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Q13428 (TCOF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Treacle protein
Alternative name(s):
Treacher Collins syndrome protein
Gene names
Name:TCOF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in nucleolar-cytoplasmic transport. May play a fundamental role in early embryonic development, particularly in development of the craniofacial complex By similarity. May participate in certain stages of ribosome biogenesis. Ref.8

Subunit structure

Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with NOP56 in an RNA-independent manner. Ref.8

Subcellular location

Nucleusnucleolus Ref.8.

Involvement in disease

Treacher Collins syndrome 1 (TCS1) [MIM:154500]: A form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Contains 1 LisH domain.

Sequence caution

The sequence AAH16144.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARRB1P494073EBI-396105,EBI-743313
ARRB2P321213EBI-396105,EBI-714559

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13428-1)

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.
Note: Major.
Isoform 2 (identifier: Q13428-2)

The sequence of this isoform differs from the canonical sequence as follows:
     214-290: Missing.
Isoform 3 (identifier: Q13428-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1172-1172: L → LV
Isoform 4 (identifier: Q13428-4)

The sequence of this isoform differs from the canonical sequence as follows:
     953-953: Q → QDSNSKPARSKTLAPAPPERNTEGSSESSEEELPLTQ
Note: Minor.
Isoform 5 (identifier: Q13428-5)

The sequence of this isoform differs from the canonical sequence as follows:
     954-958: VIKPP → DQESS
     959-1488: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q13428-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1062-1099: Missing.
Isoform 7 (identifier: Q13428-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1062-1099: Missing.
     1172-1172: L → LV
Isoform 8 (identifier: Q13428-8)

The sequence of this isoform differs from the canonical sequence as follows:
     214-290: Missing.
     1172-1172: L → LV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14881488Treacle protein
PRO_0000072459

Regions

Domain6 – 3833LisH
Compositional bias89 – 979Poly-Glu
Compositional bias204 – 2074Poly-Ser
Compositional bias693 – 6964Poly-Ser
Compositional bias996 – 10016Poly-Ser
Compositional bias1362 – 13665Poly-Lys
Compositional bias1452 – 146312Poly-Lys
Compositional bias1475 – 14828Poly-Lys

Amino acid modifications

Modified residue831Phosphoserine Ref.15
Modified residue841Phosphothreonine Ref.15
Modified residue851Phosphoserine Ref.15
Modified residue871Phosphoserine Ref.15
Modified residue881Phosphoserine Ref.15
Modified residue1341N6-acetyllysine By similarity
Modified residue1531Phosphoserine Ref.15
Modified residue1551N6-acetyllysine Ref.19
Modified residue1561Phosphoserine Ref.15 Ref.18 Ref.20 Ref.22
Modified residue1711Phosphoserine By similarity
Modified residue1731Phosphothreonine By similarity
Modified residue2331Phosphoserine Ref.20 Ref.22
Modified residue2491Phosphothreonine Ref.10 Ref.18 Ref.20
Modified residue2961N6-acetyllysine Ref.19
Modified residue3101Phosphothreonine Ref.15 Ref.20
Modified residue3131N6-acetyllysine By similarity
Modified residue3161Phosphothreonine Ref.15
Modified residue3221N6-acetyllysine By similarity
Modified residue3811Phosphoserine Ref.9 Ref.11 Ref.15 Ref.18 Ref.20 Ref.22
Modified residue4461Phosphoserine Ref.9 Ref.11 Ref.20 Ref.22
Modified residue5031Phosphoserine Ref.15 Ref.20 Ref.22
Modified residue5811Phosphothreonine Ref.15
Modified residue5831Phosphoserine Ref.15 Ref.18 Ref.20 Ref.22
Modified residue6001N6-acetyllysine Ref.19
Modified residue6201Phosphoserine Ref.9
Modified residue6791Phosphoserine By similarity
Modified residue7161N6-acetyllysine By similarity
Modified residue7201N6-acetyllysine By similarity
Modified residue7551N6-acetyllysine Ref.19
Modified residue7621Phosphoserine Ref.15
Modified residue7641Phosphoserine Ref.15
Modified residue7651Phosphoserine Ref.15
Modified residue7691Phosphoserine Ref.15
Modified residue7711Phosphoserine Ref.15
Modified residue7771Phosphoserine Ref.15
Modified residue8681Phosphoserine Ref.15 Ref.20
Modified residue8701Phosphoserine Ref.15 Ref.20
Modified residue8711Phosphoserine Ref.15 Ref.20
Modified residue8751Phosphoserine Ref.15 Ref.20
Modified residue8771Phosphoserine Ref.15 Ref.20
Modified residue9061Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14 Ref.20 Ref.22
Modified residue9141Phosphothreonine Ref.11 Ref.20
Modified residue9671Phosphoserine Ref.13 Ref.22
Modified residue9831Phosphothreonine Ref.18
Modified residue9981Phosphoserine Ref.15
Modified residue11111Phosphoserine Ref.10 Ref.15 Ref.18
Modified residue11901Phosphoserine Ref.15
Modified residue12281Phosphoserine Ref.10 Ref.15 Ref.18 Ref.22
Modified residue12341Phosphothreonine Ref.15
Modified residue12571Phosphoserine Ref.9 Ref.15 Ref.20 Ref.22
Modified residue13501Phosphoserine Ref.9 Ref.14 Ref.20 Ref.22
Modified residue13761Phosphoserine Ref.15 Ref.18 Ref.22
Modified residue13781Phosphoserine Ref.10 Ref.15 Ref.18 Ref.20 Ref.22
Modified residue14071Phosphoserine Ref.15
Modified residue14101Phosphoserine Ref.15 Ref.20
Modified residue14141N6-acetyllysine Ref.19

