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TCP1

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Paleosuchus palpebrosus
Length
559 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.385 kDa
Sequence
MAALEGPLAVLGERSSGDTVRNQNVTAAATIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELAELQDKEVGDGTTSVVIIAAELLKNSDELVKQKIHPTSIIGGYRLACKEAVRYINENLIINTDELGRDCLINSAKTSMSSKIIGIDGDFFASMVVDAASAVKYTDQKGQARYPINSINVLKAHGRSQKESILVNGYALNCVVGSQGMTKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVDAGAMAVRRVLKKDLKRIAKASGATVCSTLANLEGEESFEASMLGQAEEVVQERVCDDELILIKNTKARTSASIILRGANDFMCDEMERSIHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLIIPNTLAVNAAQDATDLVAKLRAFHNEAQVNPERKNLKWIGLDLINGKPRDNKQAGVFEPTLVKTKSLKFATEAAITILRIDDLIKLHPESKDDKGGCYEDAVRSGALEE

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
559 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.481 kDa
Sequence
MSQLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKMLVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVVIIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDTLGKETLINIAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKAHGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAMGVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLKEFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLCDEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSVVKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLIIPKTLAVNAAKDSSELVAKLRSYHAASQMAKPEDVKRRSYRNYGLDLIRGKIVDEIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPEPPKEDPHDH

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Monodelphis domestica
Length
557 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.579 kDa
Sequence
MEGPLSVFGERTTGESIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSIIGGYRLACKEAVRYINENLIINTDELGKDCLINAAKTSMSSKIIGIDGDFFANMVVDAVLAVKYTDVKGQPRYPVNSINVLKAHGRSQKESMLINGYALNCVVASQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRKREADITKERIQKILATGANVILTTGGIDDMCLKYFVESMTIAVRRVLKRDLKRIAKASGATILSTLASLEGEESFEASMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLIIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVNGKPRDNRQTGVFEPTMVKVKSLKFATEAAITILRIDDLIKLHPESKDDKRGGTYEDAVHSGAIED

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Cricetulus griseus
Length
556 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.339 kDa
Sequence
MEGPLSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYISENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAVKYTDLRGQPRYPVNSVNILKAHGRSQVESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIEKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLINGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPETKDDKHGSYENAVHSGALDD

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Homo sapiens
Length
556 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.344 kDa
Sequence
MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYEDAVHSGALND

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Macaca fascicularis
Length
556 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.256 kDa
Sequence
MEGPLSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELGKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDTRGQPRYPVNSVNILKAHGRSQMESKLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYEDAVHSGALND

Gene
Tcp1
Protein
T-complex protein 1 subunit alpha
Organism
Mus musculus
Length
556 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.449 kDa
Sequence
MEGPLSVFGDRSTGEAVRSQNVMAAASIANIVKSSFGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEETFEVTMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYENAVHSGALDD

Gene
Tcp1
Protein
T-complex protein 1 subunit alpha
Organism
Rattus norvegicus
Length
556 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.36 kDa
Sequence
MEGPLSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAVKYTDIRGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMLKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGASILSTLANLEGEETFEATMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGGYENAVHSGALDD

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Bos taurus
Length
556 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
60.206 kDa
Sequence
MEGPLSVFGDRSTGEAIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYISENLIINTDELGRDCLINAAKTSMSSKVIGINGDFFANLVVDAVLAIKYTDIRGQPRYPVNSINVLKAHGRSQMESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATVLSTLANLEGEETFEASMLGQAEEVVQERICDDELILIKNTKARTSASVILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLPVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGGYEDAVHSGALDA

Gene
tcp1
Protein
T-complex protein 1 subunit alpha
Organism
Dictyostelium discoideum
Length
548 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
59.406 kDa
Sequence
MSNKVLMIDGDRISGNEVRAQNVLAVTAIANIVKTSFGPIGLDKMLIDNIGSIVVTNDGATILQKIDIEHPAAKILVQLSELQDQEVGDGTTTVVILAAELLKRANELVARKVHPTVIISGFRLACTEAIKYINETLAVKVETLPKDFIVNIAKTSMSSKTINDDSDFFSKIVIEAITRVKTIDYKGDVKYPINAINILKAHGKSAKESTLVEGYALNCTVASEGMPKRIQGAKIAFLDFNLAKTKMKLGQKVVVTNVNDLEAIRDRENDIVKERISLIIKSGANVVLTTKGIDDLCLKYFVEAGCMAVRRCKKEDLKRIAKSCGGTVLITLANLEGEESFDTTALGIADEVVQDRLADDELIIVKNSNKKSASIILRGANELMLDEMERSIHDSLCIVKRTLESGTIVPGGGAVESALSIYLDNIAATMGSRKQLAISEFAESLLVVPKQLAVNAALDASDLVSKLKAYHHAAQTDPSKKSYAYSGLDLFNNKVRNNLEAGVLEPAIAKIKCIKFATESAITILRIDDKITLNPREQQGGDHEGHGH

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Encephalitozoon cuniculi (strain GB-M1)
Length
540 amino acids
Function
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
58.211 kDa
Sequence
MNKEISTADILSGGESYSGISAVEKNAKAMMKVYNAIKTSFGPLGLDKMCVDSAGEVSITNDGATILQNMLIDDPAAKILVDLATQQDHEVGDGTTSVVLIAVSLIEKGAKLIASGVHPSVVVSGYKMAFNECVQFIKKSMSKSTLNLGSKALRNVVETSISSKVISSESEVFCGIVIDALKCIESVDENRKNMYPIEDINILKHPGGSMKESFLHQGYALNCSLASNFMKRQVKKPKILCIDFGLQKYKNPLTVSIVVDDPNKLEDIRKKELEITRRQIKTIIDSGANVVLTTRGIDDMCTKLLVEADVVGIRRCKKEDLLVIAKATGTSLVSSIADISGADSISSLGFADKFEVVQIGEEECVLINGLKKKMASIILRGANCQLLDEMQRSVHDAVCVLKRTLESNSVVPGGGAVECALSLMLEKFAFTVNSKEHVAIHRYAESLLSIPKILSTNAGLDSNELVANLLSSQSREMANSSGSKFLGIDVTSGKIQDNFEFGIIEPSVNKMKSLKAATEAAISILRINEVIILPPDQSKN

Gene
TCP1
Protein
Transcription factor TCP1
Organism
Arabidopsis thaliana
Length
359 amino acids
Function
Involved in petal morphogenesis.
Mass
40.754 kDa
Sequence
MSSSTNDYNDGNNNGVYPLSLYLSSLSGHQDIIHNPYNHQLKASPGHMVSAVPESLIDYMAFKSNNVVNQQGFEFPEVSKEIKKVVKKDRHSKIQTAQGIRDRRVRLSIGIARQFFDLQDMLGFDKASKTLDWLLKKSRKAIKEVVQAKNLNNDDEDFGNIGGDVEQEEEKEEDDNGDKSFVYGLSPGYGEEEVVCEATKAGIRKKKSELRNISSKGLGAKARGKAKERTKEMMAYDNPETASDITQSEIMDPFKRSIVFNEGEDMTHLFYKEPIEEFDNQESILTNMTLPTKMGQSYNQNNGILMLVDQSSSSNYNTFLPQNLDYSYDQNPFHDQTLYVVTDKNFPKGKVWIQDSFVN

Gene
TCP1
Protein
T-complex protein 1 subunit alpha
Organism
Mesocricetus auratus
Length
123 amino acids
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Similarity
Belongs to the TCP-1 chaperonin family.
Mass
13.411 kDa
Fragment
multiple
Sequence
IHPTSVISGYRYISENLIINTDELGRDCLINAAKLGVQVVITDPEKLDQIRYFVEAGAMAVRSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARAFHNEAQVNPERKFATEAAITILR