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Protein

Thyroid receptor-interacting protein 11

Gene

TRIP11

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

Functioni

Binds the ligand binding domain of the thyroid receptor (THRB) in the presence of triiodothyronine and enhances THRB-modulated transcription. Golgi auto-antigen; probably involved in maintaining cis-Golgi structure.2 Publications

GO - Molecular functioni

  • transcription coactivator activity Source: ProtInc

GO - Biological processi

  • organelle organization Source: Reactome
  • protein targeting to Golgi Source: InterPro
  • regulation of nucleic acid-templated transcription Source: GOC
  • transcription from RNA polymerase II promoter Source: ProtInc
  • ventricular septum development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-5620924. Intraflagellar transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid receptor-interacting protein 11
Short name:
TR-interacting protein 11
Short name:
TRIP-11
Alternative name(s):
Clonal evolution-related gene on chromosome 14 protein
Golgi-associated microtubule-binding protein 210
Short name:
GMAP-210
Trip230
Gene namesi
Name:TRIP11
Synonyms:CEV14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:12305. TRIP11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TRIP11 may be a cause of acute myelogenous leukemia. Translocation t(5;14)(q33;q32) with PDGFRB. The fusion protein may be involved in clonal evolution of leukemia and eosinophilia.

Achondrogenesis 1A (ACG1A)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of achondrogenesis type 1, a lethal form of chondrodysplasia characterized by deficient ossification in the lumbar vertebrae and absent ossification in the sacral, pubic and ischial bones and clinically by stillbirth or early death. In addition to severe micromelia, there is a disproportionately large cranium due to marked edema of soft tissues.
See also OMIM:200600

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1754 – 17552Breakpoint for translocation to form TRIP11-PDGFRB

Keywords - Diseasei

Dwarfism

Organism-specific databases

MalaCardsiTRIP11.
MIMi200600. phenotype.
Orphaneti93299. Achondrogenesis type 1A.
PharmGKBiPA36984.

Polymorphism and mutation databases

BioMutaiTRIP11.
DMDMi292495059.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 19791978Thyroid receptor-interacting protein 11PRO_0000190076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei464 – 4641PhosphoserineCombined sources
Modified residuei1842 – 18421PhosphoserineCombined sources
Modified residuei1846 – 18461PhosphothreonineCombined sources
Modified residuei1891 – 18911PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15643.
MaxQBiQ15643.
PaxDbiQ15643.
PRIDEiQ15643.

PTM databases

iPTMnetiQ15643.
PhosphoSiteiQ15643.

Expressioni

Tissue specificityi

Highly expressed in pancreas, muscle, heart, testis, peripheral blood leukocytes, and in several leukemia cell lines. Detected at intermediate levels in placenta and kidney, and at low levels in brain and lung.2 Publications

Gene expression databases

BgeeiQ15643.
CleanExiHS_TRIP11.
ExpressionAtlasiQ15643. baseline and differential.
GenevisibleiQ15643. HS.

Organism-specific databases

HPAiHPA002570.

Interactioni

Subunit structurei

Binds RB1.

Protein-protein interaction databases

BioGridi114732. 18 interactions.
DIPiDIP-40357N.
IntActiQ15643. 19 interactions.
MINTiMINT-2866314.
STRINGi9606.ENSP00000267622.

Structurei

3D structure databases

ProteinModelPortaliQ15643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1774 – 182350GRIPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili52 – 17731722Sequence analysisAdd
BLAST

Domaini

Extended rod-like protein with coiled-coil domains.

Sequence similaritiesi

Contains 1 GRIP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IF24. Eukaryota.
ENOG410XT0E. LUCA.
GeneTreeiENSGT00710000106769.
HOGENOMiHOG000168282.
HOVERGENiHBG079281.
InParanoidiQ15643.
OMAiKLVLACE.
OrthoDBiEOG7H791F.
PhylomeDBiQ15643.
TreeFamiTF351148.

Family and domain databases

InterProiIPR000237. GRIP.
[Graphical view]
PROSITEiPS50913. GRIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q15643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSWLGGLGS GLGQSLGQVG GSLASLTGQI SNFTKDMLME GTEEVEAELP
60 70 80 90 100
DSRTKEIEAI HAILRSENER LKKLCTDLEE KHEASEIQIK QQSTSYRNQL
110 120 130 140 150
QQKEVEISHL KARQIALQDQ LLKLQSAAQS VPSGAGVPAT TASSSFAYGI
160 170 180 190 200
SHHPSAFHDD DMDFGDIISS QQEINRLSNE VSRLESEVGH WRHIAQTSKA
210 220 230 240 250
QGTDNSDQSE ICKLQNIIKE LKQNRSQEID DHQHEMSVLQ NAHQQKLTEI
260 270 280 290 300
SRRHREELSD YEERIEELEN LLQQGGSGVI ETDLSKIYEM QKTIQVLQIE
310 320 330 340 350
KVESTKKMEQ LEDKIKDINK KLSSAENDRD ILRREQEQLN VEKRQIMEEC
360 370 380 390 400
ENLKLECSKL QPSAVKQSDT MTEKERILAQ SASVEEVFRL QQALSDAENE
410 420 430 440 450
IMRLSSLNQD NSLAEDNLKL KMRIEVLEKE KSLLSQEKEE LQMSLLKLNN
460 470 480 490 500
EYEVIKSTAT RDISLDSELH DLRLNLEAKE QELNQSISEK ETLIAEIEEL
510 520 530 540 550
DRQNQEATKH MILIKDQLSK QQNEGDSIIS KLKQDLNDEK KRVHQLEDDK
560 570 580 590 600
MDITKELDVQ KEKLIQSEVA LNDLHLTKQK LEDKVENLVD QLNKSQESNV
610 620 630 640 650
SIQKENLELK EHIRQNEEEL SRIRNELMQS LNQDSNSNFK DTLLKEREAE
660 670 680 690 700
VRNLKQNLSE LEQLNENLKK VAFDVKMENE KLVLACEDVR HQLEECLAGN
710 720 730 740 750
NQLSLEKNTI VETLKMEKGE IEAELCWAKK RLLEEANKYE KTIEELSNAR
760 770 780 790 800
NLNTSALQLE HEHLIKLNQK KDMEIAELKK NIEQMDTDHK ETKDVLSSSL
810 820 830 840 850
EEQKQLTQLI NKKEIFIEKL KERSSKLQEE LDKYSQALRK NEILRQTIEE
860 870 880 890 900
KDRSLGSMKE ENNHLQEELE RLREEQSRTA PVADPKTLDS VTELASEVSQ
910 920 930 940 950
LNTIKEHLEE EIKHHQKIIE DQNQSKMQLL QSLQEQKKEM DEFRYQHEQM
960 970 980 990 1000
NATHTQLFLE KDEEIKSLQK TIEQIKTQLH EERQDIQTDN SDIFQETKVQ
1010 1020 1030 1040 1050
SLNIENGSEK HDLSKAETER LVKGIKEREL EIKLLNEKNI SLTKQIDQLS
1060 1070 1080 1090 1100
KDEVGKLTQI IQQKDLEIQA LHARISSTSH TQDVVYLQQQ LQAYAMEREK
1110 1120 1130 1140 1150
VFAVLNEKTR ENSHLKTEYH KMMDIVAAKE AALIKLQDEN KKLSTRFESS
1160 1170 1180 1190 1200
GQDMFRETIQ NLSRIIREKD IEIDALSQKC QTLLAVLQTS STGNEAGGVN
1210 1220 1230 1240 1250
SNQFEELLQE RDKLKQQVKK MEEWKQQVMT TVQNMQHESA QLQEELHQLQ
1260 1270 1280 1290 1300
AQVLVDSDNN SKLQVDYTGL IQSYEQNETK LKNFGQELAQ VQHSIGQLCN
1310 1320 1330 1340 1350
TKDLLLGKLD IISPQLSSAS LLTPQSAECL RASKSEVLSE SSELLQQELE
1360 1370 1380 1390 1400
ELRKSLQEKD ATIRTLQENN HRLSDSIAAT SELERKEHEQ TDSEIKQLKE
1410 1420 1430 1440 1450
KQDVLQKLLK EKDLLIKAKS DQLLSSNENF TNKVNENELL RQAVTNLKER
1460 1470 1480 1490 1500
ILILEMDIGK LKGENEKIVE TYRGKETEYQ ALQETNMKFS MMLREKEFEC
1510 1520 1530 1540 1550
HSMKEKALAF EQLLKEKEQG KTGELNQLLN AVKSMQEKTV VFQQERDQVM
1560 1570 1580 1590 1600
LALKQKQMEN TALQNEVQRL RDKEFRSNQE LERLRNHLLE SEDSYTREAL
1610 1620 1630 1640 1650
AAEDREAKLR KKVTVLEEKL VSSSNAMENA SHQASVQVES LQEQLNVVSK
1660 1670 1680 1690 1700
QRDETALQLS VSQEQVKQYA LSLANLQMVL EHFQQEEKAM YSAELEKQKQ
1710 1720 1730 1740 1750
LIAEWKKNAE NLEGKVISLQ ECLDEANAAL DSASRLTEQL DVKEEQIEEL
1760 1770 1780 1790 1800
KRQNELRQEM LDDVQKKLMS LANSSEGKVD KVLMRNLFIG HFHTPKNQRH
1810 1820 1830 1840 1850
EVLRLMGSIL GVRREEMEQL FHDDQGGVTR WMTGWLGGGS KSVPNTPLRP
1860 1870 1880 1890 1900
NQQSVVNSSF SELFVKFLET ESHPSIPPPK LSVHDMKPLD SPGRRKRDTN
1910 1920 1930 1940 1950
APESFKDTAE SRSGRRTDVN PFLAPRSAAV PLINPAGLGP GGPGHLLLKP
1960 1970
ISDVLPTFTP LPALPDNSAG VVLKDLLKQ
Length:1,979
Mass (Da):227,586
Last modified:March 23, 2010 - v3
Checksum:i437EB5F5966BB1AE
GO

Sequence cautioni

The sequence AAB84386.1 differs from that shown. Reason: Frameshift at positions 1932 and 1955. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211L → F in AAD09135 (PubMed:9256431).Curated
Sequence conflicti382 – 3821A → G in AAD09135 (PubMed:9256431).Curated
Sequence conflicti391 – 3911Q → R in AAD09135 (PubMed:9256431).Curated
Sequence conflicti516 – 5161D → A in AAD09135 (PubMed:9256431).Curated
Sequence conflicti561 – 5633KEK → FVL in AAD09135 (PubMed:9256431).Curated
Sequence conflicti1202 – 12021N → H (PubMed:10189370).Curated
Sequence conflicti1237 – 12371H → R in AAB84386 (PubMed:9373237).Curated
Sequence conflicti1346 – 13472QQ → HE in AAB84386 (PubMed:9373237).Curated
Sequence conflicti1658 – 16658QLSVSQEQ → RFCLSGT in AAD09135 (PubMed:9256431).Curated
Sequence conflicti1670 – 16701A → R in AAD09135 (PubMed:9256431).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391M → L.1 Publication
Corresponds to variant rs17127898 [ dbSNP | Ensembl ].
VAR_055861
Natural varianti506 – 5061E → A.
Corresponds to variant rs2273186 [ dbSNP | Ensembl ].
VAR_055862
Natural varianti795 – 7951V → L.
Corresponds to variant rs34699762 [ dbSNP | Ensembl ].
VAR_055863
Natural varianti884 – 8841D → G.
Corresponds to variant rs34967261 [ dbSNP | Ensembl ].
VAR_055864
Natural varianti1040 – 10401I → V.
Corresponds to variant rs34805848 [ dbSNP | Ensembl ].
VAR_055865
Natural varianti1107 – 11071E → D.
Corresponds to variant rs4619320 [ dbSNP | Ensembl ].
VAR_060344
Natural varianti1413 – 14131D → A.
Corresponds to variant rs12884523 [ dbSNP | Ensembl ].
VAR_060345
Natural varianti1503 – 15031M → V.
Corresponds to variant rs34839498 [ dbSNP | Ensembl ].
VAR_055866
Natural varianti1576 – 15761R → H.
Corresponds to variant rs35007347 [ dbSNP | Ensembl ].
VAR_055867
Natural varianti1749 – 17491E → A.
Corresponds to variant rs2273183 [ dbSNP | Ensembl ].
VAR_055868
Natural varianti1752 – 17521R → K.
Corresponds to variant rs11851376 [ dbSNP | Ensembl ].
VAR_055869
Natural varianti1827 – 18271G → S.4 Publications
Corresponds to variant rs1051340 [ dbSNP | Ensembl ].
VAR_060346
Natural varianti1846 – 18461T → I.1 Publication
Corresponds to variant rs141259390 [ dbSNP | Ensembl ].
VAR_054151

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007217 mRNA. Translation: AAD09135.1.
Y12490 mRNA. Translation: CAA73095.1.
AL049872 Genomic DNA. No translation available.
BC146845 mRNA. Translation: AAI46846.1.
AF011368 mRNA. Translation: AAB84386.1. Frameshift.
L40380 mRNA. Translation: AAC41730.1. Sequence problems.
CCDSiCCDS9899.1.
PIRiT03719.
RefSeqiNP_004230.2. NM_004239.3.
UniGeneiHs.632339.
Hs.741740.

Genome annotation databases

EnsembliENST00000267622; ENSP00000267622; ENSG00000100815.
GeneIDi9321.
KEGGihsa:9321.
UCSCiuc001xzy.4. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007217 mRNA. Translation: AAD09135.1.
Y12490 mRNA. Translation: CAA73095.1.
AL049872 Genomic DNA. No translation available.
BC146845 mRNA. Translation: AAI46846.1.
AF011368 mRNA. Translation: AAB84386.1. Frameshift.
L40380 mRNA. Translation: AAC41730.1. Sequence problems.
CCDSiCCDS9899.1.
PIRiT03719.
RefSeqiNP_004230.2. NM_004239.3.
UniGeneiHs.632339.
Hs.741740.

3D structure databases

ProteinModelPortaliQ15643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114732. 18 interactions.
DIPiDIP-40357N.
IntActiQ15643. 19 interactions.
MINTiMINT-2866314.
STRINGi9606.ENSP00000267622.

PTM databases

iPTMnetiQ15643.
PhosphoSiteiQ15643.

Polymorphism and mutation databases

BioMutaiTRIP11.
DMDMi292495059.

Proteomic databases

EPDiQ15643.
MaxQBiQ15643.
PaxDbiQ15643.
PRIDEiQ15643.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267622; ENSP00000267622; ENSG00000100815.
GeneIDi9321.
KEGGihsa:9321.
UCSCiuc001xzy.4. human.

Organism-specific databases

CTDi9321.
GeneCardsiTRIP11.
H-InvDBHIX0202079.
HGNCiHGNC:12305. TRIP11.
HPAiHPA002570.
MalaCardsiTRIP11.
MIMi200600. phenotype.
604505. gene.
neXtProtiNX_Q15643.
Orphaneti93299. Achondrogenesis type 1A.
PharmGKBiPA36984.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF24. Eukaryota.
ENOG410XT0E. LUCA.
GeneTreeiENSGT00710000106769.
HOGENOMiHOG000168282.
HOVERGENiHBG079281.
InParanoidiQ15643.
OMAiKLVLACE.
OrthoDBiEOG7H791F.
PhylomeDBiQ15643.
TreeFamiTF351148.

Enzyme and pathway databases

ReactomeiR-HSA-5620924. Intraflagellar transport.

Miscellaneous databases

GeneWikiiTRIP11.
GenomeRNAii9321.
NextBioi34917.
PROiQ15643.
SOURCEiSearch...

Gene expression databases

BgeeiQ15643.
CleanExiHS_TRIP11.
ExpressionAtlasiQ15643. baseline and differential.
GenevisibleiQ15643. HS.

Family and domain databases

InterProiIPR000237. GRIP.
[Graphical view]
PROSITEiPS50913. GRIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A thyroid hormone receptor coactivator negatively regulated by the retinoblastoma protein."
    Chang K.-H., Chen Y., Chen T.-T., Chou W.-H., Chen P.-L., Ma Y.-T., Yang-Feng T.L., Leng L., Tsai M.-J., O'Malley B.W., Lee W.-H.
    Proc. Natl. Acad. Sci. U.S.A. 94:9040-9045(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RB1 AND THRB.
    Tissue: Fibroblast.
  2. "GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein."
    Infante C., Ramos-Morales F., Fedriani F., Bornens M., Rios R.M.
    J. Cell Biol. 145:83-98(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH MICROTUBULES, VARIANT SER-1827.
    Tissue: Cervix carcinoma.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS LEU-39 AND SER-1827.
    Tissue: Brain.
  5. "Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution."
    Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.
    Blood 90:4271-4277(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1188-1979, CHROMOSOMAL TRANSLOCATION WITH PDGFRB, TISSUE SPECIFICITY, VARIANT SER-1827.
    Tissue: Leukemia.
  6. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
    Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
    Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1757-1944, INTERACTION WITH THRB, VARIANT SER-1827.
    Tissue: Cervix carcinoma.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1891, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-1842 AND THR-1846, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 SER-1842 AND THR-1846, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: INVOLVEMENT IN ACG1A.
  12. "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-464 AND SER-1842, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-1846.

Entry informationi

Entry nameiTRIPB_HUMAN
AccessioniPrimary (citable) accession number: Q15643
Secondary accession number(s): B2RUT2
, O14689, O15154, O95949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 23, 2010
Last modified: May 11, 2016
This is version 147 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

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.