Q15643 (TRIPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRIP11
Synonyms:	CEV14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1979 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2
Subunit structure	Binds RB1.
Subcellular location	Golgi apparatus › cis-Golgi network membrane; Peripheral membrane protein. Cytoplasm › cytoskeleton. Note: Associates with the ends of centrosome-nucleated microtubules. Ref.2
Tissue specificity	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. Ref.2 Ref.4
Domain	Extended rod-like protein with coiled-coil domains.
Involvement in disease	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) [MIM:200600]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9
Sequence similarities	Contains 1 GRIP domain.
Sequence caution	The sequence AAB84386.1 differs from that shown. Reason: Frameshift at positions 1932 and 1955.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Golgi apparatus Membrane
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Dwarfism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein targeting to Golgi Inferred from electronic annotation. Source: InterPro transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA
Molecular_function	transcription coactivator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1979	1979	Thyroid receptor-interacting protein 11		PRO_0000190076
Regions
	Domain	1774 – 1823	50	GRIP
	Coiled coil	52 – 1773	1722	Potential
Sites
	Site	1754 – 1755	2	Breakpoint for translocation to form TRIP11-PDGFRB
Amino acid modifications
	Modified residue	464	1	Phosphoserine Ref.7 Ref.10
	Modified residue	1842	1	Phosphoserine Ref.7 Ref.8 Ref.10
	Modified residue	1846	1	Phosphothreonine Ref.7 Ref.8
	Modified residue	1891	1	Phosphoserine Ref.6
Natural variations
	Natural variant	39	1	M → L. Corresponds to variant rs17127898 [ dbSNP | Ensembl ].		VAR_055861
	Natural variant	506	1	E → A. Corresponds to variant rs2273186 [ dbSNP | Ensembl ].		VAR_055862
	Natural variant	795	1	V → L. Corresponds to variant rs34699762 [ dbSNP | Ensembl ].		VAR_055863
	Natural variant	884	1	D → G. Corresponds to variant rs34967261 [ dbSNP | Ensembl ].		VAR_055864
	Natural variant	1040	1	I → V. Corresponds to variant rs34805848 [ dbSNP | Ensembl ].		VAR_055865
	Natural variant	1107	1	E → D. Corresponds to variant rs4619320 [ dbSNP | Ensembl ].		VAR_060344
	Natural variant	1413	1	D → A. Corresponds to variant rs12884523 [ dbSNP | Ensembl ].		VAR_060345
	Natural variant	1503	1	M → V. Corresponds to variant rs34839498 [ dbSNP | Ensembl ].		VAR_055866
	Natural variant	1576	1	R → H. Corresponds to variant rs35007347 [ dbSNP | Ensembl ].		VAR_055867
	Natural variant	1749	1	E → A. Corresponds to variant rs2273183 [ dbSNP | Ensembl ].		VAR_055868
	Natural variant	1752	1	R → K. Corresponds to variant rs11851376 [ dbSNP | Ensembl ].		VAR_055869
	Natural variant	1827	1	G → S. Ref.2 Ref.4 Ref.5 Corresponds to variant rs1051340 [ dbSNP | Ensembl ].		VAR_060346
	Natural variant	1846	1	T → I. Ref.12		VAR_054151
Experimental info
	Sequence conflict	121	1	L → F in AAD09135. Ref.1
