Q3KQU3 · MA7D1_HUMAN

  • Protein
    MAP7 domain-containing protein 1
  • Gene
    MAP7D1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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 Componentcytoplasm
Cellular Componentmicrotubule cytoskeleton
Cellular Componentspindle
Biological Processmicrotubule cytoskeleton organization

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    MAP7 domain-containing protein 1
  • Alternative names
    • Arginine/proline-rich coiled-coil domain-containing protein 1
    • Proline/arginine-rich coiled-coil domain-containing protein 1

Gene names

    • Name
      MAP7D1
    • Synonyms
      KIAA1187, PARCC1, RPRC1
    • ORF names
      PP2464

Organism names

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

Accessions

  • Primary accession
    Q3KQU3
  • Secondary accessions
    • D3DPS4
    • Q7L8J5
    • Q8N905
    • Q8TAK0
    • Q9HBQ2

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_035312104in dbSNP:rs2296266
Natural variantVAR_053970531in dbSNP:rs12563354

Variants

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

The viewer provides 1,056 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, cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00003068071-841UniProtMAP7 domain-containing protein 1
Modified residue (large scale data)21PRIDEPhosphothreonine
Modified residue (large scale data)34PRIDEPhosphoserine
Modified residue (large scale data)41PRIDEPhosphoserine
Modified residue47UniProtPhosphothreonine
Modified residue (large scale data)47PRIDEPhosphothreonine
Modified residue51UniProtPhosphothreonine
Modified residue (large scale data)51PRIDEPhosphothreonine
Modified residue70UniProtPhosphoserine
Modified residue (large scale data)70PRIDEPhosphoserine
Modified residue (large scale data)72PRIDEPhosphoserine
Modified residue86UniProtPhosphoserine
Modified residue (large scale data)86PRIDEPhosphoserine
Modified residue (large scale data)88PRIDEPhosphoserine
Modified residue (large scale data)89PRIDEPhosphoserine
Modified residue93UniProtPhosphoserine
Modified residue (large scale data)93PRIDEPhosphoserine
Modified residue97UniProtPhosphothreonine
Modified residue (large scale data)97PRIDEPhosphothreonine
Modified residue (large scale data)112PRIDEPhosphoserine
Modified residue113UniProtPhosphoserine
Modified residue (large scale data)113PRIDEPhosphoserine
Modified residue116UniProtPhosphoserine
Modified residue (large scale data)116PRIDEPhosphoserine
Modified residue118UniProtPhosphothreonine
Modified residue (large scale data)118PRIDEPhosphothreonine
Modified residue123UniProtPhosphoserine
Modified residue (large scale data)123PRIDEPhosphoserine
Modified residue125UniProtPhosphoserine
Modified residue (large scale data)125PRIDEPhosphoserine
Modified residue (large scale data)232PRIDEPhosphoserine
Modified residue (large scale data)241PRIDEPhosphoserine
Modified residue (large scale data)252PRIDEPhosphoserine
Modified residue254UniProtPhosphoserine
Modified residue (large scale data)254PRIDEPhosphoserine
Modified residue273UniProtPhosphoserine
Modified residue (large scale data)273PRIDEPhosphoserine
Modified residue (large scale data)274PRIDEPhosphoserine
Modified residue (large scale data)276PRIDEPhosphothreonine
Modified residue (large scale data)280PRIDEPhosphoserine
Modified residue (large scale data)282PRIDEPhosphoserine
Modified residue (large scale data)290PRIDEPhosphoserine
Modified residue (large scale data)311PRIDEPhosphoserine
Modified residue313UniProtPhosphoserine