Natural variations

Alternative sequence214 – 29077Missing in isoform 2 and isoform 8.
VSP_022295
Alternative sequence9531Q → QDSNSKPARSKTLAPAPPER NTEGSSESSEEELPLTQ in isoform 4.
VSP_022296
Alternative sequence954 – 9585VIKPP → DQESS in isoform 5.
VSP_023133
Alternative sequence959 – 1488530Missing in isoform 5.
VSP_023134
Alternative sequence1062 – 109938Missing in isoform 6 and isoform 7.
VSP_040382
Alternative sequence11721L → LV in isoform 3, isoform 7 and isoform 8.
VSP_022297
Natural variant531W → R in TCS1. Ref.23
VAR_005630
Natural variant2211A → P.
Corresponds to variant rs11541811 [ dbSNP | Ensembl ].
VAR_057002
Natural variant5161P → L. Ref.23
VAR_005631
Natural variant6651A → P. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs2071240 [ dbSNP | Ensembl ].
VAR_029869
Natural variant8871V → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.23
Corresponds to variant rs7713638 [ dbSNP | Ensembl ].
VAR_005632
Natural variant10301R → K in a colorectal cancer sample; somatic mutation. Ref.24
VAR_035666
Natural variant11761P → R.
Corresponds to variant rs1136103 [ dbSNP | Ensembl ].
VAR_059729
Natural variant12801G → R.
Corresponds to variant rs11541812 [ dbSNP | Ensembl ].
VAR_059730
Natural variant13901A → V. Ref.23
Corresponds to variant rs15251 [ dbSNP | Ensembl ].
VAR_005633
Natural variant14311G → A.
Corresponds to variant rs45491898 [ dbSNP | Ensembl ].
VAR_061709
Natural variant14321D → G. Ref.23
VAR_005634

Experimental info

Sequence conflict12711P → L in BAG64623. Ref.7
Sequence conflict13891K → Q in AAB40722. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 10, 2010. Version 3.
Checksum: 6348306D0479790B

FASTA1,488152,106
        10         20         30         40         50         60 
MAEARKRREL LPLIYHHLLR AGYVRAAREV KEQSGQKCFL AQPVTLLDIY THWQQTSELG 

        70         80         90        100        110        120 
RKRKAEEDAA LQAKKTRVSD PISTSESSEE EEEAEAETAK ATPRLASTNS SVLGADLPSS 

       130        140        150        160        170        180 
MKEKAKAETE KAGKTGNSMP HPATGKTVAN LLSGKSPRKS AEPSANTTLV SETEEEGSVP 

       190        200        210        220        230        240 
AFGAAAKPGM VSAGQADSSS EDTSSSSDET DVEGKPSVKP AQVKASSVST KESPARKAAP 

