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Protein

E3 ubiquitin-protein ligase TRIP12

Gene

TRIP12

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

Functioni

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1959 – 19591Glycyl thioester intermediateCurated

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • thyroid hormone receptor binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • embryo development Source: UniProtKB
  • negative regulation of double-strand break repair Source: UniProtKB
  • negative regulation of histone H2A K63-linked ubiquitination Source: UniProtKB
  • protein polyubiquitination Source: Reactome
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B9. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIP12 (EC:6.3.2.-)
Alternative name(s):
E3 ubiquitin-protein ligase for Arf
Short name:
ULF
Thyroid receptor-interacting protein 12
Short name:
TR-interacting protein 12
Short name:
TRIP-12
Gene namesi
Name:TRIP12
Synonyms:KIAA0045, ULF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12306. TRIP12.

Subcellular locationi

  • Nucleusnucleoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1959 – 19591C → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA36985.

Polymorphism and mutation databases

DMDMi2499839.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 19921991E3 ubiquitin-protein ligase TRIP12PRO_0000173872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei77 – 771PhosphoserineCombined sources
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei181 – 1811N6-acetyllysineBy similarity
Modified residuei310 – 3101PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei942 – 9421PhosphoserineCombined sources
Modified residuei991 – 9911PhosphoserineCombined sources
Modified residuei997 – 9971PhosphoserineCombined sources
Modified residuei1016 – 10161PhosphoserineBy similarity
Modified residuei1030 – 10301PhosphoserineCombined sources
Modified residuei1317 – 13171PhosphoserineCombined sources
Modified residuei1322 – 13221PhosphoserineCombined sources
Modified residuei1329 – 13291PhosphoserineBy similarity
Modified residuei1376 – 13761PhosphoserineBy similarity
Modified residuei1377 – 13771PhosphothreonineBy similarity
Modified residuei1425 – 14251N6-acetyllysineBy similarity
Modified residuei1427 – 14271PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14669.
MaxQBiQ14669.
PaxDbiQ14669.
PRIDEiQ14669.

PTM databases

iPTMnetiQ14669.
PhosphoSiteiQ14669.

Expressioni

Gene expression databases

BgeeiQ14669.
CleanExiHS_TRIP12.
ExpressionAtlasiQ14669. baseline and differential.
GenevisibleiQ14669. HS.

Organism-specific databases

HPAiHPA036835.
HPA045893.

Interactioni

Subunit structurei

Interacts with MYC; leading to disrupt interaction with isoform p19ARF/ARF of CDKN2A. Interacts with TRADD; leading to disrupt interaction with isoform p19ARF/ARF of CDKN2A. Interacts with SMARCC1; leading to disrupt interaction with SMARCE1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MTNR1BP492863EBI-308443,EBI-1188341

GO - Molecular functioni

  • thyroid hormone receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114731. 52 interactions.
DIPiDIP-58584N.
IntActiQ14669. 26 interactions.
MINTiMINT-1192877.
STRINGi9606.ENSP00000283943.

Structurei

3D structure databases

ProteinModelPortaliQ14669.
SMRiQ14669. Positions 441-669, 1585-1986.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini749 – 83688WWEPROSITE-ProRule annotationAdd
BLAST
Domaini1885 – 1992108HECTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1496 – 157075K-boxAdd
BLAST

Sequence similaritiesi

Belongs to the UPL family. K-HECT subfamily.Curated
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 1 WWE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0168. Eukaryota.
KOG0170. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00530000063470.
HOGENOMiHOG000007873.
HOVERGENiHBG062085.
InParanoidiQ14669.
KOiK10590.
OMAiTHFDISH.
OrthoDBiEOG7H791G.
PhylomeDBiQ14669.
TreeFamiTF323674.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000569. HECT_dom.
IPR004170. WWE-dom.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q14669-1) [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
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSCSSSSA VIVPQPEDPD
60 70 80 90 100
RANTSERQKT GQVPKKDNSR GVKRSASPDY NRTNSPSSAK KPKALQHTES
110 120 130 140 150
PSETNKPHSK SKKRHLDQEQ QLKSAQSPST SKAHTRKSGA TGGSRSQKRK
160 170 180 190 200
RTESSCVKSG SGSESTGAEE RSAKPTKLAS KSATSAKAGC STITDSSSAA
210 220 230 240 250
STSSSSSAVA SASSTVPPGA RVKQGKDQNK ARRSRSASSP SPRRSSREKE
260 270 280 290 300
QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSETSKP GPSGLQAKLA
310 320 330 340 350
SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASTSRRGS GLGKRGAAEA
360 370 380 390 400
RRQEKMADPE SNQEAVNSSA ARTDEAPQGA AGAVGMTTSG ESESDDSEMG
410 420 430 440 450
RLQALLEARG LPPHLFGPLG PRMSQLFHRT IGSGASSKAQ QLLQGLQASD
460 470 480 490 500
ESQQLQAVIE MCQLLVMGNE ETLGGFPVKS VVPALITLLQ MEHNFDIMNH
510 520 530 540 550
ACRALTYMME ALPRSSAVVV DAIPVFLEKL QVIQCIDVAE QALTALEMLS
560 570 580 590 600
RRHSKAILQA GGLADCLLYL EFFSINAQRN ALAIAANCCQ SITPDEFHFV
610 620 630 640 650
ADSLPLLTQR LTHQDKKSVE STCLCFARLV DNFQHEENLL QQVASKDLLT
660 670 680 690 700
NVQQLLVVTP PILSSGMFIM VVRMFSLMCS NCPTLAVQLM KQNIAETLHF
710 720 730 740 750
LLCGASNGSC QEQIDLVPRS PQELYELTSL ICELMPCLPK EGIFAVDTML
760 770 780 790 800
KKGNAQNTDG AIWQWRDDRG LWHPYNRIDS RIIEQINEDT GTARAIQRKP
810 820 830 840 850
NPLANSNTSG YSESKKDDAR AQLMKEDPEL AKSFIKTLFG VLYEVYSSSA
860 870 880 890 900
GPAVRHKCLR AILRIIYFAD AELLKDVLKN HAVSSHIASM LSSQDLKIVV
910 920 930 940 950
GALQMAEILM QKLPDIFSVY FRREGVMHQV KHLAESESLL TSPPKACTNG
960 970 980 990 1000
SGSMGSTTSV SSGTATAATH AAADLGSPSL QHSRDDSLDL SPQGRLSDVL
1010 1020 1030 1040 1050
KRKRLPKRGP RRPKYSPPRD DDKVDNQAKS PTTTQSPKSS FLASLNPKTW
1060 1070 1080 1090 1100
GRLSTQSNSN NIEPARTAGG SGLARAASKD TISNNREKIK GWIKEQAHKF
1110 1120 1130 1140 1150
VERYFSSENM DGSNPALNVL QRLCAATEQL NLQVDGGAEC LVEIRSIVSE
1160 1170 1180 1190 1200
SDVSSFEIQH SGFVKQLLLY LTSKSEKDAV SREIRLKRFL HVFFSSPLPG
1210 1220 1230 1240 1250
EEPIGRVEPV GNAPLLALVH KMNNCLSQME QFPVKVHDFP SGNGTGGSFS
1260 1270 1280 1290 1300
LNRGSQALKF FNTHQLKCQL QRHPDCANVK QWKGGPVKID PLALVQAIER
1310 1320 1330 1340 1350
YLVVRGYGRV REDDEDSDDD GSDEEIDESL AAQFLNSGNV RHRLQFYIGE
1360 1370 1380 1390 1400
HLLPYNMTVY QAVRQFSIQA EDERESTDDE SNPLGRAGIW TKTHTIWYKP
1410 1420 1430 1440 1450
VREDEESNKD CVGGKRGRAQ TAPTKTSPRN AKKHDELWHD GVCPSVSNPL
1460 1470 1480 1490 1500
EVYLIPTPPE NITFEDPSLD VILLLRVLHA ISRYWYYLYD NAMCKEIIPT
1510 1520 1530 1540 1550
SEFINSKLTA KANRQLQDPL VIMTGNIPTW LTELGKTCPF FFPFDTRQML
1560 1570 1580 1590 1600
FYVTAFDRDR AMQRLLDTNP EINQSDSQDS RVAPRLDRKK RTVNREELLK
1610 1620 1630 1640 1650
QAESVMQDLG SSRAMLEIQY ENEVGTGLGP TLEFYALVSQ ELQRADLGLW
1660 1670 1680 1690 1700
RGEEVTLSNP KGSQEGTKYI QNLQGLFALP FGRTAKPAHI AKVKMKFRFL
1710 1720 1730 1740 1750
GKLMAKAIMD FRLVDLPLGL PFYKWMLRQE TSLTSHDLFD IDPVVARSVY
1760 1770 1780 1790 1800
HLEDIVRQKK RLEQDKSQTK ESLQYALETL TMNGCSVEDL GLDFTLPGFP
1810 1820 1830 1840 1850
NIELKKGGKD IPVTIHNLEE YLRLVIFWAL NEGVSRQFDS FRDGFESVFP
1860 1870 1880 1890 1900
LSHLQYFYPE ELDQLLCGSK ADTWDAKTLM ECCRPDHGYT HDSRAVKFLF
1910 1920 1930 1940 1950
EILSSFDNEQ QRLFLQFVTG SPRLPVGGFR SLNPPLTIVR KTFESTENPD
1960 1970 1980 1990
DFLPSVMTCV NYLKLPDYSS IEIMREKLLI AAREGQQSFH LS
Length:1,992
Mass (Da):220,434
Last modified:November 1, 1997 - v1
Checksum:i294A7C063A3332DE
GO
Isoform 2 (identifier: Q14669-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-380: A → AAASSSV
     784-784: E → EAAHQVGEDEISLSTLGRVYTIDFNSMQ

Show »
Length:2,025
Mass (Da):223,900
Checksum:iCCC35A77D4040B85
GO
Isoform 3 (identifier: Q14669-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-32: G → GRSHLGQAKHKGYSPPESRKSNSKAPKVQSNTTSELSRGHLSK
     380-380: A → AAASSSV

Note: No experimental confirmation available.
Show »
Length:2,040
Mass (Da):225,520
Checksum:i8038779A69BBE66B
GO
Isoform 4 (identifier: Q14669-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-335: Missing.
     380-380: A → AAASSSV
     784-784: E → EAAHQVGEDEISLSTLGRVYTIDFNSMQ

Note: No experimental confirmation available.
Show »
Length:1,722
Mass (Da):192,075
Checksum:iDF23E5E19D306C51
GO

Sequence cautioni

The sequence AAY14681.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAY14755.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA05837.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1969 – 199224SSIEI…SFHLS → QALRYA in AAC41731 (PubMed:7776974).CuratedAdd
BLAST
Isoform 2 (identifier: Q14669-2)
Sequence conflicti380 – 3801A → T in ACC99349 (PubMed:20208519).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 321G → GRSHLGQAKHKGYSPPESRK SNSKAPKVQSNTTSELSRGH LSK in isoform 3. 1 PublicationVSP_044326
Alternative sequencei33 – 335303Missing in isoform 4. 1 PublicationVSP_044327Add
BLAST
Alternative sequencei380 – 3801A → AAASSSV in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_044328
Alternative sequencei784 – 7841E → EAAHQVGEDEISLSTLGRVY TIDFNSMQ in isoform 2 and isoform 4. 2 PublicationsVSP_044329

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU489742 mRNA. Translation: ACC99349.1.
D28476 mRNA. Translation: BAA05837.2. Different initiation.
AC009973 Genomic DNA. Translation: AAY14755.1. Sequence problems.
AC093384 Genomic DNA. Translation: AAY14681.1. Sequence problems.
AC105380 Genomic DNA. No translation available.
BC114556 mRNA. Translation: AAI14557.1.
BC113891 mRNA. Translation: AAI13892.1.
L40383 mRNA. Translation: AAC41731.1.
CCDSiCCDS33391.1. [Q14669-1]
CCDS63145.1. [Q14669-4]
CCDS63146.1. [Q14669-3]
RefSeqiNP_001271143.1. NM_001284214.1. [Q14669-3]
NP_001271144.1. NM_001284215.1. [Q14669-2]
NP_001271145.1. NM_001284216.1. [Q14669-4]
NP_004229.1. NM_004238.2. [Q14669-1]
XP_005247019.1. XM_005246962.3. [Q14669-2]
UniGeneiHs.572642.
Hs.591633.
Hs.601806.

Genome annotation databases

EnsembliENST00000283943; ENSP00000283943; ENSG00000153827. [Q14669-1]
ENST00000389044; ENSP00000373696; ENSG00000153827. [Q14669-3]
ENST00000389045; ENSP00000373697; ENSG00000153827. [Q14669-4]
GeneIDi9320.
KEGGihsa:9320.
UCSCiuc002vpw.3. human. [Q14669-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU489742 mRNA. Translation: ACC99349.1.
D28476 mRNA. Translation: BAA05837.2. Different initiation.
AC009973 Genomic DNA. Translation: AAY14755.1. Sequence problems.
AC093384 Genomic DNA. Translation: AAY14681.1. Sequence problems.
AC105380 Genomic DNA. No translation available.
BC114556 mRNA. Translation: AAI14557.1.
BC113891 mRNA. Translation: AAI13892.1.
L40383 mRNA. Translation: AAC41731.1.
CCDSiCCDS33391.1. [Q14669-1]
CCDS63145.1. [Q14669-4]
CCDS63146.1. [Q14669-3]
RefSeqiNP_001271143.1. NM_001284214.1. [Q14669-3]
NP_001271144.1. NM_001284215.1. [Q14669-2]
NP_001271145.1. NM_001284216.1. [Q14669-4]
NP_004229.1. NM_004238.2. [Q14669-1]
XP_005247019.1. XM_005246962.3. [Q14669-2]
UniGeneiHs.572642.
Hs.591633.
Hs.601806.

3D structure databases

ProteinModelPortaliQ14669.
SMRiQ14669. Positions 441-669, 1585-1986.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114731. 52 interactions.
DIPiDIP-58584N.
IntActiQ14669. 26 interactions.
MINTiMINT-1192877.
STRINGi9606.ENSP00000283943.

PTM databases

iPTMnetiQ14669.
PhosphoSiteiQ14669.

Polymorphism and mutation databases

DMDMi2499839.

Proteomic databases

EPDiQ14669.
MaxQBiQ14669.
PaxDbiQ14669.
PRIDEiQ14669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000283943; ENSP00000283943; ENSG00000153827. [Q14669-1]
ENST00000389044; ENSP00000373696; ENSG00000153827. [Q14669-3]
ENST00000389045; ENSP00000373697; ENSG00000153827. [Q14669-4]
GeneIDi9320.
KEGGihsa:9320.
UCSCiuc002vpw.3. human. [Q14669-1]

Organism-specific databases

CTDi9320.
GeneCardsiTRIP12.
HGNCiHGNC:12306. TRIP12.
HPAiHPA036835.
HPA045893.
MIMi604506. gene.
neXtProtiNX_Q14669.
PharmGKBiPA36985.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0168. Eukaryota.
KOG0170. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00530000063470.
HOGENOMiHOG000007873.
HOVERGENiHBG062085.
InParanoidiQ14669.
KOiK10590.
OMAiTHFDISH.
OrthoDBiEOG7H791G.
PhylomeDBiQ14669.
TreeFamiTF323674.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B9. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiTRIP12. human.
GeneWikiiTRIP12.
GenomeRNAii9320.
PROiQ14669.
SOURCEiSearch...

Gene expression databases

BgeeiQ14669.
CleanExiHS_TRIP12.
ExpressionAtlasiQ14669. baseline and differential.
GenevisibleiQ14669. HS.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000569. HECT_dom.
IPR004170. WWE-dom.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcription-independent ARF regulation in oncogenic stress-mediated p53 responses."
    Chen D., Shan J., Zhu W.G., Qin J., Gu W.
    Nature 464:624-627(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYC AND CDKN2A, MUTAGENESIS OF CYS-1959.
  2. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "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].
  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] (ISOFORMS 3 AND 4).
  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 1801-1992.
  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-1317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "TRIP12 functions as an E3 ubiquitin ligase of APP-BP1."
    Park Y., Yoon S.K., Yoon J.B.
    Biochem. Biophys. Res. Commun. 374:294-298(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-312; SER-991; SER-997; SER-1317 AND SER-1322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway."
    Park Y., Yoon S.K., Yoon J.B.
    J. Biol. Chem. 284:1540-1549(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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-312; SER-991; SER-1317 AND SER-1322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Ubiquitin-dependent and ubiquitin-independent control of subunit stoichiometry in the SWI/SNF complex."
    Keppler B.R., Archer T.K.
    J. Biol. Chem. 285:35665-35674(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMARCC1.
  14. "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-77; SER-312 AND SER-942, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-310; SER-1030; SER-1317 AND SER-1322, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: FUNCTION.
  18. "TRADD contributes to tumour suppression by regulating ULF-dependent p19Arf ubiquitylation."
    Chio I.I., Sasaki M., Ghazarian D., Moreno J., Done S., Ueda T., Inoue S., Chang Y.L., Chen N.J., Mak T.W.
    Nat. Cell Biol. 14:625-633(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRADD.
  19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1317 AND SER-1322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTRIPC_HUMAN
AccessioniPrimary (citable) accession number: Q14669
Secondary accession number(s): D4HL82
, Q14CA3, Q14CF1, Q15644, Q53R87, Q53TE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 149 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.