Modified residue (large scale data)313PRIDEPhosphoserine
Modified residue (large scale data)364PRIDEPhosphoserine
Modified residue366UniProtPhosphoserine
Modified residue (large scale data)366PRIDEPhosphoserine
Modified residue (large scale data)368PRIDEPhosphoserine
Modified residue (large scale data)371PRIDEPhosphothreonine
Modified residue399UniProtPhosphoserine
Modified residue (large scale data)399PRIDEPhosphoserine
Modified residue (large scale data)410PRIDEPhosphoserine
Modified residue442UniProtPhosphoserine
Modified residue (large scale data)442PRIDEPhosphoserine
Modified residue446UniProtPhosphoserine
Modified residue (large scale data)446PRIDEPhosphoserine
Modified residue452UniProtPhosphoserine
Modified residue (large scale data)452PRIDEPhosphoserine
Modified residue454UniProtPhosphoserine
Modified residue (large scale data)454PRIDEPhosphoserine
Modified residue (large scale data)455PRIDEPhosphothreonine
Modified residue (large scale data)457PRIDEPhosphoserine
Modified residue460UniProtPhosphoserine
Modified residue (large scale data)460PRIDEPhosphoserine
Cross-link462UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)468PRIDEPhosphoserine
Modified residue (large scale data)469PRIDEPhosphoserine
Modified residue479UniProtPhosphoserine
Modified residue (large scale data)479PRIDEPhosphoserine
Modified residue (large scale data)483PRIDEPhosphoserine
Modified residue (large scale data)489PRIDEPhosphothreonine
Modified residue496UniProtPhosphoserine
Modified residue (large scale data)496PRIDEPhosphoserine
Modified residue (large scale data)517PRIDEPhosphoserine
Modified residue (large scale data)534PRIDEPhosphoserine
Modified residue (large scale data)539PRIDEPhosphoserine
Modified residue544UniProtPhosphoserine
Modified residue (large scale data)544PRIDEPhosphoserine
Modified residue548UniProtPhosphoserine
Modified residue (large scale data)548PRIDEPhosphoserine
Modified residue552UniProtPhosphoserine
Modified residue (large scale data)552PRIDEPhosphoserine
Modified residue554UniProtPhosphothreonine
Modified residue (large scale data)554PRIDEPhosphothreonine
Modified residue (large scale data)576PRIDEPhosphoserine
Modified residue (large scale data)585PRIDEPhosphothreonine
Modified residue742UniProtPhosphoserine
Modified residue (large scale data)742PRIDEPhosphoserine
Modified residue753UniProtPhosphoserine
Modified residue (large scale data)753PRIDEPhosphoserine
Modified residue (large scale data)809PRIDEPhosphoserine
Modified residue (large scale data)811PRIDEPhosphoserine
Modified residue813UniProtPhosphothreonine
Modified residue (large scale data)813PRIDEPhosphothreonine
Modified residue816UniProtPhosphothreonine
Modified residue834UniProtPhosphoserine
Modified residue (large scale data)834PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region1-151Disordered
Compositional bias18-52Pro residues
Compositional bias53-68Polar residues
Compositional bias111-125Polar residues
Coiled coil128-222
Compositional bias130-151Basic and acidic residues
Region184-208Disordered
Region316-813Disordered
Compositional bias408-441Basic and acidic residues
Coiled coil412-441
Compositional bias447-476Polar residues
Compositional bias477-499Pro residues
Compositional bias505-537Basic and acidic residues
Compositional bias544-564Pro residues
Coiled coil593-721
Compositional bias594-733Basic and acidic residues
Compositional bias793-812Polar residues

Sequence similarities

Belongs to the MAP7 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

Q3KQU3-1

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.

