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Protein

Tubulin-specific chaperone E

Gene

TBCE

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

Functioni

Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation.1 Publication

GO - Molecular functioni

  • chaperone binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiR-HSA-389977. Post-chaperonin tubulin folding pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-specific chaperone E
Alternative name(s):
Tubulin-folding cofactor E
Gene namesi
Name:TBCE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11582. TBCE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • microtubule Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Hypoparathyroidism-retardation-dysmorphism syndrome (HRD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disorder reported almost exclusively in Middle Eastern populations.
See also OMIM:241410
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 554Missing in HRD and KCS1. 1 Publication
VAR_032920
Kenny-Caffey syndrome 1 (KCS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive form of Kenny-Caffey syndrome, a disorder characterized by impaired skeletal development with small and dense bones, short stature, and primary hypoparathyroidism with hypocalcemia. Clinical features include cortical thickening and medullary stenosis of the tubular bones, delayed closure of fontanels, defective dentition, small eyes with hypermetropia, and frontal bossing with a triangular face.
See also OMIM:244460
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 554Missing in HRD and KCS1. 1 Publication
VAR_032920

Keywords - Diseasei

Disease mutation, Dwarfism, Mental retardation

Organism-specific databases

MalaCardsiTBCE.
MIMi241410. phenotype.
244460. phenotype.
Orphaneti93324. Autosomal recessive Kenny-Caffey syndrome.
2323. Sanjad-Sakati syndrome.
PharmGKBiPA36346.

Polymorphism and mutation databases

DMDMi74762146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 527526Tubulin-specific chaperone EPRO_0000083538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei463 – 4631N6-acetyllysineCombined sources
Modified residuei495 – 4951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15813.
MaxQBiQ15813.
PaxDbiQ15813.
PeptideAtlasiQ15813.
PRIDEiQ15813.

PTM databases

iPTMnetiQ15813.
PhosphoSiteiQ15813.

Expressioni

Gene expression databases

BgeeiQ15813.
CleanExiHS_TBCE.
GenevisibleiQ15813. HS.

Organism-specific databases

HPAiHPA026552.
HPA026557.
HPA026559.

Interactioni

Subunit structurei

Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state. Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers.

GO - Molecular functioni

  • chaperone binding Source: ProtInc

Protein-protein interaction databases

BioGridi112768. 20 interactions.
IntActiQ15813. 1 interaction.
STRINGi9606.ENSP00000355560.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi445 – 4517Combined sources
Turni453 – 4553Combined sources
Helixi457 – 4593Combined sources
Beta strandi461 – 4666Combined sources
Helixi471 – 48212Combined sources
Helixi486 – 4883Combined sources
Beta strandi490 – 4945Combined sources
Helixi513 – 5153Combined sources
Beta strandi522 – 5265Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ICUX-ray2.40A/B/C/D443-527[»]
4ICVX-ray1.45A443-527[»]
ProteinModelPortaliQ15813.
SMRiQ15813. Positions 10-75, 122-385, 444-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 7145CAP-GlyPROSITE-ProRule annotationAdd
BLAST
Repeati154 – 17522LRR 1Add
BLAST
Repeati180 – 20021LRR 2Add
BLAST
Repeati205 – 22622LRR 3Add
BLAST
Repeati230 – 25223LRR 4Add
BLAST
Repeati253 – 27422LRR 5Add
BLAST
Repeati278 – 29922LRR 6Add
BLAST
Repeati308 – 32922LRR 7Add
BLAST
Domaini342 – 38443LRRCTAdd
BLAST

