Q53SF7 · COBL1_HUMAN

  • Protein
    Cordon-bleu protein-like 1
  • Gene
    COBLL1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

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 Componentextracellular exosome
Molecular Functionactin monomer binding
Molecular Functioncadherin binding

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cordon-bleu protein-like 1

Gene names

    • Name
      COBLL1
    • Synonyms
      KIAA0977

Organism names

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

Accessions

  • Primary accession
    Q53SF7
  • Secondary accessions
    • A6NMZ3
    • Q6IQ33
    • Q7Z3I6
    • Q9BRH4
    • Q9UG88
    • Q9Y2I3

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Variants

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

The viewer provides 1,424 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002604931-1128UniProtCordon-bleu protein-like 1
Modified residue (large scale data)5PRIDEPhosphothreonine
Modified residue139UniProtPhosphothreonine
Modified residue (large scale data)164PRIDEPhosphoserine
Modified residue204UniProtPhosphoserine
Modified residue222UniProtPhosphoserine
Modified residue (large scale data)247PRIDEPhosphoserine
Modified residue (large scale data)254PRIDEPhosphothreonine
Modified residue256UniProtPhosphoserine
Modified residue (large scale data)256PRIDEPhosphoserine
Modified residue260UniProtPhosphothreonine
Modified residue (large scale data)260PRIDEPhosphothreonine
Modified residue273UniProtPhosphoserine
Modified residue (large scale data)275PRIDEPhosphothreonine
Modified residue (large scale data)282PRIDEPhosphoserine
Modified residue284UniProtPhosphothreonine
Modified residue (large scale data)284PRIDEPhosphothreonine
Modified residue (large scale data)303PRIDEPhosphoserine
Modified residue (large scale data)305PRIDEPhosphoserine
Modified residue326UniProtPhosphoserine
Modified residue (large scale data)326PRIDEPhosphoserine
Modified residue333UniProtPhosphoserine
Modified residue (large scale data)333PRIDEPhosphoserine
Modified residue344UniProtPhosphoserine
Modified residue (large scale data)344PRIDEPhosphoserine
Modified residue (large scale data)348PRIDEPhosphoserine
Modified residue (large scale data)349PRIDEPhosphoserine
Modified residue356UniProtPhosphoserine
Modified residue (large scale data)356PRIDEPhosphoserine
Modified residue (large scale data)366PRIDEPhosphoserine
Modified residue438UniProtPhosphoserine
Modified residue (large scale data)438PRIDEPhosphoserine
Modified residue441UniProtPhosphoserine
Modified residue (large scale data)441PRIDEPhosphoserine
Modified residue (large scale data)448PRIDEPhosphoserine
Modified residue461UniProtPhosphoserine
Modified residue471UniProtPhosphoserine
Modified residue474UniProtPhosphoserine
Modified residue (large scale data)483PRIDEPhosphoserine
Modified residue (large scale data)494PRIDEPhosphotyrosine
Modified residue563UniProtPhosphoserine
Modified residue584UniProtPhosphoserine
Modified residue (large scale data)607PRIDEPhosphothreonine
Modified residue (large scale data)609PRIDEPhosphoserine
Modified residue (large scale data)612PRIDEPhosphoserine
Modified residue (large scale data)623PRIDEPhosphoserine
Modified residue786UniProtPhosphoserine
Modified residue (large scale data)788PRIDEPhosphoserine
Modified residue813UniProtPhosphoserine
Modified residue814UniProtPhosphoserine
Modified residue (large scale data)814PRIDEPhosphoserine
Modified residue821UniProtPhosphoserine
Modified residue (large scale data)821PRIDEPhosphoserine
Modified residue (large scale data)876PRIDEPhosphoserine
Modified residue (large scale data)879PRIDEPhosphotyrosine
Modified residue911UniProtPhosphoserine
Modified residue (large scale data)911PRIDEPhosphoserine
Modified residue (large scale data)915PRIDEPhosphothreonine
Modified residue917UniProtPhosphoserine
Modified residue (large scale data)917PRIDEPhosphoserine
Modified residue947UniProtPhosphoserine
Modified residue (large scale data)947PRIDEPhosphoserine
Modified residue (large scale data)981PRIDEPhosphoserine
Modified residue (large scale data)986PRIDEPhosphoserine
Modified residue (large scale data)998PRIDEPhosphoserine
Modified residue (large scale data)1006PRIDEPhosphoserine
Modified residue (large scale data)1056PRIDEPhosphothreonine
Modified residue1069UniProtPhosphoserine
Modified residue (large scale data)1069PRIDEPhosphoserine
Modified residue1070UniProtPhosphoserine
Modified residue (large scale data)1070PRIDEPhosphoserine
Modified residue (large scale data)1117PRIDEPhosphoserine
Modified residue (large scale data)1119PRIDEPhosphoserine
Modified residue1121UniProtPhosphoserine
Modified residue (large scale data)1121PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q53SF7PACSIN1 Q9BY113EBI-2835780, EBI-721769

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, motif, domain.

TypeIDPosition(s)Description
Compositional bias1-22Basic and acidic residues
Region1-35Disordered
Region249-309Disordered
Compositional bias266-284Polar residues
Motif291-296KKRRAP 1
Region325-441Disordered
Compositional bias344-362Polar residues
Motif360-365KKRRAP 2
Compositional bias399-413Polar residues
Compositional bias454-474Polar residues
Region454-499Disordered
Region780-840Disordered
Region882-964Disordered
Region995-1081Disordered
Compositional bias1002-1024Polar residues
Compositional bias1038-1081Polar residues
Domain1081-1101WH2
Compositional bias1103-1121Polar residues
Region1103-1128Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q53SF7-4

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.

  • Length
    1,128
  • Mass (Da)
    123,868
  • Last updated
    2019-09-18 v3
  • Checksum
    B0BC3812F4BA93E8
MDGRTPRPQDAPARRKPKAKAPLPPAETKYTDVSSAADSVESTAFIMEQKENMIDKDVELSVVLPGDIIKSTTVHGSKPMMDLLIFLCAQYHLNPSSYTIDLLSAEQNHIKFKPNTPIGMLEVEKVILKPKMLDKKKPTPIIPEKTVRVVINFKKTQKTIVRVSPHASLQELAPIICSKCEFDPLHTLLLKDYQSQEPLDLTKSLNDLGLRELYAMDVNRESCQISQNLDIMKEKENKGFFSFFQRSKKKRDQTASAPATPLVNKHRPTFTRSNTISKPYISNTLPSDAPKKRRAPLPPMPASQSVPQDLAHIQERPASCIVKSMSVDETDKSPCEAGRVRAGSLQLSSMSAGNSSLRRTKRKAPSPPSKIPPHQSDENSRVTALQPVDGVPPDSASEANSPEELSSPAGISSDYSLEEIDEKEELSEVPKVEAENISPKSQDIPFVSTDIINTLKNDPDSALGNGSGEFSQNSMEEKQETKSTDGQEPHSVVYDTSNGKKVVDSIRNLKSLGPNQENVVQNEIIVYPENTEDNMKNGVKKTEINVEGVAKNNNIDMEVERPSNSEAHETDTAISYKENHLAASSVPDQKLNQPSAEKTKDAAIQTTPSCNSFDGKHQDHNLSDSKVEECVQTSNNNISTQHSCLSSQDSVNTSREFRSQGTLIIHSEDPLTVKDPICAHGNDDLLPPVDRIDKNSTASYLKNYPLYRQDYNPKPKPSNEITREYIPKIGMTTYKIVPPKSLEISKDWQSETIEYKDDQDMHALGKKHTHENVKETAIQTEDSAISESPEEPLPNLKPKPNLRTEHQVPSSVSSPDDAMVSPLKPAPKMTRDTGTAPFAPNLEEINNILESKFKSRASNAQAKPSSFFLQMQKRVSGHYVTSAAAKSVHAAPNPAPKELTNKEAERDMLPSPEQTLSPLSKMPHSVPQPLVEKTDDDVIGQAPAEASPPPIAPKPVTIPASQVSTQNLKTLKTFGAPRPYSSSGPSPFALAVVKRSQSFSKERTESPSASALVQPPANTEEGKTHSVNKFVDIPQLGVSDKENNSAHNEQNSQIPTPTDGPSFTVMRQSSLTFQSSDPEQMRQSLLTAIRSGEAAAKLKRVTIPSNTISVNGRSRLSHSMSPDAQDGH

Q53SF7-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MCGRAAEAAASSRTPGREMGQAVTRRLGAGARAAPRRAM

Q53SF7-3

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

Computationally mapped potential isoform sequences

There are 12 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J5Y6C9J5Y6_HUMANCOBLL1163
C9J8C4C9J8C4_HUMANCOBLL1226
F8WEK0F8WEK0_HUMANCOBLL1148
C9JWZ0C9JWZ0_HUMANCOBLL1138
A0A0X1KG75A0A0X1KG75_HUMANCOBLL11174
C9JK90C9JK90_HUMANCOBLL1170
A0A7P0T9X3A0A7P0T9X3_HUMANCOBLL160
A0A7P0TAY7A0A7P0TAY7_HUMANCOBLL1152
A0A7P0TAB9A0A7P0TAB9_HUMANCOBLL1106
C9JAU3C9JAU3_HUMANCOBLL1157
A0A0D9SG04A0A0D9SG04_HUMANCOBLL11233
A0A0B4J1Z0A0A0B4J1Z0_HUMANCOBLL1424

Sequence caution

The sequence AAH06264.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.
The sequence BAA76821.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0602961in isoform 2
Compositional bias1-22Basic and acidic residues
Compositional bias266-284Polar residues
Sequence conflict330in Ref. 5; AAH71588
Compositional bias344-362Polar residues
Compositional bias399-413Polar residues
Alternative sequenceVSP_060297409in isoform 3
Compositional bias454-474Polar residues
Alternative sequenceVSP_060298519in isoform 3
Sequence conflict769in Ref. 6; CAB43215
Sequence conflict871in Ref. 6; CAD97877
Sequence conflict972in Ref. 5; AAH71588
Compositional bias1002-1024Polar residues
Sequence conflict1019in Ref. 6; CAD97877
Compositional bias1038-1081Polar residues
Sequence conflict1075in Ref. 6; CAB43215
Compositional bias1103-1121Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB023194
EMBL· GenBank· DDBJ
BAA76821.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK225849
EMBL· GenBank· DDBJ
-mRNA No translation available.
AC019181
EMBL· GenBank· DDBJ
AAX93068.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471058
EMBL· GenBank· DDBJ
EAX11340.1
EMBL· GenBank· DDBJ
Genomic DNA
BC006264
EMBL· GenBank· DDBJ
AAH06264.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC071588
EMBL· GenBank· DDBJ
AAH71588.1
EMBL· GenBank· DDBJ
mRNA
AL049939
EMBL· GenBank· DDBJ
CAB43215.1
EMBL· GenBank· DDBJ
mRNA
BX537877
EMBL· GenBank· DDBJ
CAD97877.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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