Q13428 · TCOF_HUMAN

  • Protein
    Treacle protein
  • Gene
    TCOF1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832).
Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentfibrillar center
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Molecular Functionprotein heterodimerization activity
Molecular Functionprotein-macromolecule adaptor activity
Molecular FunctionRNA binding
Molecular Functionscaffold protein binding
Biological Processneural crest cell development
Biological Processneural crest formation
Biological Processnucleolar large rRNA transcription by RNA polymerase I
Biological Processregulation of translation
Biological Processskeletal system development

Enzyme and pathway databases

Community curation (1)

Serves as a scaffold protein necessary for the formation of the fibrillar center of the nucleolus through self-assembly.

Source:  PMID - 37586369Contributor:  AnonymousView submission

Names & Taxonomy

Protein names

  • Recommended name
    Treacle protein
  • Alternative names
    • Treacher Collins syndrome protein

Gene names

    • Name
      TCOF1
Community curation (1)

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q13428
  • Secondary accessions
    • A0JLU0
    • B4E111
    • Q6SC72
    • Q7Z5W9
    • Q96A52

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Treacher Collins syndrome 1 (TCS1)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:154500
Natural variants in TCS1
Variant IDPosition(s)ChangeDescription
VAR_00563053W>Rin TCS1

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_00563053in TCS1
Natural variantVAR_057002221in dbSNP:rs11541811
Natural variantVAR_005631516in dbSNP:rs138645438
Natural variantVAR_029869665in dbSNP:rs2071240
Natural variantVAR_005632887in dbSNP:rs7713638
Natural variantVAR_0356661030in a colorectal cancer sample; somatic mutation; dbSNP:rs1206146416
Natural variantVAR_0597291176in dbSNP:rs1136103
Natural variantVAR_0597301280in dbSNP:rs11541812
Natural variantVAR_0056331390in dbSNP:rs15251
Natural variantVAR_0617091431in dbSNP:rs45491898
Natural variantVAR_0056341432in dbSNP:rs151344580