Sequence similaritiesi

Belongs to the TBCE family.Curated
Contains 1 CAP-Gly domain.PROSITE-ProRule annotation
Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG3207. Eukaryota.
ENOG410YS3M. LUCA.
GeneTreeiENSGT00530000063405.
HOGENOMiHOG000154513.
HOVERGENiHBG084170.
InParanoidiQ15813.
OMAiVSLRNCA.
OrthoDBiEOG7T1RB1.
PhylomeDBiQ15813.
TreeFamiTF313455.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032675. L_dom-like.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01302. CAP_GLY. 1 hit.
PF14560. Ubiquitin_2. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15813-1) [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
MSDTLTADVI GRRVEVNGEH ATVRFAGVVP PVAGPWLGVE WDNPERGKHD
60 70 80 90 100
GSHEGTVYFK CRHPTGGSFI RPNKVNFGTD FLTAIKNRYV LEDGPEEDRK
110 120 130 140 150
EQIVTIGNKP VETIGFDSIM KQQSQLSKLQ EVSLRNCAVS CAGEKGGVAE
160 170 180 190 200
ACPNIRKVDL SKNLLSSWDE VIHIADQLRH LEVLNVSENK LKFPSGSVLT
210 220 230 240 250
GTLSVLKVLV LNQTGITWAE VLRCVAGCPG LEELYLESNN IFISERPTDV
260 270 280 290 300
LQTVKLLDLS SNQLIDENQL YLIAHLPRLE QLILSDTGIS SLHFPDAGIG
310 320 330 340 350
CKTSMFPSLK YLVVNDNQIS QWSFFNELEK LPSLRALSCL RNPLTKEDKE
360 370 380 390 400
AETARLLIIA SIGQLKTLNK CEILPEERRR AELDYRKAFG NEWKQAGGHK
410 420 430 440 450
DPEKNRLSEE FLTAHPRYQF LCLKYGAPED WELKTQQPLM LKNQLLTLKI
460 470 480 490 500
KYPHQLDQKV LEKQLPGSMT IQKVKGLLSR LLKVPVSDLL LSYESPKKPG
510 520
REIELENDLK SLQFYSVENG DCLLVRW
Length:527
Mass (Da):59,346
Last modified:November 1, 1996 - v1
Checksum:iC919052D2D463BA1
GO
Isoform 2 (identifier: Q15813-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-220: E → EAHAQCGGSRHGLDMQKDASKFVDLCVLQKCSTSNCIISAKDHTSMRMNVAK

Note: No experimental confirmation available.
Show »
Length:578
Mass (Da):64,852
Checksum:i2719A81F520471CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti450 – 4501I → V in BAF84976 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 554Missing in HRD and KCS1. 1 Publication
VAR_032920
Natural varianti205 – 2051V → A.
Corresponds to variant rs16832611 [ dbSNP | Ensembl ].
VAR_032921
Natural varianti333 – 3331S → T.
Corresponds to variant rs35579976 [ dbSNP | Ensembl ].
VAR_032922
Natural varianti409 – 4091E → G.
Corresponds to variant rs16832619 [ dbSNP | Ensembl ].
VAR_032923

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei220 – 2201E → EAHAQCGGSRHGLDMQKDAS KFVDLCVLQKCSTSNCIISA KDHTSMRMNVAK in isoform 2. 1 PublicationVSP_053870

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61232 mRNA. Translation: AAB17538.1.
BT007086 mRNA. Translation: AAP35749.1.
AK292287 mRNA. Translation: BAF84976.1.
AK296185 mRNA. Translation: BAH12277.1.
AL357556 Genomic DNA. No translation available.
AL672237 Genomic DNA. No translation available.
FO393422 Genomic DNA. No translation available.
BC008654 mRNA. Translation: AAH08654.1.
CCDSiCCDS1605.1. [Q15813-1]
CCDS73052.1. [Q15813-2]
RefSeqiNP_001072983.1. NM_001079515.2. [Q15813-1]
NP_001274730.1. NM_001287801.1. [Q15813-2]
NP_001274731.1. NM_001287802.1.
NP_003184.1. NM_003193.4. [Q15813-1]
UniGeneiHs.744998.

Genome annotation databases

EnsembliENST00000366601; ENSP00000355560; ENSG00000116957. [Q15813-1]
ENST00000406207; ENSP00000384571; ENSG00000116957. [Q15813-1]
ENST00000543662; ENSP00000439170; ENSG00000116957. [Q15813-2]
ENST00000634751; ENSP00000489110; ENSG00000282984. [Q15813-1]
ENST00000634780; ENSP00000488933; ENSG00000282984. [Q15813-1]
ENST00000635692; ENSP00000489157; ENSG00000282984. [Q15813-2]
GeneIDi6905.
KEGGihsa:6905.
UCSCiuc001hwz.2. human. [Q15813-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61232 mRNA. Translation: AAB17538.1.
BT007086 mRNA. Translation: AAP35749.1.
AK292287 mRNA. Translation: BAF84976.1.
AK296185 mRNA. Translation: BAH12277.1.
AL357556 Genomic DNA. No translation available.
AL672237 Genomic DNA. No translation available.
FO393422 Genomic DNA. No translation available.
BC008654 mRNA. Translation: AAH08654.1.
CCDSiCCDS1605.1. [Q15813-1]
CCDS73052.1. [Q15813-2]
RefSeqiNP_001072983.1. NM_001079515.2. [Q15813-1]
NP_001274730.1. NM_001287801.1. [Q15813-2]
NP_001274731.1. NM_001287802.1.
NP_003184.1. NM_003193.4. [Q15813-1]
UniGeneiHs.744998.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ICUX-ray2.40A/B/C/D443-527[»]
4ICVX-ray1.45A443-527[»]
ProteinModelPortaliQ15813.
SMRiQ15813. Positions 10-75, 122-385, 444-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112768. 20 interactions.
IntActiQ15813. 1 interaction.
STRINGi9606.ENSP00000355560.

PTM databases

iPTMnetiQ15813.
PhosphoSiteiQ15813.

Polymorphism and mutation databases

DMDMi74762146.

Proteomic databases

EPDiQ15813.
MaxQBiQ15813.
PaxDbiQ15813.
PeptideAtlasiQ15813.
PRIDEiQ15813.

Protocols and materials databases

DNASUi6905.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366601; ENSP00000355560; ENSG00000116957. [Q15813-1]
ENST00000406207; ENSP00000384571; ENSG00000116957. [Q15813-1]
ENST00000543662; ENSP00000439170; ENSG00000116957. [Q15813-2]
ENST00000634751; ENSP00000489110; ENSG00000282984. [Q15813-1]
ENST00000634780; ENSP00000488933; ENSG00000282984. [Q15813-1]
ENST00000635692; ENSP00000489157; ENSG00000282984. [Q15813-2]
GeneIDi6905.
KEGGihsa:6905.
UCSCiuc001hwz.2. human. [Q15813-1]

Organism-specific databases

CTDi6905.
GeneCardsiTBCE.
HGNCiHGNC:11582. TBCE.
HPAiHPA026552.
HPA026557.
HPA026559.
MalaCardsiTBCE.
MIMi241410. phenotype.
244460. phenotype.
604934. gene.
neXtProtiNX_Q15813.
Orphaneti93324. Autosomal recessive Kenny-Caffey syndrome.
2323. Sanjad-Sakati syndrome.
PharmGKBiPA36346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3207. Eukaryota.
ENOG410YS3M. LUCA.
GeneTreeiENSGT00530000063405.
HOGENOMiHOG000154513.
HOVERGENiHBG084170.
InParanoidiQ15813.
OMAiVSLRNCA.
OrthoDBiEOG7T1RB1.
PhylomeDBiQ15813.
TreeFamiTF313455.

Enzyme and pathway databases

ReactomeiR-HSA-389977. Post-chaperonin tubulin folding pathway.

Miscellaneous databases

ChiTaRSiTBCE. human.
GeneWikiiTBCE.
GenomeRNAii6905.
NextBioi27001.
PROiQ15813.
SOURCEiSearch...

Gene expression databases

BgeeiQ15813.
CleanExiHS_TBCE.
GenevisibleiQ15813. HS.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032675. L_dom-like.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01302. CAP_GLY. 1 hit.
PF14560. Ubiquitin_2. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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 (MAY-2003) 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 AND 2).
    Tissue: Testis and Thalamus.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Eye.
  6. "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C."
    Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., Cowan N.J.
    J. Biol. Chem. 277:14629-14634(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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 SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANT HRD 52-SER--GLY-55 DEL, VARIANT KCS1 52-SER--GLY-55 DEL.

Entry informationi

Entry nameiTBCE_HUMAN
AccessioniPrimary (citable) accession number: Q15813
Secondary accession number(s): A8K8C2, B7Z3P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 147 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.