	Sequence conflict	382	1	A → G in AAD09135. Ref.1
	Sequence conflict	391	1	Q → R in AAD09135. Ref.1
	Sequence conflict	516	1	D → A in AAD09135. Ref.1
	Sequence conflict	561 – 563	3	KEK → FVL in AAD09135. Ref.1
	Sequence conflict	1202	1	N → H Ref.2
	Sequence conflict	1237	1	H → R in AAB84386. Ref.4
	Sequence conflict	1346 – 1347	2	QQ → HE in AAB84386. Ref.4
	Sequence conflict	1658 – 1665	8	QLSVSQEQ → RFCLSGT in AAD09135. Ref.1
	Sequence conflict	1670	1	A → R in AAD09135. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q15643 [UniParc]. Last modified March 23, 2010. Version 3. Checksum: 437EB5F5966BB1AE	FASTA	1,979	227,586
	10 20 30 40 50 60 MSSWLGGLGS GLGQSLGQVG GSLASLTGQI SNFTKDMLME GTEEVEAELP DSRTKEIEAI 70 80 90 100 110 120 HAILRSENER LKKLCTDLEE KHEASEIQIK QQSTSYRNQL QQKEVEISHL KARQIALQDQ 130 140 150 160 170 180 LLKLQSAAQS VPSGAGVPAT TASSSFAYGI SHHPSAFHDD DMDFGDIISS QQEINRLSNE 190 200 210 220 230 240 VSRLESEVGH WRHIAQTSKA QGTDNSDQSE ICKLQNIIKE LKQNRSQEID DHQHEMSVLQ 250 260 270 280 290 300 NAHQQKLTEI SRRHREELSD YEERIEELEN LLQQGGSGVI ETDLSKIYEM QKTIQVLQIE 310 320 330 340 350 360 KVESTKKMEQ LEDKIKDINK KLSSAENDRD ILRREQEQLN VEKRQIMEEC ENLKLECSKL 370 380 390 400 410 420 QPSAVKQSDT MTEKERILAQ SASVEEVFRL QQALSDAENE IMRLSSLNQD NSLAEDNLKL 430 440 450 460 470 480 KMRIEVLEKE KSLLSQEKEE LQMSLLKLNN EYEVIKSTAT RDISLDSELH DLRLNLEAKE 490 500 510 520 530 540 QELNQSISEK ETLIAEIEEL DRQNQEATKH MILIKDQLSK QQNEGDSIIS KLKQDLNDEK 550 560 570 580 590 600 KRVHQLEDDK MDITKELDVQ KEKLIQSEVA LNDLHLTKQK LEDKVENLVD QLNKSQESNV 610 620 630 640 650 660 SIQKENLELK EHIRQNEEEL SRIRNELMQS LNQDSNSNFK DTLLKEREAE VRNLKQNLSE 670 680 690 700 710 720 LEQLNENLKK VAFDVKMENE KLVLACEDVR HQLEECLAGN NQLSLEKNTI VETLKMEKGE 730 740 750 760 770 780 IEAELCWAKK RLLEEANKYE KTIEELSNAR NLNTSALQLE HEHLIKLNQK KDMEIAELKK 790 800 810 820 830 840 NIEQMDTDHK ETKDVLSSSL EEQKQLTQLI NKKEIFIEKL KERSSKLQEE LDKYSQALRK 850 860 870 880 890 900 NEILRQTIEE KDRSLGSMKE ENNHLQEELE RLREEQSRTA PVADPKTLDS VTELASEVSQ 910 920 930 940 950 960 LNTIKEHLEE EIKHHQKIIE DQNQSKMQLL QSLQEQKKEM DEFRYQHEQM NATHTQLFLE 970 980 990 1000 1010 1020 KDEEIKSLQK TIEQIKTQLH EERQDIQTDN SDIFQETKVQ SLNIENGSEK HDLSKAETER 1030 1040 1050 1060 1070 1080 LVKGIKEREL EIKLLNEKNI SLTKQIDQLS KDEVGKLTQI IQQKDLEIQA LHARISSTSH 1090 1100 1110 1120 1130 1140 TQDVVYLQQQ LQAYAMEREK VFAVLNEKTR ENSHLKTEYH KMMDIVAAKE AALIKLQDEN 1150 1160 1170 1180 1190 1200 KKLSTRFESS GQDMFRETIQ NLSRIIREKD IEIDALSQKC QTLLAVLQTS STGNEAGGVN 1210 1220 1230 1240 1250 1260 SNQFEELLQE RDKLKQQVKK MEEWKQQVMT TVQNMQHESA QLQEELHQLQ AQVLVDSDNN 1270 1280 1290 1300 1310 1320 SKLQVDYTGL IQSYEQNETK LKNFGQELAQ VQHSIGQLCN TKDLLLGKLD IISPQLSSAS 1330 1340 1350 1360 1370 1380 LLTPQSAECL RASKSEVLSE SSELLQQELE ELRKSLQEKD ATIRTLQENN HRLSDSIAAT 1390 1400 1410 1420 1430 1440 SELERKEHEQ TDSEIKQLKE KQDVLQKLLK EKDLLIKAKS DQLLSSNENF TNKVNENELL 1450 1460 1470 1480 1490 1500 RQAVTNLKER ILILEMDIGK LKGENEKIVE TYRGKETEYQ ALQETNMKFS MMLREKEFEC 1510 1520 1530 1540 1550 1560 HSMKEKALAF EQLLKEKEQG KTGELNQLLN AVKSMQEKTV VFQQERDQVM LALKQKQMEN 1570 1580 1590 1600 1610 1620 TALQNEVQRL RDKEFRSNQE LERLRNHLLE SEDSYTREAL AAEDREAKLR KKVTVLEEKL 1630 1640 1650 1660 1670 1680 VSSSNAMENA SHQASVQVES LQEQLNVVSK QRDETALQLS VSQEQVKQYA LSLANLQMVL 1690 1700 1710 1720 1730 1740 EHFQQEEKAM YSAELEKQKQ LIAEWKKNAE NLEGKVISLQ ECLDEANAAL DSASRLTEQL 1750 1760 1770 1780 1790 1800 DVKEEQIEEL KRQNELRQEM LDDVQKKLMS LANSSEGKVD KVLMRNLFIG HFHTPKNQRH 1810 1820 1830 1840 1850 1860 EVLRLMGSIL GVRREEMEQL FHDDQGGVTR WMTGWLGGGS KSVPNTPLRP NQQSVVNSSF 1870 1880 1890 1900 1910 1920 SELFVKFLET ESHPSIPPPK LSVHDMKPLD SPGRRKRDTN APESFKDTAE SRSGRRTDVN 1930 1940 1950 1960 1970 PFLAPRSAAV PLINPAGLGP GGPGHLLLKP ISDVLPTFTP LPALPDNSAG VVLKDLLKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[5]	"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.
[6]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-1842 AND THR-1846, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210." Smits P., Bolton A.D., Funari V., Hong M., Boyden E.D., Lu L., Manning D.K., Dwyer N.D., Moran J.L., Prysak M., Merriman B., Nelson S.F., Bonafe L., Superti-Furga A., Ikegawa S., Krakow D., Cohn D.H., Kirchhausen T., Warman M.L., Beier D.R. N. Engl. J. Med. 362:206-216(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ACG1A.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-1846.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF007217 mRNA. Translation: AAD09135.1. Y12490 mRNA. Translation: CAA73095.1. AL049872 Genomic DNA. No translation available. AF011368 mRNA. Translation: AAB84386.1. Frameshift. L40380 mRNA. Translation: AAC41730.1. Sequence problems.
IPI	IPI00003515.
PIR	T03719.
RefSeq	NP_004230.2. NM_004239.3.
UniGene	Hs.632339. Hs.741740.
3D structure databases
ProteinModelPortal	Q15643.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-40357N.
IntAct	Q15643. 8 interactions.
MINT	MINT-2866314.
STRING	9606.ENSP00000267622.
PTM databases
PhosphoSite	Q15643.
Polymorphism databases
DMDM	292495059.
Proteomic databases
PaxDb	Q15643.
PRIDE	Q15643.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000267622; ENSP00000267622; ENSG00000100815.
GeneID	9321.
KEGG	hsa:9321.
UCSC	uc001xzy.3. human.
Organism-specific databases
CTD	9321.
GeneCards	GC14M092435.
H-InvDB	HIX0202079.
HGNC	HGNC:12305. TRIP11.
HPA	HPA002570.
MIM	200600. phenotype. 604505. gene.
neXtProt	NX_Q15643.
Orphanet	93299. Achondrogenesis type 1A.
PharmGKB	PA36984.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000168282.
HOVERGEN	HBG079281.
InParanoid	Q15643.
OMA	IEAELCW.
OrthoDB	EOG4229HV.
PhylomeDB	Q15643.
Gene expression databases
ArrayExpress	Q15643.
Bgee	Q15643.
CleanEx	HS_TRIP11.
Genevestigator	Q15643.
GermOnline	ENSG00000100815. Homo sapiens.
Family and domain databases
InterPro	IPR000237. GRIP. [Graphical view]
PROSITE	PS50913. GRIP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9321.
NextBio	34917.
SOURCE	Search...

Entry information

Entry name

TRIPB_HUMAN

Accession

Primary (citable) accession number: Q15643
Secondary accession number(s): O14689, O15154, O95949

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 23, 2010
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.