       250        260        270        280        290        300 
APGKVGDVTP QVKGGALPPA KRAKKPEEES ESSEEGSESE EEAPAGTRSQ VKASEKILQV 

       310        320        330        340        350        360 
RAASAPAKGT PGKGATPAPP GKAGAVASQT KAGKPEEDSE SSSEESSDSE EETPAAKALL 

       370        380        390        400        410        420 
QAKASGKTSQ VGAASAPAKE SPRKGAAPAP PGKTGPAVAK AQAGKREEDS QSSSEESDSE 

       430        440        450        460        470        480 
EEAPAQAKPS GKAPQVRAAS APAKESPRKG AAPAPPRKTG PAAAQVQVGK QEEDSRSSSE 

       490        500        510        520        530        540 
ESDSDREALA AMNAAQVKPL GKSPQVKPAS TMGMGPLGKG AGPVPPGKVG PATPSAQVGK 

       550        560        570        580        590        600 
WEEDSESSSE ESSDSSDGEV PTAVAPAQEK SLGNILQAKP TSSPAKGPPQ KAGPVAVQVK 

       610        620        630        640        650        660 
AEKPMDNSES SEESSDSADS EEAPAAMTAA QAKPALKIPQ TKACPKKTNT TASAKVAPVR 

       670        680        690        700        710        720 
VGTQAPRKAG TATSPAGSSP AVAGGTQRPA EDSSSSEESD SEEEKTGLAV TVGQAKSVGK 

       730        740        750        760        770        780 
GLQVKAASVP VKGSLGQGTA PVLPGKTGPT VTQVKAEKQE DSESSEEESD SEEAAASPAQ 

       790        800        810        820        830        840 
VKTSVKKTQA KANPAAARAP SAKGTISAPG KVVTAAAQAK QRSPSKVKPP VRNPQNSTVL 

       850        860        870        880        890        900 
ARGPASVPSV GKAVATAAQA QTGPEEDSGS SEEESDSEEE AETLAQVKPS GKTHQIRAAL 

       910        920        930        940        950        960 
APAKESPRKG AAPTPPGKTG PSAAQAGKQD DSGSSSEESD SDGEAPAAVT SAQVIKPPLI 

       970        980        990       1000       1010       1020 
FVDPNRSPAG PAATPAQAQA ASTPRKARAS ESTARSSSSE SEDEDVIPAT QCLTPGIRTN 

      1030       1040       1050       1060       1070       1080 
VVTMPTAHPR IAPKASMAGA SSSKESSRIS DGKKQEGPAT QVSKKNPASL PLTQAALKVL 

      1090       1100       1110       1120       1130       1140 
AQKASEAQPP VARTQPSSGV DSAVGTLPAT SPQSTSVQAK GTNKLRKPKL PEVQQATKAP 

      1150       1160       1170       1180       1190       1200 
ESSDDSEDSS DSSSGSEEDG EGPQGAKSAH TLGPTPSRTE TLVEETAAES SEDDVVAPSQ 

      1210       1220       1230       1240       1250       1260 
SLLSGYMTPG LTPANSQASK ATPKLDSSPS VSSTLAAKDD PDGKQEAKPQ QAAGMLSPKT 

      1270       1280       1290       1300       1310       1320 
GGKEAASGTT PQKSRKPKKG AGNPQASTLA LQSNITQCLL GQPWPLNEAQ VQASVVKVLT 

      1330       1340       1350       1360       1370       1380 
ELLEQERKKV VDTTKESSRK GWESRKRKLS GDQPAARTPR SKKKKKLGAG EGGEASVSPE 

      1390       1400       1410       1420       1430       1440 
KTSTTSKGKA KRDKASGDVK EKKGKGSLGS QGAKDEPEEE LQKGMGTVEG GDQSNPKSKK 

      1450       1460       1470       1480 
EKKKSDKRKK DKEKKEKKKK AKKASTKDSE SPSQKKKKKK KKTAEQTV 

« Hide

Isoform 2 [UniParc].

Checksum: 54E198A54B9062B2
Show »

FASTA1,411144,314
Isoform 3 [UniParc].

Checksum: E24970345707B2CC
Show »

FASTA1,489152,205
Isoform 4 [UniParc].

Checksum: B9CB0B8858C31E3F
Show »

FASTA1,524155,929
Isoform 5 [UniParc].

