TCP1/YDR212W Protein Information

Standard Name	Tcp1p
Systematic Name	Ydr212wp
Alias	Cct1p
ORF Classification	Verified
Description	Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein (1, 2, 3, 4, 5)
Name Description	Tailless Complex Polypeptide

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	559
Molecular Weight (Da)	60,480
Isoelectric Point (pI)	6.45

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Tcp1p (InterPro)
Physical Interactions	There are 58 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000136AF1 \| P12612 MIPS: YDR212W NCBI: 1122345 \| 1204153 \| 172880 \| 1729867 \| 339717516 \| 339717524 \| 388326563 \| 388326571 \| 6320418 \| NP_010498.1 GenBank/EMBL/DDBJ: DAA12056.1 \| M21160 \| Z68194 \| Z68195

Amino Acid Sequence (or in FASTA format)
1 MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD 51 KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQQ DREIGDGTTS 101 VVIIASELLK RANELVKNKI HPTTIITGFR VALREAIRFI NEVLSTSVDT 151 LGKETLINIA KTSMSSKIIG ADSDFFSNMV VDALLAVKTQ NSKGEIKYPV 201 KAVNVLKAHG KSATESLLVP GYALNCTVAS QAMPKRIAGG NVKIACLDLN 251 LQKARMAMGV QINIDDPEQL EQIRKREAGI VLERVKKIID AGAQVVLTTK 301 GIDDLCLKEF VEAKIMGVRR CKKEDLRRIA RATGATLVSS MSNLEGEETF 351 ESSYLGLCDE VVQAKFSDDE CILIKGTSKH SSSSIILRGA NDYSLDEMER 401 SLHDSLSVVK RTLESGNVVP GGGCVEAALN IYLDNFATTV GSREQLAIAE 451 FAAALLIIPK TLAVNAAKDS SELVAKLRSY HAASQMAKPE DVKRRSYRNY 501 GLDLIRGKIV DEIHAGVLEP TISKVKSLKS ALEACVAILR IDTMITVDPE 551 PPKEDPHDH*

Amino Acid Sequence (or in FASTA format)

       1  MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD
      51  KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQQ DREIGDGTTS
     101  VVIIASELLK RANELVKNKI HPTTIITGFR VALREAIRFI NEVLSTSVDT
     151  LGKETLINIA KTSMSSKIIG ADSDFFSNMV VDALLAVKTQ NSKGEIKYPV
     201  KAVNVLKAHG KSATESLLVP GYALNCTVAS QAMPKRIAGG NVKIACLDLN
     251  LQKARMAMGV QINIDDPEQL EQIRKREAGI VLERVKKIID AGAQVVLTTK
     301  GIDDLCLKEF VEAKIMGVRR CKKEDLRRIA RATGATLVSS MSNLEGEETF
     351  ESSYLGLCDE VVQAKFSDDE CILIKGTSKH SSSSIILRGA NDYSLDEMER
     401  SLHDSLSVVK RTLESGNVVP GGGCVEAALN IYLDNFATTV GSREQLAIAE
     451  FAAALLIIPK TLAVNAAKDS SELVAKLRSY HAASQMAKPE DVKRRSYRNY
     501  GLDLIRGKIV DEIHAGVLEP TISKVKSLKS ALEACVAILR IDTMITVDPE
     551  PPKEDPHDH*

external links for Tcp1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Tcp1p

1)	Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40
2)	Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80
3)	Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84
4)	Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40
5)	Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62