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Protein

T-complex protein 1 subunit eta

Gene

CCT7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: ProtInc

GO - Biological processi

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 eta
Short name:
TCP-1-eta
Alternative name(s):
CCT-eta
HIV-1 Nef-interacting protein
Gene namesi
Name:CCT7
Synonyms:CCTH, NIP7-1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1622. CCT7.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: Ensembl
  • chaperonin-containing T-complex Source: UniProtKB
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB
  • mitochondrion Source: Ensembl
  • zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26185.

Polymorphism and mutation databases

BioMutaiCCT7.
DMDMi3041738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543T-complex protein 1 subunit etaPRO_0000128365Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei67 – 671N6-acetyllysine1 Publication
Modified residuei250 – 2501N6-acetyllysineBy similarity
Modified residuei320 – 3201N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99832.
PaxDbiQ99832.
PRIDEiQ99832.

2D gel databases

REPRODUCTION-2DPAGEIPI00018465.

PTM databases

PhosphoSiteiQ99832.

Expressioni

Gene expression databases

BgeeiQ99832.
CleanExiHS_CCT7.
ExpressionAtlasiQ99832. baseline and differential.
GenevisibleiQ99832. HS.

Organism-specific databases

HPAiHPA008425.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SSSCA1O602323EBI-357046,EBI-741415

Protein-protein interaction databases

BioGridi115825. 119 interactions.
DIPiDIP-51608N.
IntActiQ99832. 61 interactions.
MINTiMINT-1131353.
STRINGi9606.ENSP00000258091.

Structurei

3D structure databases

ProteinModelPortaliQ99832.
SMRiQ99832. Positions 6-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074832.
HOGENOMiHOG000226730.
HOVERGENiHBG001052.
InParanoidiQ99832.
KOiK09499.
OMAiNINACQV.
OrthoDBiEOG7V49Z2.
PhylomeDBiQ99832.
TreeFamiTF105641.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012720. Chap_CCT_eta.
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:SF22. PTHR11353:SF22. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99832-1) [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
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV
60 70 80 90 100
DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL
110 120 130 140 150
AAEFLKQVKP YVEEGLHPQI IIRAFRTATQ LAVNKIKEIA VTVKKADKVE
160 170 180 190 200
QRKLLEKCAM TALSSKLISQ QKAFFAKMVV DAVMMLDDLL QLKMIGIKKV
210 220 230 240 250
QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL NVELELKAEK
260 270 280 290 300
DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT
310 320 330 340 350
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE
360 370 380 390 400
TQIGGERYNF FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI
410 420 430 440 450
KNDSVVAGGG AIEMELSKYL RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC
460 470 480 490 500
DNAGFDATNI LNKLRARHAQ GGTWYGVDIN NEDIADNFEA FVWEPAMVRI
510 520 530 540
NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG RPH
Length:543
Mass (Da):59,367
Last modified:July 15, 1998 - v2
Checksum:i9F1E33FA80E6238E
GO
Isoform 2 (identifier: Q99832-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-89: Missing.
     90-206: Missing.

Note: No experimental confirmation available.
Show »
Length:339
Mass (Da):37,499
Checksum:iBA74E59CE7977306
GO
Isoform 3 (identifier: Q99832-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Note: No experimental confirmation available. Contains a N-acetylmethionine at position 1.1 Publication
Show »
Length:499
Mass (Da):54,804
Checksum:i19F19C1820F6A80A
GO
Isoform 4 (identifier: Q99832-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-89: Missing.

Note: No experimental confirmation available.
Show »
Length:456
Mass (Da):50,352
Checksum:iAD52175094D0BD23
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2832HH → RQ in AAB41437 (Ref. 8) Curated
Sequence conflicti293 – 2931L → P in AAB41437 (Ref. 8) Curated
Sequence conflicti336 – 3361A → P in AAB41437 (Ref. 8) Curated
Sequence conflicti364 – 3641C → L in AAB41437 (Ref. 8) Curated
Sequence conflicti374 – 3763LRG → SPC in AAB41437 (Ref. 8) Curated
Sequence conflicti407 – 4071A → P in AAB41437 (Ref. 8) Curated
Sequence conflicti411 – 4111A → P in AAB41437 (Ref. 8) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591T → A.
Corresponds to variant rs2231427 [ dbSNP | Ensembl ].
VAR_052269

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444Missing in isoform 3. 1 PublicationVSP_043572Add
BLAST
Alternative sequencei3 – 8987Missing in isoform 2 and isoform 4. 1 PublicationVSP_043573Add
BLAST
Alternative sequencei90 – 206117Missing in isoform 2. 1 PublicationVSP_043574Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026292 mRNA. Translation: AAC96011.1.
CR536511 mRNA. Translation: CAG38749.1.
AK291961 mRNA. Translation: BAF84650.1.
AK293597 mRNA. Translation: BAH11543.1.
AK297846 mRNA. Translation: BAH12675.1.
AK298153 mRNA. Translation: BAH12733.1.
AC010913 Genomic DNA. Translation: AAX88902.1.
CH471053 Genomic DNA. Translation: EAW99739.1.
CH471053 Genomic DNA. Translation: EAW99740.1.
BC019296 mRNA. Translation: AAH19296.1.
BC088351 mRNA. Translation: AAH88351.1.
U83843 mRNA. Translation: AAB41437.1.
CCDSiCCDS42696.1. [Q99832-2]
CCDS46336.1. [Q99832-1]
CCDS54366.1. [Q99832-4]
CCDS54367.1. [Q99832-3]
RefSeqiNP_001009570.1. NM_001009570.2. [Q99832-2]
NP_001159756.1. NM_001166284.1. [Q99832-4]
NP_001159757.1. NM_001166285.1. [Q99832-3]
NP_006420.1. NM_006429.3. [Q99832-1]
UniGeneiHs.368149.