Checksum: 1F041264A162451C
Show »

FASTA95896,757
Isoform 6 [UniParc].

Checksum: 99FE142AD43AD2A5
Show »

FASTA1,450148,254
Isoform 7 [UniParc].

Checksum: 0493C61010D7F167
Show »

FASTA1,451148,353
Isoform 8 [UniParc].

Checksum: 1B4ED99C9F485BD7
Show »

FASTA1,412144,414

References

« Hide 'large scale' references
[1]"Positional cloning of a gene involved in the pathogenesis of Treacher Collins syndrome."
Dixon J., Edwards S.J., Gladwin A.J., Dixon M.J., Loftus S.K., Bonner C.A., Koprivnikar K., Wasmuth J.J.
Nat. Genet. 12:130-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS PRO-665 AND ALA-887.
[2]"Identification of the complete coding sequence and genomic organization of the Treacher Collins syndrome gene."
Dixon J., Edwards S.J., Anderson I., Brass A., Scambler P.J., Dixon M.J.
Genome Res. 7:223-234(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANTS PRO-665 AND ALA-887.
[3]"TCOF1 gene encodes a putative nucleolar phosphoprotein that exhibits mutations in Treacher Collins syndrome throughout its coding region."
Wise C.A., Chiang L.C., Paznekas W.A., Sharma M., Musy M.M., Ashley J.A., Lovett M., Jabs E.W.
Proc. Natl. Acad. Sci. U.S.A. 94:3110-3115(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS PRO-665 AND ALA-887.
[4]"Another face of the Treacher Collins syndrome (TCOF1) gene: identification of additional exons."
So R.B., Gonzales B., Henning D., Dixon J., Dixon M.J., Valdez B.C.
Gene 328:49-57(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 4), VARIANTS PRO-665 AND ALA-887.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1448 (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-1188 (ISOFORM 3).
Tissue: Eye and Skin.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1452 (ISOFORM 7), VARIANT ALA-887.
Tissue: Thymus.
[8]"Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome."
Hayano T., Yanagida M., Yamauchi Y., Shinkawa T., Isobe T., Takahashi N.
J. Biol. Chem. 278:34309-34319(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 63-74; 101-122; 135-155; 297-308; 368-379; 433-444; 503-519; 571-586; 706-716; 733-755; 792-803; 893-904; 1065-1078; 1130-1138; 1225-1238; 1245-1259; 1318-1329 AND 1424-1437, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRE-RIBOSOMAL RNP COMPLEX, INTERACTION WITH NOP56, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"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-381; SER-446; SER-620; SER-906; SER-1257 AND SER-1350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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 THR-249; SER-1111; SER-1228 AND SER-1378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-446; SER-906 AND THR-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND SER-967, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND SER-1350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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-83; THR-84; SER-85; SER-87; SER-88; SER-153; SER-156; THR-310; THR-316; SER-381; SER-503; THR-581; SER-583; SER-762; SER-764; SER-765; SER-769; SER-771; SER-777; SER-868; SER-870; SER-871; SER-875; SER-877; SER-998; SER-1111; SER-1190; SER-1228; THR-1234; SER-1257; SER-1376; SER-1378; SER-1407 AND SER-1410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-156; THR-249; SER-381; SER-583; THR-983; SER-1111; SER-1228; SER-1376 AND SER-1378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-296; LYS-600; LYS-755 AND LYS-1414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-156; SER-233; THR-249; THR-310; SER-381; SER-446; SER-503; SER-583; SER-868; SER-870; SER-871; SER-875; SER-877; SER-906; THR-914; SER-1257; SER-1350; SER-1378 AND SER-1410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"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-156; SER-233; SER-381; SER-446; SER-503; SER-583; SER-906; SER-967; SER-1228; SER-1257; SER-1350; SER-1376 AND SER-1378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The mutational spectrum in Treacher Collins syndrome reveals a predominance of mutations that create a premature-termination codon."
Edwards S.J., Gladwin A.J., Dixon M.J.
Am. J. Hum. Genet. 60:515-524(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-516; ALA-887; VAL-1390 AND GLY-1432, VARIANT TCS1 ARG-53.
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-1030.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40847 mRNA. Translation: AAC50903.1.
U76366 mRNA. Translation: AAC51181.1.
U84664 expand/collapse EMBL AC list , U84640, U84641, U84642, U84643, U84644, U84645, U84646, U84647, U84648, U84649, U84650, U84651, U84652, U84653, U84654, U84655, U84656, U84657, U84658, U84659, U84660, U84661, U84662, U84663 Genomic DNA. Translation: AAC51185.1.
U79659 expand/collapse EMBL AC list , U79645, U79646, U79647, U79648, U79649, U79650, U79651, U79652, U79653, U79654, U79655, U79656, U79657, U79658 Genomic DNA. Translation: AAB40722.1.
AY460334 mRNA. Translation: AAR87774.1.
AC011372 Genomic DNA. No translation available.
BC011764 mRNA. Translation: AAH11764.1.
BC014559 mRNA. Translation: AAH14559.1.
BC016144 mRNA. Translation: AAH16144.1. Sequence problems.
BC027252 mRNA. Translation: AAH27252.1.
BC033093 mRNA. Translation: AAH33093.1.
AK303611 mRNA. Translation: BAG64623.1.
RefSeqNP_000347.2. NM_000356.3.
NP_001008657.1. NM_001008657.2.
NP_001128715.1. NM_001135243.1.
NP_001128716.1. NM_001135244.1.
NP_001128717.1. NM_001135245.1.
NP_001182070.1. NM_001195141.1.
XP_005268562.1. XM_005268505.1.
UniGeneHs.519672.
Hs.605019.

3D structure databases

ProteinModelPortalQ13428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112809. 37 interactions.
IntActQ13428. 16 interactions.
MINTMINT-4995561.
STRING9606.ENSP00000406888.

PTM databases

PhosphoSiteQ13428.

Polymorphism databases

DMDM302393806.

Proteomic databases

PaxDbQ13428.
PRIDEQ13428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323668; ENSP00000325223; ENSG00000070814. [Q13428-2]
ENST00000377797; ENSP00000367028; ENSG00000070814. [Q13428-3]
ENST00000394269; ENSP00000377811; ENSG00000070814. [Q13428-5]
ENST00000439160; ENSP00000406888; ENSG00000070814. [Q13428-7]
ENST00000445265; ENSP00000409944; ENSG00000070814. [Q13428-8]
ENST00000504761; ENSP00000421655; ENSG00000070814. [Q13428-1]
GeneID6949.
KEGGhsa:6949.
UCSCuc003lrw.3. human. [Q13428-5]
uc003lrx.3. human. [Q13428-8]
uc003lry.3. human. [Q13428-1]
uc003lrz.3. human. [Q13428-6]
uc003lsa.3. human. [Q13428-2]
uc011dch.2. human. [Q13428-7]

Organism-specific databases

CTD6949.
GeneCardsGC05P149717.
H-InvDBHIX0005313.
HGNCHGNC:11654. TCOF1.
HPACAB033199.
HPA038237.
HPA038238.
MIM154500. phenotype.
606847. gene.
neXtProtNX_Q13428.
Orphanet861. Treacher-Collins syndrome.
PharmGKBPA36405.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG006664.
InParanoidQ13428.
KOK14562.
OrthoDBEOG7M0NQT.
PhylomeDBQ13428.
TreeFamTF341730.

Gene expression databases

ArrayExpressQ13428.
BgeeQ13428.
CleanExHS_TCOF1.
GenevestigatorQ13428.

Family and domain databases

InterProIPR006594. LisH_dimerisation.
IPR003993. TCS_treacle.
IPR017859. Treacle-like_TCS.
[Graphical view]
PfamPF03546. Treacle. 6 hits.
[Graphical view]
PRINTSPR01503. TREACLE.
SMARTSM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTCOF1. human.
GeneWikiTreacle_protein.
GenomeRNAi6949.
NextBio27207.
PMAP-CutDBQ13428.
PROQ13428.
SOURCESearch...

Entry information

Entry nameTCOF_HUMAN
AccessionPrimary (citable) accession number: Q13428
Secondary accession number(s): A0JLU0 expand/collapse secondary AC list , B4E111, Q6SC72, Q7Z5W9, Q96A52, Q99408, Q99860
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 10, 2010
Last modified: April 16, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM