeneMm.229342.

3D structure databases

ProteinModelPortalP11983.
SMRP11983. Positions 9-542.
ModBaseSearch...

Protein-protein interaction databases

IntActP11983. 7 interactions.

PTM databases

PhosphoSiteP11983.

2D gel databases

REPRODUCTION-2DPAGEIPI00459493.
P11983.

Proteomic databases

PaxDbP11983.
PRIDEP11983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089024; ENSMUSP00000086418; ENSMUSG00000068039.
ENSMUST00000151287; ENSMUSP00000116108; ENSMUSG00000068039.
GeneID21454.
KEGGmmu:21454.

Organism-specific databases

CTD6950.
MGIMGI:98535. Tcp1.

Phylogenomic databases

eggNOGCOG0459.
GeneTreeENSGT00550000074878.
HOVERGENHBG001052.
InParanoidP11983.
KOK09493.
OMAKGYALNC.

Gene expression databases

ArrayExpressP11983.
BgeeP11983.
CleanExMM_TCP1.
GenevestigatorP11983.
GermOnlineENSMUSG00000068039. Mus musculus.

Family and domain databases

InterProIPR012715. Chap_CCT_alpha.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
[Graphical view]
PANTHERPTHR11353. PTHR11353. 1 hit.
PTHR11353:SF20. PTHR11353:SF20. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00304. TCOMPLEXTCP1.
SUPFAMSSF48592. GroEL-ATPase. 1 hit.
TIGRFAMsTIGR02340. chap_CCT_alpha. 1 hit.
PROSITEPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTCP1. mouse.
NextBio300820.
SOURCESearch...

Entry information

Entry nameTCPA_MOUSE
AccessionPrimary (citable) accession number: P11983
Secondary accession number(s): P11984 expand/collapse secondary AC list , Q3TJ96, Q3TKU1, Q3U5T8, Q3U7I8, Q3UAA8, Q3UB80, Q3UE48
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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