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P17987

- TCPA_HUMAN

UniProt

P17987 - TCPA_HUMAN

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Protein

T-complex protein 1 subunit alpha

Gene

TCP1

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
  5. tubulin complex assembly 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 alpha
Short name:
TCP-1-alpha
Alternative name(s):
CCT-alpha
Gene namesi
Name:TCP1
Synonyms:CCT1, CCTA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11655. TCP1.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. cell body Source: Ensembl
  3. centrosome Source: MGI
  4. chaperonin-containing T-complex Source: Ensembl
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. Golgi apparatus Source: Ensembl
  8. microtubule Source: UniProtKB
  9. nuclear heterochromatin Source: Ensembl
  10. pericentriolar material Source: Ensembl
  11. zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556T-complex protein 1 subunit alphaPRO_0000128302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei181 – 1811Phosphotyrosine1 Publication
Modified residuei182 – 1821Phosphothreonine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei400 – 4001N6-acetyllysine1 Publication
Modified residuei494 – 4941N6-acetyllysineBy similarity
Modified residuei544 – 5441Phosphoserine4 Publications
Modified residuei551 – 5511Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17987.
PaxDbiP17987.
PeptideAtlasiP17987.
PRIDEiP17987.

2D gel databases

OGPiP17987.
REPRODUCTION-2DPAGEIPI00290566.
P17987.
UCD-2DPAGEP17987.

PTM databases

PhosphoSiteiP17987.

Expressioni

Gene expression databases

BgeeiP17987.
CleanExiHS_TCP1.
ExpressionAtlasiP17987. baseline and differential.
GenevestigatoriP17987.

Organism-specific databases

HPAiCAB017460.
HPA027337.
HPA031082.

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 CCT8.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OLR1P783805EBI-356553,EBI-7151999

Protein-protein interaction databases

BioGridi112810. 109 interactions.
DIPiDIP-33676N.
IntActiP17987. 58 interactions.
MINTiMINT-4999235.
STRINGi9606.ENSP00000317334.

Structurei

3D structure databases

ProteinModelPortaliP17987.
SMRiP17987. Positions 9-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074878.
HOGENOMiHOG000226729.
HOVERGENiHBG001052.
InParanoidiP17987.
KOiK09493.
OMAiIMRIDTL.
OrthoDBiEOG7K3TKJ.
PhylomeDBiP17987.
TreeFamiTF106331.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR017998. 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.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17987-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG
60 70 80 90 100
DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL
110 120 130 140 150
LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN
160 170 180 190 200
AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA
210 220 230 240 250
HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV
260 270 280 290 300
QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
310 320 330 340 350
VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE
360 370 380 390 400
VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK
410 420 430 440 450
RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN
460 470 480 490 500
TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ
510 520 530 540 550
AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH

SGALND
Length:556
Mass (Da):60,344
Last modified:November 1, 1990 - v1
Checksum:i486ECA836EA258A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti480 – 4801R → S in AAA61060. (PubMed:3653076)Curated
Sequence conflicti537 – 5404SKDD → ILRI in CAA37064. (PubMed:2377466)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71V → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036258

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52882 mRNA. Translation: CAA37064.1.
BT006969 mRNA. Translation: AAP35615.1.
AL135914 Genomic DNA. Translation: CAI21851.1.
CH471051 Genomic DNA. Translation: EAW47616.1.
CH471051 Genomic DNA. Translation: EAW47618.1.
BC000665 mRNA. Translation: AAH00665.1.
M26885 Genomic DNA. Translation: AAA61059.1.
M27272, M26889 Genomic DNA. Translation: AAA61060.1.
CCDSiCCDS5269.1.
PIRiS10486.
RefSeqiNP_110379.2. NM_030752.2.
UniGeneiHs.363137.

Genome annotation databases

EnsembliENST00000321394; ENSP00000317334; ENSG00000120438.
GeneIDi6950.
KEGGihsa:6950.
UCSCiuc003qsr.3. human.

Polymorphism databases

DMDMi135538.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52882 mRNA. Translation: CAA37064.1 .
BT006969 mRNA. Translation: AAP35615.1 .
AL135914 Genomic DNA. Translation: CAI21851.1 .
CH471051 Genomic DNA. Translation: EAW47616.1 .
CH471051 Genomic DNA. Translation: EAW47618.1 .
BC000665 mRNA. Translation: AAH00665.1 .
M26885 Genomic DNA. Translation: AAA61059.1 .
M27272 , M26889 Genomic DNA. Translation: AAA61060.1 .
CCDSi CCDS5269.1.
PIRi S10486.
RefSeqi NP_110379.2. NM_030752.2.
UniGenei Hs.363137.

3D structure databases

ProteinModelPortali P17987.
SMRi P17987. Positions 9-542.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112810. 109 interactions.
DIPi DIP-33676N.
IntActi P17987. 58 interactions.
MINTi MINT-4999235.
STRINGi 9606.ENSP00000317334.

PTM databases

PhosphoSitei P17987.

Polymorphism databases

DMDMi 135538.

2D gel databases

OGPi P17987.
REPRODUCTION-2DPAGE IPI00290566.
P17987.
UCD-2DPAGE P17987.

Proteomic databases

MaxQBi P17987.
PaxDbi P17987.
PeptideAtlasi P17987.
PRIDEi P17987.

Protocols and materials databases

DNASUi 6950.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321394 ; ENSP00000317334 ; ENSG00000120438 .
GeneIDi 6950.
KEGGi hsa:6950.
UCSCi uc003qsr.3. human.

Organism-specific databases

CTDi 6950.
GeneCardsi GC06M160199.
HGNCi HGNC:11655. TCP1.
HPAi CAB017460.
HPA027337.
HPA031082.
MIMi 186980. gene.
neXtProti NX_P17987.
PharmGKBi PA36406.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0459.
GeneTreei ENSGT00550000074878.
HOGENOMi HOG000226729.
HOVERGENi HBG001052.
InParanoidi P17987.
KOi K09493.
OMAi IMRIDTL.
OrthoDBi EOG7K3TKJ.
PhylomeDBi P17987.
TreeFami TF106331.

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 TCP1. human.
GeneWikii T-complex_1.
GenomeRNAii 6950.
NextBioi 27215.
PROi P17987.
SOURCEi Search...

Gene expression databases

Bgeei P17987.
CleanExi HS_TCP1.
ExpressionAtlasi P17987. baseline and differential.
Genevestigatori P17987.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProi 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.
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. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Colon.
  6. "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 1-11, ACETYLATION AT MET-1.
    Tissue: Platelet.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 112-122; 131-145; 248-264; 469-480 AND 516-526, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "The human homologue of the mouse T-complex gene, TCP1, is located on chromosome 6 but is not near the HLA region."
    Willison K., Kelly A., Dudley K., Goodfellow P., Spurr N., Groves V., Gorman P., Sheer D., Trowsdale J.
    EMBO J. 6:1967-1974(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-365 AND 462-516.
  9. "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol."
    Lewis V.A., Hynes G.M., Zheng D., Saibil H., Willison K.R.
    Nature 358:249-252(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  10. "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.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. "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 TYR-181; THR-182 AND SER-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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 LYS-199 AND LYS-400, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-7.

Entry informationi

Entry nameiTCPA_HUMAN
AccessioniPrimary (citable) accession number: P17987
Secondary accession number(s): E1P5B2, Q15556, Q5TCM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 156 of the entry and version 1 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 6
    Human chromosome 6: 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

Dasty 3