Genome annotation databases

EnsembliENST00000258091; ENSP00000258091; ENSG00000135624. [Q99832-1]
ENST00000398422; ENSP00000381456; ENSG00000135624. [Q99832-2]
ENST00000539919; ENSP00000437824; ENSG00000135624. [Q99832-3]
ENST00000540468; ENSP00000442058; ENSG00000135624. [Q99832-4]
GeneIDi10574.
KEGGihsa:10574.
UCSCiuc002siz.3. human. [Q99832-1]
uc002sja.3. human. [Q99832-2]
uc010yri.2. human. [Q99832-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026292 mRNA. Translation: AAC96011.1.
CR536511 mRNA. Translation: CAG38749.1.
AK291961 mRNA. Translation: BAF84650.1.
AK293597 mRNA. Translation: BAH11543.1.
AK297846 mRNA. Translation: BAH12675.1.
AK298153 mRNA. Translation: BAH12733.1.
AC010913 Genomic DNA. Translation: AAX88902.1.
CH471053 Genomic DNA. Translation: EAW99739.1.
CH471053 Genomic DNA. Translation: EAW99740.1.
BC019296 mRNA. Translation: AAH19296.1.
BC088351 mRNA. Translation: AAH88351.1.
U83843 mRNA. Translation: AAB41437.1.
CCDSiCCDS42696.1. [Q99832-2]
CCDS46336.1. [Q99832-1]
CCDS54366.1. [Q99832-4]
CCDS54367.1. [Q99832-3]
RefSeqiNP_001009570.1. NM_001009570.2. [Q99832-2]
NP_001159756.1. NM_001166284.1. [Q99832-4]
NP_001159757.1. NM_001166285.1. [Q99832-3]
NP_006420.1. NM_006429.3. [Q99832-1]
UniGeneiHs.368149.

3D structure databases

ProteinModelPortaliQ99832.
SMRiQ99832. Positions 6-523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115825. 119 interactions.
DIPiDIP-51608N.
IntActiQ99832. 61 interactions.
MINTiMINT-1131353.
STRINGi9606.ENSP00000258091.

PTM databases

PhosphoSiteiQ99832.

Polymorphism and mutation databases

BioMutaiCCT7.
DMDMi3041738.

2D gel databases

REPRODUCTION-2DPAGEIPI00018465.

Proteomic databases

MaxQBiQ99832.
PaxDbiQ99832.
PRIDEiQ99832.

Protocols and materials databases

DNASUi10574.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258091; ENSP00000258091; ENSG00000135624. [Q99832-1]
ENST00000398422; ENSP00000381456; ENSG00000135624. [Q99832-2]
ENST00000539919; ENSP00000437824; ENSG00000135624. [Q99832-3]
ENST00000540468; ENSP00000442058; ENSG00000135624. [Q99832-4]
GeneIDi10574.
KEGGihsa:10574.
UCSCiuc002siz.3. human. [Q99832-1]
uc002sja.3. human. [Q99832-2]
uc010yri.2. human. [Q99832-4]

Organism-specific databases

CTDi10574.
GeneCardsiGC02P073460.
HGNCiHGNC:1622. CCT7.
HPAiHPA008425.
MIMi605140. gene.
neXtProtiNX_Q99832.
PharmGKBiPA26185.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0459.
GeneTreeiENSGT00550000074832.
HOGENOMiHOG000226730.
HOVERGENiHBG001052.
InParanoidiQ99832.
KOiK09499.
OMAiNINACQV.
OrthoDBiEOG7V49Z2.
PhylomeDBiQ99832.
TreeFamiTF105641.

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.

Miscellaneous databases

ChiTaRSiCCT7. human.
GeneWikiiCCT7.
GenomeRNAii10574.
NextBioi40131.
PROiQ99832.
SOURCEiSearch...

Gene expression databases

BgeeiQ99832.
CleanExiHS_CCT7.
ExpressionAtlasiQ99832. baseline and differential.
GenevisibleiQ99832. HS.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012720. Chap_CCT_eta.
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:SF22. PTHR11353:SF22. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT."
    Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.
    Mol. Cell. Biol. 18:7584-7589(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Cerebellum and Heart.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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).
    Tissue: PNS and Skin.
  7. Cited for: PROTEIN SEQUENCE OF 1-10; 56-67; 85-123; 127-144; 178-193; 200-217; 219-230; 237-247; 293-306; 314-320; 376-397; 402-418; 431-447 AND 500-535, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma, Hepatoma and Osteosarcoma.
  8. Fukushi M., Kimura T., Yamamoto N.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-424 (ISOFORM 1).
  9. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 107-123, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  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. "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].
  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-67 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTCPH_HUMAN
AccessioniPrimary (citable) accession number: Q99832
Secondary accession number(s): A8K7E6
, A8MWI8, B7WNW9, B7Z4T9, B7Z4Z7, O14871, Q6FI26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: June 24, 2015
This is version 153 of the entry and version 2 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 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.