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,961 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00000724591-1488UniProtTreacle protein
Modified residue83UniProtPhosphoserine
Modified residue (large scale data)83PRIDEPhosphoserine
Modified residue84UniProtPhosphothreonine
Modified residue (large scale data)84PRIDEPhosphothreonine
Modified residue85UniProtPhosphoserine
Modified residue (large scale data)85PRIDEPhosphoserine
Modified residue87UniProtPhosphoserine
Modified residue (large scale data)87PRIDEPhosphoserine
Modified residue88UniProtPhosphoserine
Modified residue (large scale data)88PRIDEPhosphoserine
Modified residue102UniProtPhosphothreonine
Modified residue107UniProtPhosphoserine
Modified residue (large scale data)107PRIDEPhosphoserine
Modified residue (large scale data)110PRIDEPhosphoserine
Modified residue (large scale data)111PRIDEPhosphoserine
Modified residue (large scale data)119PRIDEPhosphoserine
Modified residue (large scale data)120PRIDEPhosphoserine
Cross-link126UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue134UniProtN6-acetyllysine
Modified residue (large scale data)147PRIDEPhosphothreonine
Modified residue153UniProtPhosphoserine
Modified residue (large scale data)153PRIDEPhosphoserine
Modified residue155UniProtN6-acetyllysine
Modified residue156UniProtPhosphoserine
Modified residue (large scale data)156PRIDEPhosphoserine
Modified residue (large scale data)160PRIDEPhosphoserine
Modified residue (large scale data)164PRIDEPhosphoserine
Modified residue (large scale data)167PRIDEPhosphothreonine
Modified residue (large scale data)168PRIDEPhosphothreonine
Modified residue171UniProtPhosphoserine
Modified residue (large scale data)171PRIDEPhosphoserine
Modified residue173UniProtPhosphothreonine
Modified residue (large scale data)173PRIDEPhosphothreonine
Modified residue (large scale data)178PRIDEPhosphoserine
Modified residue (large scale data)226PRIDEPhosphoserine
Modified residue (large scale data)227PRIDEPhosphoserine
Modified residue (large scale data)229PRIDEPhosphoserine
Modified residue (large scale data)230PRIDEPhosphothreonine
Modified residue233UniProtPhosphoserine
Modified residue (large scale data)233PRIDEPhosphoserine
Modified residue249UniProtPhosphothreonine
Modified residue (large scale data)249PRIDEPhosphothreonine
Modified residue (large scale data)270PRIDEPhosphoserine
Modified residue (large scale data)272PRIDEPhosphoserine
Modified residue (large scale data)273PRIDEPhosphoserine
Modified residue (large scale data)277PRIDEPhosphoserine
Modified residue (large scale data)279PRIDEPhosphoserine
Modified residue296UniProtN6-acetyllysine
Modified residue310UniProtPhosphothreonine
Modified residue (large scale data)310PRIDEPhosphothreonine
Modified residue313UniProtN6-acetyllysine
Modified residue316UniProtPhosphothreonine
Modified residue (large scale data)316PRIDEPhosphothreonine
Modified residue322UniProtN6-acetyllysine
Modified residue (large scale data)328PRIDEPhosphoserine
Modified residue (large scale data)349PRIDEPhosphoserine
Modified residue (large scale data)368PRIDEPhosphothreonine
Modified residue (large scale data)369PRIDEPhosphoserine
Modified residue (large scale data)375PRIDEPhosphoserine
Modified residue381UniProtPhosphoserine
Modified residue (large scale data)381PRIDEPhosphoserine
Modified residue413UniProtPhosphoserine
Modified residue414UniProtPhosphoserine
Modified residue (large scale data)419PRIDEPhosphoserine
Modified residue (large scale data)440PRIDEPhosphoserine
Modified residue446UniProtPhosphoserine
Modified residue (large scale data)446PRIDEPhosphoserine
Modified residue (large scale data)475PRIDEPhosphoserine
Modified residue (large scale data)482PRIDEPhosphoserine
Modified residue484UniProtPhosphoserine
Modified residue (large scale data)484PRIDEPhosphoserine
Modified residue503UniProtPhosphoserine
Modified residue (large scale data)503PRIDEPhosphoserine
Cross-link507UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue533UniProtPhosphothreonine
Modified residue (large scale data)533PRIDEPhosphothreonine
Modified residue (large scale data)571PRIDEPhosphoserine
Modified residue581UniProtPhosphothreonine
Modified residue (large scale data)581PRIDEPhosphothreonine
Modified residue (large scale data)582PRIDEPhosphoserine
Modified residue583UniProtPhosphoserine
Modified residue (large scale data)583PRIDEPhosphoserine
Modified residue600UniProtN6-acetyllysine; alternate
Cross-link600UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue620UniProtPhosphoserine
Cross-link637UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)673PRIDEPhosphothreonine
Modified residue (large scale data)674PRIDEPhosphoserine
Modified residue (large scale data)678PRIDEPhosphoserine
Modified residue679UniProtPhosphoserine
Modified residue (large scale data)679PRIDEPhosphoserine
Modified residue (large scale data)699PRIDEPhosphoserine
Modified residue (large scale data)701PRIDEPhosphoserine
Modified residue716UniProtN6-acetyllysine
Modified residue720UniProtN6-acetyllysine
Cross-link725UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link732UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)734PRIDEPhosphoserine
Modified residue755UniProtN6-acetyllysine; alternate
Cross-link755UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link755UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue762UniProtPhosphoserine
Modified residue (large scale data)762PRIDEPhosphoserine
Modified residue764UniProtPhosphoserine
Modified residue (large scale data)764PRIDEPhosphoserine
Modified residue765UniProtPhosphoserine
Modified residue (large scale data)765PRIDEPhosphoserine
Modified residue769UniProtPhosphoserine
Modified residue (large scale data)769PRIDEPhosphoserine
Modified residue771UniProtPhosphoserine
Modified residue777UniProtPhosphoserine
Modified residue (large scale data)777PRIDEPhosphoserine
Modified residue (large scale data)801PRIDEPhosphoserine
Modified residue (large scale data)823PRIDEPhosphoserine
Modified residue (large scale data)846PRIDEPhosphoserine
Modified residue868UniProtPhosphoserine
Modified residue870UniProtPhosphoserine
Modified residue871UniProtPhosphoserine
Modified residue875UniProtPhosphoserine
Modified residue877UniProtPhosphoserine
Modified residue (large scale data)877PRIDEPhosphoserine
Modified residue906UniProtPhosphoserine
Modified residue (large scale data)906PRIDEPhosphoserine
Modified residue914UniProtPhosphothreonine
Modified residue (large scale data)914PRIDEPhosphothreonine
Modified residue967UniProtPhosphoserine
Modified residue (large scale data)967PRIDEPhosphoserine
Modified residue974UniProtPhosphothreonine
Modified residue (large scale data)974PRIDEPhosphothreonine
Modified residue (large scale data)982PRIDEPhosphoserine
Modified residue983UniProtPhosphothreonine
Modified residue (large scale data)983PRIDEPhosphothreonine
Modified residue998UniProtPhosphoserine
Modified residue (large scale data)1036PRIDEPhosphoserine
Modified residue (large scale data)1050PRIDEPhosphoserine
Modified residue (large scale data)1069PRIDEPhosphoserine
Modified residue (large scale data)1110PRIDEPhosphothreonine
Modified residue1111UniProtPhosphoserine
Modified residue (large scale data)1111PRIDEPhosphoserine
Modified residue (large scale data)1114PRIDEPhosphoserine
Modified residue (large scale data)1116PRIDEPhosphoserine
Modified residue1175UniProtPhosphothreonine
Modified residue (large scale data)1175PRIDEPhosphothreonine
Modified residue (large scale data)1186PRIDEPhosphothreonine
Modified residue1190UniProtPhosphoserine
Modified residue (large scale data)1190PRIDEPhosphoserine
Modified residue (large scale data)1191PRIDEPhosphoserine
Modified residue1222UniProtPhosphothreonine
Modified residue (large scale data)1222PRIDEPhosphothreonine
Cross-link1224UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1227PRIDEPhosphoserine
Modified residue1228UniProtPhosphoserine
Modified residue (large scale data)1228PRIDEPhosphoserine
Modified residue (large scale data)1230PRIDEPhosphoserine
Modified residue (large scale data)1232PRIDEPhosphoserine
Modified residue (large scale data)1233PRIDEPhosphoserine
Modified residue1234UniProtPhosphothreonine
Modified residue (large scale data)1234PRIDEPhosphothreonine
Cross-link1238UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1248UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1257UniProtPhosphoserine
Modified residue (large scale data)1257PRIDEPhosphoserine
Modified residue (large scale data)1260PRIDEPhosphothreonine
Modified residue (large scale data)1269PRIDEPhosphothreonine
Modified residue (large scale data)1270PRIDEPhosphothreonine
Modified residue1350UniProtPhosphoserine
Modified residue (large scale data)1350PRIDEPhosphoserine
Modified residue1358UniProtPhosphothreonine
Modified residue (large scale data)1358PRIDEPhosphothreonine
Modified residue1376UniProtPhosphoserine
Modified residue (large scale data)1376PRIDEPhosphoserine
Modified residue1378UniProtPhosphoserine
Modified residue (large scale data)1378PRIDEPhosphoserine
Modified residue (large scale data)1382PRIDEPhosphothreonine
Modified residue (large scale data)1384PRIDEPhosphothreonine
Modified residue1407UniProtPhosphoserine
Modified residue (large scale data)1407PRIDEPhosphoserine
Modified residue1410UniProtPhosphoserine
Modified residue (large scale data)1410PRIDEPhosphoserine
Modified residue1414UniProtN6-acetyllysine; alternate
Cross-link1414UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue (large scale data)1434PRIDEPhosphoserine
Modified residue1469UniProtPhosphoserine
Modified residue1471UniProtPhosphoserine
Modified residue (large scale data)1471PRIDEPhosphoserine

