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Q12789

- TF3C1_HUMAN

UniProt

Q12789 - TF3C1_HUMAN

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Protein

General transcription factor 3C polypeptide 1

Gene

GTF3C1

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

Functioni

Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. 5S class rRNA transcription from RNA polymerase III type 1 promoter Source: HGNC
  2. gene expression Source: Reactome
  3. rRNA transcription Source: ProtInc
  4. transcription, DNA-templated Source: HGNC
  5. transcription from RNA polymerase III promoter Source: HGNC
  6. tRNA transcription Source: ProtInc
  7. tRNA transcription from RNA polymerase III promoter Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor 3C polypeptide 1
Alternative name(s):
TF3C-alpha
TFIIIC box B-binding subunit
Transcription factor IIIC 220 kDa subunit
Short name:
TFIIIC 220 kDa subunit
Short name:
TFIIIC220
Transcription factor IIIC subunit alpha
Gene namesi
Name:GTF3C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4664. GTF3C1.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleolus Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
  5. ribonucleoprotein complex Source: Ensembl
  6. transcription factor TFIIIC complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21092109General transcription factor 3C polypeptide 1PRO_0000209710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei667 – 6671Phosphoserine1 Publication
Modified residuei739 – 7391Phosphoserine2 Publications
Modified residuei1062 – 10621Phosphoserine3 Publications
Modified residuei1068 – 10681Phosphoserine4 Publications
Modified residuei1632 – 16321Phosphoserine2 Publications
Modified residuei1653 – 16531Phosphoserine3 Publications
Modified residuei1856 – 18561Phosphoserine1 Publication
Modified residuei1865 – 18651Phosphoserine3 Publications
Modified residuei1868 – 18681Phosphoserine3 Publications
Modified residuei1896 – 18961PhosphoserineBy similarity
Modified residuei1969 – 19691Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12789.
PaxDbiQ12789.
PRIDEiQ12789.

PTM databases

PhosphoSiteiQ12789.

Expressioni

Gene expression databases

BgeeiQ12789.
CleanExiHS_GTF3C1.
ExpressionAtlasiQ12789. baseline and differential.
GenevestigatoriQ12789.

Organism-specific databases

HPAiHPA051617.

Interactioni

Subunit structurei

Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts with IGHMBP2.1 Publication

Protein-protein interaction databases

BioGridi109230. 66 interactions.
DIPiDIP-38212N.
IntActiQ12789. 25 interactions.
MINTiMINT-1154812.
STRINGi9606.ENSP00000348510.

Structurei

3D structure databases

ProteinModelPortaliQ12789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi343 – 3519Asp/Glu-rich (acidic)
Compositional biasi1205 – 123329Arg/Lys-rich (basic)Add
BLAST
Compositional biasi1613 – 162412Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the TFIIIC subunit 1 family.Curated

Phylogenomic databases

eggNOGiNOG322015.
GeneTreeiENSGT00390000008664.
HOGENOMiHOG000154556.
HOVERGENiHBG057283.
InParanoidiQ12789.
KOiK15199.
OMAiEFLWRAL.
OrthoDBiEOG75J0MB.
PhylomeDBiQ12789.
TreeFamiTF351624.

Family and domain databases

InterProiIPR007309. TFIIIC_Bblock-bd.
[Graphical view]
PfamiPF04182. B-block_TFIIIC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12789-2) [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
MDALESLLDE VALEGLDGLC LPALWSRLET RVPPFPLPLE PCTQEFLWRA
60 70 80 90 100
LATHPGISFY EEPRERPDLQ LQDRYEEIDL ETGILESRRD PVALEDVYPI
110 120 130 140 150
HMILENKDGI QGSCRYFKER KNITNDIRTK SLQPRCTMVE AFDRWGKKLI
160 170 180 190 200
IVASQAMRYR ALIGQEGDPD LKLPDFSYCI LERLGRSRWQ GELQRDLHTT
210 220 230 240 250
AFKVDAGKLH YHRKILNKNG LITMQSHVIR LPTGAQQHSI LLLLNRFHVD
260 270 280 290 300
RRSKYDILME KLSVMLSTRT NHIETLGKLR EELGLCERTF KRLYQYMLNA
310 320 330 340 350
GLAKVVSLRL QEIHPECGPC KTKKGTDVMV RCLKLLKEFK RNDHDDDEDE
360 370 380 390 400
EVISKTVPPV DIVFERDMLT QTYDLIERRG TKGISQAEIR VAMNVGKLEA
410 420 430 440 450
RMLCRLLQRF KVVKGFMEDE GRQRTTKYIS CVFAEESDLS RQYQREKARS
460 470 480 490 500
ELLTTVSLAS MQEESLLPEG EDTFLSESDS EEERSSSKRR GRGSQKDTRA
510 520 530 540 550
SANLRPKTQP HHSTPTKGGW KVVNLHPLKK QPPSFPGAAE ERACQSLASR
560 570 580 590 600
DSLLDTSSVS EPNVSFVSHC ADSNSGDIAV IEEVRMENPK ESSSSLKTGR
610 620 630 640 650
HSSGQDKPHE TYRLLKRRNL IIEAVTNLRL IESLFTIQKM IMDQEKQEGV
660 670 680 690 700
STKCCKKSIV RLVRNLSEEG LLRLYRTTVI QDGIKKKVDL VVHPSMDQND
710 720 730 740 750
PLVRSAIEQV RFRISNSSTA NRVKTSQPPV PQGEAEEDSQ GKEGPSGSGD
760 770 780 790 800
SQLSASSRSE SGRMKKSDNK MGITPLRNYH PIVVPGLGRS LGFLPKMPRL
810 820 830 840 850
RVVHMFLWYL IYGHPASNTV EKPSFISERR TIKQESGRAG VRPSSSGSAW
860 870 880 890 900
EACSEAPSKG SQDGVTWEAE VELATETVYV DDASWMRYIP PIPVHRDFGF
910 920 930 940 950
GWALVSDILL CLPLSIFIQI VQVSYKVDNL EEFLNDPLKK HTLIRFLPRP
960 970 980 990 1000
IRQQLLYKRR YIFSVVENLQ RLCYMGLLQF GPTEKFQDKD QVFIFLKKNA
1010 1020 1030 1040 1050
VIVDTTICDP HYNLARSSRP FERRLYVLNS MQDVENYWFD LQCVCLNTPL
1060 1070 1080 1090 1100
GVVRCPRVRK NSSTDQGSDE EGSLQKEQES AMDKHNLERK CAMLEYTTGS
1110 1120 1130 1140 1150
REVVDEGLIP GDGLGAAGLD SSFYGHLKRN WIWTSYIINQ AKKENTAAEN
1160 1170 1180 1190 1200
GLTVRLQTFL SKRPMPLSAR GNSRLNIWGE ARVGSELCAG WEEQFEVDRE
1210 1220 1230 1240 1250
PSLDRNRRVR GGKSQKRKRL KKDPGKKIKR KKKGEFPGEK SKRLRYHDEA
1260 1270 1280 1290 1300
DQSALQRMTR LRVTWSMQED GLLVLCRIAS NVLNTKVKGP FVTWQVVRDI
1310 1320 1330 1340 1350
LHATFEESLD KTSHSVGRRA RYIVKNPQAY LNYKVCLAEV YQDKALVGDF
1360 1370 1380 1390 1400
MNRRGDYDDP KVCANEFKEF VEKLKEKFSS ALRNSNLEIP DTLQELFARY
1410 1420 1430 1440 1450
RVLAIGDEKD QTRKEDELNS VDDIHFLVLQ NLIQSTLALS DSQMKSYQSF
1460 1470 1480 1490 1500
QTFRLYREYK DHVLVKAFME CQKRSLVNRR RVNHTLGPKK NRALPFVPMS
1510 1520 1530 1540 1550
YQLSQTYYRI FTWRFPSTIC TESFQFLDRM RAAGKLDQPD RFSFKDQDNN
1560 1570 1580 1590 1600
EPTNDMVAFS LDGPGGNCVA VLTLFSLGLI SVDVRIPEQI IVVDSSMVEN
1610 1620 1630 1640 1650
EVIKSLGKDG SLEDDEDEED DLDEGVGGKR RSMEVKPAQA SHTNYLLMRG
1660 1670 1680 1690 1700
YYSPGIVSTR NLNPNDSIVV NSCQMKFQLR CTPVPARLRP AAAPLEELTM
1710 1720 1730 1740 1750
GTSCLPDTFT KLINPQENTC SLEEFVLQLE LSGYSPEDLT AALEILEAII
1760 1770 1780 1790 1800
ATGCFGIDKE ELRRRFSALE KAGGGRTRTF ADCIQALLEQ HQVLEVGGNT
1810 1820 1830 1840 1850
ARLVAMGSAW PWLLHSVRLK DREDADIQRE DPQARPLEGS SSEDSPPEGQ
1860 1870 1880 1890 1900
APPSHSPRGT KRRASWASEN GETDAEGTQM TPAKRPALQD SNLAPSLGPG
1910 1920 1930 1940 1950
AEDGAEAQAP SPPPALEDTA AAGAAQEDQE GVGEFSSPGQ EQLSGQAQPP
1960 1970 1980 1990 2000
EGSEDPRGFT ESFGAANISQ AARERDCESV CFIGRPWRVV DGHLNLPVCK
2010 2020 2030 2040 2050
GMMEAMLYHI MTRPGIPESS LLRHYQGVLQ PVAVLELLQG LESLGCIRKR
2060 2070 2080 2090 2100
WLRKPRPVSL FSTPVVEEVE VPSSLDESPM AFYEPTLDCT LRLGRVFPHE

VNWNKWIHL
Length:2,109
Mass (Da):238,875
Last modified:November 25, 2008 - v4
Checksum:i37A03135EFE695FC
GO
Isoform 2 (identifier: Q12789-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1933-1957: Missing.

Note: No experimental confirmation available.

Show »
Length:2,084
Mass (Da):236,278
Checksum:iD1D74F05BF1C6051
GO

Sequence cautioni

The sequence AAA17985.1 differs from that shown. Reason: Frameshift at positions 152 and 189. Curated
The sequence AAA85638.1 differs from that shown. Reason: Contaminating sequence. Potential vector sequence at the N-terminus.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411A → P in AAA17985. (PubMed:8127861)Curated
Sequence conflicti153 – 1531A → P in AAA17985. (PubMed:8127861)Curated
Sequence conflicti156 – 1561A → P in AAA17985. (PubMed:8127861)Curated
Sequence conflicti161 – 1611A → P in AAA17985. (PubMed:8127861)Curated
Sequence conflicti164 – 1641G → A in AAA17985. (PubMed:8127861)Curated
Sequence conflicti977 – 9771L → V in AAA17985. (PubMed:8127861)Curated
Sequence conflicti1015 – 10184ARSS → GRRR in AAA17985. (PubMed:8127861)Curated
Sequence conflicti1256 – 12561Q → H in AAA17985. (PubMed:8127861)Curated
Sequence conflicti1316 – 13161V → L in AAA17985. (PubMed:8127861)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1889 – 18891Q → E.
Corresponds to variant rs35233306 [ dbSNP | Ensembl ].
VAR_047534
Natural varianti1959 – 19591F → S.
Corresponds to variant rs12919017 [ dbSNP | Ensembl ].
VAR_047535
Natural varianti2077 – 20771E → K.
Corresponds to variant rs2228248 [ dbSNP | Ensembl ].
VAR_047536

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1933 – 195725Missing in isoform 2. 1 PublicationVSP_021819Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02619 mRNA. Translation: AAA17985.1. Frameshift.
AC002303 Genomic DNA. Translation: AAB67637.1.
AC025275 Genomic DNA. No translation available.
AC002551 Genomic DNA. Translation: AAC05811.1.
BC044857 mRNA. Translation: AAH44857.1.
BC137229 mRNA. Translation: AAI37230.1.
U06485 mRNA. Translation: AAA85638.1. Sequence problems.
CCDSiCCDS32414.1. [Q12789-2]
CCDS66988.1. [Q12789-3]
PIRiB56011.
I38414.
RefSeqiNP_001273171.1. NM_001286242.1. [Q12789-3]
NP_001511.2. NM_001520.3. [Q12789-2]
UniGeneiHs.371718.

Genome annotation databases

EnsembliENST00000356183; ENSP00000348510; ENSG00000077235. [Q12789-2]
ENST00000561623; ENSP00000455417; ENSG00000077235. [Q12789-3]
GeneIDi2975.
KEGGihsa:2975.
UCSCiuc002dou.3. human. [Q12789-3]
uc002dov.2. human. [Q12789-2]

Polymorphism databases

DMDMi215274233.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02619 mRNA. Translation: AAA17985.1 . Frameshift.
AC002303 Genomic DNA. Translation: AAB67637.1 .
AC025275 Genomic DNA. No translation available.
AC002551 Genomic DNA. Translation: AAC05811.1 .
BC044857 mRNA. Translation: AAH44857.1 .
BC137229 mRNA. Translation: AAI37230.1 .
U06485 mRNA. Translation: AAA85638.1 . Sequence problems.
CCDSi CCDS32414.1. [Q12789-2 ]
CCDS66988.1. [Q12789-3 ]
PIRi B56011.
I38414.
RefSeqi NP_001273171.1. NM_001286242.1. [Q12789-3 ]
NP_001511.2. NM_001520.3. [Q12789-2 ]
UniGenei Hs.371718.

3D structure databases

ProteinModelPortali Q12789.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109230. 66 interactions.
DIPi DIP-38212N.
IntActi Q12789. 25 interactions.
MINTi MINT-1154812.
STRINGi 9606.ENSP00000348510.

PTM databases

PhosphoSitei Q12789.

Polymorphism databases

DMDMi 215274233.

Proteomic databases

MaxQBi Q12789.
PaxDbi Q12789.
PRIDEi Q12789.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356183 ; ENSP00000348510 ; ENSG00000077235 . [Q12789-2 ]
ENST00000561623 ; ENSP00000455417 ; ENSG00000077235 . [Q12789-3 ]
GeneIDi 2975.
KEGGi hsa:2975.
UCSCi uc002dou.3. human. [Q12789-3 ]
uc002dov.2. human. [Q12789-2 ]

Organism-specific databases

CTDi 2975.
GeneCardsi GC16M027471.
H-InvDB HIX0012915.
HGNCi HGNC:4664. GTF3C1.
HPAi HPA051617.
MIMi 603246. gene.
neXtProti NX_Q12789.
PharmGKBi PA29052.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322015.
GeneTreei ENSGT00390000008664.
HOGENOMi HOG000154556.
HOVERGENi HBG057283.
InParanoidi Q12789.
KOi K15199.
OMAi EFLWRAL.
OrthoDBi EOG75J0MB.
PhylomeDBi Q12789.
TreeFami TF351624.

Enzyme and pathway databases

Reactomei REACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.

Miscellaneous databases

ChiTaRSi GTF3C1. human.
GeneWikii GTF3C1.
GenomeRNAii 2975.
NextBioi 11798.
PROi Q12789.
SOURCEi Search...

Gene expression databases

Bgeei Q12789.
CleanExi HS_GTF3C1.
ExpressionAtlasi Q12789. baseline and differential.
Genevestigatori Q12789.

Family and domain databases

InterProi IPR007309. TFIIIC_Bblock-bd.
[Graphical view ]
Pfami PF04182. B-block_TFIIIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1103-1121.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1107-2109 (ISOFORM 2).
    Tissue: Brain and Cervix.
  5. "Cloning and characterization of an evolutionarily divergent DNA-binding subunit of mammalian TFIIIC."
    Lagna G., Kovelman R., Sukegawa J., Roeder R.G.
    Mol. Cell. Biol. 14:3053-3064(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 71-728 (ISOFORM 1).
  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-1068, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1969, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-1062; SER-1632; SER-1653; SER-1856; SER-1865 AND SER-1868, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery."
    de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A., Mourelatos Z.
    Hum. Mol. Genet. 18:2115-2126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGHMBP2.
  13. "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-1068; SER-1865 AND SER-1868, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-1062; SER-1068; SER-1632; SER-1653; SER-1865 AND SER-1868, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-739; SER-1062 AND SER-1068, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTF3C1_HUMAN
AccessioniPrimary (citable) accession number: Q12789
Secondary accession number(s): B2RP21
, Q12838, Q6DKN9, Q9Y4W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 121 of the entry and version 4 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 16
    Human chromosome 16: 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