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Q12789

- TF3C1_HUMAN

UniProt

Q12789 - TF3C1_HUMAN

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
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    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
    2. protein binding Source: UniProtKB

    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

    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

    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

    ArrayExpressiQ12789.
    BgeeiQ12789.
    CleanExiHS_GTF3C1.
    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. 60 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.
    HOGENOMiHOG000154556.
    HOVERGENiHBG057283.
    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

    MDALESLLDE VALEGLDGLC LPALWSRLET RVPPFPLPLE PCTQEFLWRA     50
    LATHPGISFY EEPRERPDLQ LQDRYEEIDL ETGILESRRD PVALEDVYPI 100
    HMILENKDGI QGSCRYFKER KNITNDIRTK SLQPRCTMVE AFDRWGKKLI 150
    IVASQAMRYR ALIGQEGDPD LKLPDFSYCI LERLGRSRWQ GELQRDLHTT 200
    AFKVDAGKLH YHRKILNKNG LITMQSHVIR LPTGAQQHSI LLLLNRFHVD 250
    RRSKYDILME KLSVMLSTRT NHIETLGKLR EELGLCERTF KRLYQYMLNA 300
    GLAKVVSLRL QEIHPECGPC KTKKGTDVMV RCLKLLKEFK RNDHDDDEDE 350
    EVISKTVPPV DIVFERDMLT QTYDLIERRG TKGISQAEIR VAMNVGKLEA 400
    RMLCRLLQRF KVVKGFMEDE GRQRTTKYIS CVFAEESDLS RQYQREKARS 450
    ELLTTVSLAS MQEESLLPEG EDTFLSESDS EEERSSSKRR GRGSQKDTRA 500
    SANLRPKTQP HHSTPTKGGW KVVNLHPLKK QPPSFPGAAE ERACQSLASR 550
    DSLLDTSSVS EPNVSFVSHC ADSNSGDIAV IEEVRMENPK ESSSSLKTGR 600
    HSSGQDKPHE TYRLLKRRNL IIEAVTNLRL IESLFTIQKM IMDQEKQEGV 650
    STKCCKKSIV RLVRNLSEEG LLRLYRTTVI QDGIKKKVDL VVHPSMDQND 700
    PLVRSAIEQV RFRISNSSTA NRVKTSQPPV PQGEAEEDSQ GKEGPSGSGD 750
    SQLSASSRSE SGRMKKSDNK MGITPLRNYH PIVVPGLGRS LGFLPKMPRL 800
    RVVHMFLWYL IYGHPASNTV EKPSFISERR TIKQESGRAG VRPSSSGSAW 850
    EACSEAPSKG SQDGVTWEAE VELATETVYV DDASWMRYIP PIPVHRDFGF 900
    GWALVSDILL CLPLSIFIQI VQVSYKVDNL EEFLNDPLKK HTLIRFLPRP 950
    IRQQLLYKRR YIFSVVENLQ RLCYMGLLQF GPTEKFQDKD QVFIFLKKNA 1000
    VIVDTTICDP HYNLARSSRP FERRLYVLNS MQDVENYWFD LQCVCLNTPL 1050
    GVVRCPRVRK NSSTDQGSDE EGSLQKEQES AMDKHNLERK CAMLEYTTGS 1100
    REVVDEGLIP GDGLGAAGLD SSFYGHLKRN WIWTSYIINQ AKKENTAAEN 1150
    GLTVRLQTFL SKRPMPLSAR GNSRLNIWGE ARVGSELCAG WEEQFEVDRE 1200
    PSLDRNRRVR GGKSQKRKRL KKDPGKKIKR KKKGEFPGEK SKRLRYHDEA 1250
    DQSALQRMTR LRVTWSMQED GLLVLCRIAS NVLNTKVKGP FVTWQVVRDI 1300
    LHATFEESLD KTSHSVGRRA RYIVKNPQAY LNYKVCLAEV YQDKALVGDF 1350
    MNRRGDYDDP KVCANEFKEF VEKLKEKFSS ALRNSNLEIP DTLQELFARY 1400
    RVLAIGDEKD QTRKEDELNS VDDIHFLVLQ NLIQSTLALS DSQMKSYQSF 1450
    QTFRLYREYK DHVLVKAFME CQKRSLVNRR RVNHTLGPKK NRALPFVPMS 1500
    YQLSQTYYRI FTWRFPSTIC TESFQFLDRM RAAGKLDQPD RFSFKDQDNN 1550
    EPTNDMVAFS LDGPGGNCVA VLTLFSLGLI SVDVRIPEQI IVVDSSMVEN 1600
    EVIKSLGKDG SLEDDEDEED DLDEGVGGKR RSMEVKPAQA SHTNYLLMRG 1650
    YYSPGIVSTR NLNPNDSIVV NSCQMKFQLR CTPVPARLRP AAAPLEELTM 1700
    GTSCLPDTFT KLINPQENTC SLEEFVLQLE LSGYSPEDLT AALEILEAII 1750
    ATGCFGIDKE ELRRRFSALE KAGGGRTRTF ADCIQALLEQ HQVLEVGGNT 1800
    ARLVAMGSAW PWLLHSVRLK DREDADIQRE DPQARPLEGS SSEDSPPEGQ 1850
    APPSHSPRGT KRRASWASEN GETDAEGTQM TPAKRPALQD SNLAPSLGPG 1900
    AEDGAEAQAP SPPPALEDTA AAGAAQEDQE GVGEFSSPGQ EQLSGQAQPP 1950
    EGSEDPRGFT ESFGAANISQ AARERDCESV CFIGRPWRVV DGHLNLPVCK 2000
    GMMEAMLYHI MTRPGIPESS LLRHYQGVLQ PVAVLELLQG LESLGCIRKR 2050
    WLRKPRPVSL FSTPVVEEVE VPSSLDESPM AFYEPTLDCT LRLGRVFPHE 2100
    VNWNKWIHL 2109
    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 AAA85638.1 differs from that shown. Reason: Contaminating sequence. Potential vector sequence at the N-terminus.
    The sequence AAA17985.1 differs from that shown. Reason: Frameshift at positions 152 and 189.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 60 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.
    HOGENOMi HOG000154556.
    HOVERGENi HBG057283.
    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

    ArrayExpressi Q12789.
    Bgeei Q12789.
    CleanExi HS_GTF3C1.
    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

    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 1, 2014
    This is version 120 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