Post-translational modification

Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832).
Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-IP7). Serine pyrophosphorylation is achieved by Mg2+-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Heterodimer; heterodimerizes with NOLC1 following monoubiquitination (PubMed:26399832).
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 (PubMed:12777385).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain6-38LisH
Compositional bias57-74Basic and acidic residues
Region57-1288Disordered
Compositional bias102-116Polar residues
Compositional bias140-174Polar residues
Compositional bias473-487Basic and acidic residues
Compositional bias643-657Polar residues
Compositional bias667-681Polar residues
Compositional bias776-790Polar residues
Compositional bias828-843Polar residues
Compositional bias976-996Polar residues
Compositional bias1053-1070Polar residues
Compositional bias1088-1122Polar residues
Compositional bias1170-1184Polar residues
Compositional bias1193-1235Polar residues
Compositional bias1322-1353Basic and acidic residues
Region1322-1488Disordered
Compositional bias1385-1425Basic and acidic residues
Compositional bias1441-1462Basic residues
Compositional bias1474-1488Basic residues

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (8)
  • Sequence status
    Complete

This entry describes 8 isoforms produced by Alternative splicing.

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.

  • Name
    1
  • Note
    Major.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,488
  • Mass (Da)
    152,106
  • Last updated
    2010-08-10 v3
  • Checksum
    6348306D0479790B
MAEARKRRELLPLIYHHLLRAGYVRAAREVKEQSGQKCFLAQPVTLLDIYTHWQQTSELGRKRKAEEDAALQAKKTRVSDPISTSESSEEEEEAEAETAKATPRLASTNSSVLGADLPSSMKEKAKAETEKAGKTGNSMPHPATGKTVANLLSGKSPRKSAEPSANTTLVSETEEEGSVPAFGAAAKPGMVSAGQADSSSEDTSSSSDETDVEGKPSVKPAQVKASSVSTKESPARKAAPAPGKVGDVTPQVKGGALPPAKRAKKPEEESESSEEGSESEEEAPAGTRSQVKASEKILQVRAASAPAKGTPGKGATPAPPGKAGAVASQTKAGKPEEDSESSSEESSDSEEETPAAKALLQAKASGKTSQVGAASAPAKESPRKGAAPAPPGKTGPAVAKAQAGKREEDSQSSSEESDSEEEAPAQAKPSGKAPQVRAASAPAKESPRKGAAPAPPRKTGPAAAQVQVGKQEEDSRSSSEESDSDREALAAMNAAQVKPLGKSPQVKPASTMGMGPLGKGAGPVPPGKVGPATPSAQVGKWEEDSESSSEESSDSSDGEVPTAVAPAQEKSLGNILQAKPTSSPAKGPPQKAGPVAVQVKAEKPMDNSESSEESSDSADSEEAPAAMTAAQAKPALKIPQTKACPKKTNTTASAKVAPVRVGTQAPRKAGTATSPAGSSPAVAGGTQRPAEDSSSSEESDSEEEKTGLAVTVGQAKSVGKGLQVKAASVPVKGSLGQGTAPVLPGKTGPTVTQVKAEKQEDSESSEEESDSEEAAASPAQVKTSVKKTQAKANPAAARAPSAKGTISAPGKVVTAAAQAKQRSPSKVKPPVRNPQNSTVLARGPASVPSVGKAVATAAQAQTGPEEDSGSSEEESDSEEEAETLAQVKPSGKTHQIRAALAPAKESPRKGAAPTPPGKTGPSAAQAGKQDDSGSSSEESDSDGEAPAAVTSAQVIKPPLIFVDPNRSPAGPAATPAQAQAASTPRKARASESTARSSSSESEDEDVIPATQCLTPGIRTNVVTMPTAHPRIAPKASMAGASSSKESSRISDGKKQEGPATQVSKKNPASLPLTQAALKVLAQKASEAQPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGTNKLRKPKLPEVQQATKAPESSDDSEDSSDSSSGSEEDGEGPQGAKSAHTLGPTPSRTETLVEETAAESSEDDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTLAAKDDPDGKQEAKPQQAAGMLSPKTGGKEAASGTTPQKSRKPKKGAGNPQASTLALQSNITQCLLGQPWPLNEAQVQASVVKVLTELLEQERKKVVDTTKESSRKGWESRKRKLSGDQPAARTPRSKKKKKLGAGEGGEASVSPEKTSTTSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGMGTVEGGDQSNPKSKKEKKKSDKRKKDKEKKEKKKKAKKASTKDSESPSQKKKKKKKKTAEQTV

Q13428-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q13428-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q13428-4

  • Name
    4
  • Note
    Minor.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 953-953: Q → QDSNSKPARSKTLAPAPPERNTEGSSESSEEELPLTQ

Q13428-5

Q13428-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q13428-7

Q13428-8

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R8Y857A0A2R8Y857_HUMANTCOF1297
A0A2R8Y4M7A0A2R8Y4M7_HUMANTCOF1108
E7ETY2E7ETY2_HUMANTCOF11488
H0YA99H0YA99_HUMANTCOF1188
H0YAB7H0YAB7_HUMANTCOF1148
H0Y8Y7H0Y8Y7_HUMANTCOF1994
A0A6I8PRA0A0A6I8PRA0_HUMANTCOF11240
A0A3B3IS06A0A3B3IS06_HUMANTCOF11358

Sequence caution

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

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias57-74Basic and acidic residues
Compositional bias102-116Polar residues
Compositional bias140-174Polar residues
Alternative sequenceVSP_022295214-290in isoform 2 and isoform 8
Compositional bias473-487Basic and acidic residues
Compositional bias643-657Polar residues
Compositional bias667-681Polar residues
Compositional bias776-790Polar residues
Compositional bias828-843Polar residues
Alternative sequenceVSP_022296953in isoform 4
Alternative sequenceVSP_023133954-958in isoform 5
Alternative sequenceVSP_023134959-1488in isoform 5
Compositional bias976-996Polar residues
Compositional bias1053-1070Polar residues
Alternative sequenceVSP_0403821062-1099in isoform 6 and isoform 7
Compositional bias1088-1122Polar residues
Compositional bias1170-1184Polar residues
Alternative sequenceVSP_0222971172in isoform 3, isoform 7 and isoform 8
Compositional bias1193-1235Polar residues
Sequence conflict1271in Ref. 7; BAG64623
Compositional bias1322-1353Basic and acidic residues
Compositional bias1385-1425Basic and acidic residues
Sequence conflict1389in Ref. 2; AAB40722
Compositional bias1441-1462Basic residues
Compositional bias1474-1488Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U40847
EMBL· GenBank· DDBJ
AAC50903.1
EMBL· GenBank· DDBJ
mRNA
U76366
EMBL· GenBank· DDBJ
AAC51181.1
EMBL· GenBank· DDBJ
mRNA
U84664
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84640
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84641
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84642
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84643
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84644
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84645
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84646
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84647
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84648
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84649
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84650
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84651
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84652
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84653
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84654
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84655
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84656
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84657
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84658
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84659
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84660
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84661
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84662
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U84663
EMBL· GenBank· DDBJ
AAC51185.1
EMBL· GenBank· DDBJ
Genomic DNA
U79659
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79645
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79646
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79647
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79648
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79649
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79650
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79651
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79652
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79653
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79654
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79655
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79656
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79657
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
U79658
EMBL· GenBank· DDBJ
AAB40722.1
EMBL· GenBank· DDBJ
Genomic DNA
AY460334
EMBL· GenBank· DDBJ
AAR87774.1
EMBL· GenBank· DDBJ
mRNA
AC011372
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC011764
EMBL· GenBank· DDBJ
AAH11764.1
EMBL· GenBank· DDBJ
mRNA
BC014559
EMBL· GenBank· DDBJ
AAH14559.1
EMBL· GenBank· DDBJ
mRNA
BC016144
EMBL· GenBank· DDBJ
AAH16144.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC027252
EMBL· GenBank· DDBJ
AAH27252.1
EMBL· GenBank· DDBJ
mRNA
BC033093
EMBL· GenBank· DDBJ
AAH33093.1
EMBL· GenBank· DDBJ
mRNA
AK303611
EMBL· GenBank· DDBJ
BAG64623.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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