  • Length
    841
  • Mass (Da)
    92,820
  • Last updated
    2005-11-08 v1
  • Checksum
    47F5931376A931EF
MESGPRAELGAGAPPAVVARTPPEPRPSPEGDPSPPPPPMSALVPDTPPDTPPAMKNATSSKQLPLEPESPSGQVGPRPAPPQEESPSSEAKSRGPTPPAMGPRDARPPRRSSQPSPTAVPASDSPPTKQEVKKAGERHKLAKERREERAKYLAAKKAVWLEKEEKAKALREKQLQERRRRLEEQRLKAEQRRAALEERQRQKLEKNKERYEAAIQRSVKKTWAEIRQQRWSWAGALHHSSPGHKTSGSRCSVSAVNLPKHVDSIINKRLSKSSATLWNSPSRNRSLQLSAWESSIVDRLMTPTLSFLARSRSAVTLPRNGRDQGRGCDPGRGPTWGRAGASLARGPQPDRTHPSAAVPVCPRSASASPLTPCSVTRSVHRCAPAGERGERRKPNAGGSPAPVRRRPEASPVQKKEKKDKERENEKEKSALARERSLKKRQSLPASPRARLSASTASELSPKSKARPSSPSTSWHRPASPCPSPGPGHTLPPKPPSPRGTTASPKGRVRRKEEAKESPSAAGPEDKSQSKRRASNEKESAAPASPAPSPAPSPTPAPPQKEQPPAETPTDAAVLTSPPAPAPPVTPSKPMAGTTDREEATRLLAEKRRQAREQREREEQERRLQAERDKRMREEQLAREAEARAEREAEARRREEQEAREKAQAEQEEQERLQKQKEEAEARSREEAERQRLEREKHFQQQEQERQERRKRLEEIMKRTRKSEVSETKQKQDSKEANANGSSPEPVKAVEARSPGLQKEAVQKEEPIPQEPQWSLPSKELPASLVNGLQPLPAHQENGFSTNGPSGDKSLSRTPETLLPFAEAEAFLKKAVVQSPQVTEVL

Q3KQU3-2

Q3KQU3-3

Q3KQU3-4

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3DPS3D3DPS3_HUMANMAP7D1840
H0YF21H0YF21_HUMANMAP7D1248
C9JIR3C9JIR3_HUMANMAP7D1244
E9PLH3E9PLH3_HUMANMAP7D1140

Sequence caution

The sequence AAG17244.1 differs from that shown. Reason: Frameshift
The sequence BAA86501.2 differs from that shown. Reason: Erroneous initiation

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0284831-454in isoform 3
Compositional bias18-52Pro residues
Compositional bias53-68Polar residues
Compositional bias111-125Polar residues
Compositional bias130-151Basic and acidic residues
Sequence conflict207in Ref. 6; AAG17244
Alternative sequenceVSP_028484247-283in isoform 2
Alternative sequenceVSP_028485325-356in isoform 4
Compositional bias408-441Basic and acidic residues
Compositional bias447-476Polar residues
Alternative sequenceVSP_028486455-459in isoform 3
Compositional bias477-499Pro residues
Compositional bias505-537Basic and acidic residues
Compositional bias544-564Pro residues
Alternative sequenceVSP_028487570-578in isoform 3
Compositional bias594-733Basic and acidic residues
Alternative sequenceVSP_028488729in isoform 2, isoform 3 and isoform 4
Compositional bias793-812Polar residues
Sequence conflict794in Ref. 3; BAC04654

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB033013
EMBL· GenBank· DDBJ
BAA86501.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK001212
EMBL· GenBank· DDBJ
BAA91557.1
EMBL· GenBank· DDBJ
mRNA
AK095939
EMBL· GenBank· DDBJ
BAC04654.1
EMBL· GenBank· DDBJ
mRNA
CH471059
EMBL· GenBank· DDBJ
EAX07381.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471059
EMBL· GenBank· DDBJ
EAX07382.1
EMBL· GenBank· DDBJ
Genomic DNA
BC027334
EMBL· GenBank· DDBJ
AAH27334.1
EMBL· GenBank· DDBJ
mRNA
BC106053
EMBL· GenBank· DDBJ
AAI06054.1
EMBL· GenBank· DDBJ
mRNA
AF218002
EMBL· GenBank· DDBJ
AAG17244.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AL136547
EMBL· GenBank· DDBJ
CAB66482.2
EMBL· GenBank· DDBJ
mRNA
CR457254
EMBL· GenBank· DDBJ
CAG33535.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp