Q13601 · KRR1_HUMAN

  • Protein
    KRR1 small subunit processome component homolog
  • Gene
    KRR1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.

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 Componentchromosome
Cellular Componentcytoplasm
Cellular Componentintercellular bridge
Cellular Componentmembrane
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentsmall-subunit processome
Molecular FunctionRNA binding
Biological Processribosomal small subunit biogenesis
Biological ProcessrRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    KRR1 small subunit processome component homolog
  • Alternative names
    • HIV-1 Rev-binding protein 2
    • KRR-R motif-containing protein 1
    • Rev-interacting protein 1 (Rip-1)

Gene names

    • Name
      KRR1
    • Synonyms
      HRB2

Organism names

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

Accessions

  • Primary accession
    Q13601
  • Secondary accessions
    • A0FIK6
    • A0JLP0
    • B2R989
    • E7EUQ0
    • Q8NEA8

Proteomes

Organism-specific databases

Subcellular Location

Nucleus, nucleolus
Nucleus
Cytoplasm
Note: (Microbial infection) Translocates from cytoplasm to nucleus after exposure to HIV-1 virus or HIV-1 protein VPR or induction by hydrocortisone and dexamethasone in the absence of HIV-1 protein VPR.

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_049680134in dbSNP:rs11540407

Variants

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

The viewer provides 377 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 initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.

Type
IDPosition(s)Source
Description
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00000501142-381UniProtKRR1 small subunit processome component homolog
Modified residue3UniProtPhosphoserine
Modified residue (large scale data)3PRIDEPhosphoserine
Modified residue5UniProtPhosphoserine
Modified residue (large scale data)5PRIDEPhosphoserine
Cross-link24UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)31PRIDEPhosphoserine
Modified residue (large scale data)238PRIDEPhosphoserine
Modified residue (large scale data)267PRIDEPhosphothreonine
Cross-link340UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)345PRIDEPhosphoserine
Cross-link369UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
(Microbial infection) Directly interacts with HIV-1 protein VPR. Also identified in a complex with NR3C1 and HIV-1 protein VPR.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q13601RPS14 P622636EBI-744525, EBI-352783
BINARY Q13601SRPK1 Q96SB42EBI-744525, EBI-539478
BINARY Q13601ZBP1 Q9H1713EBI-744525, EBI-6264672

Complex viewer

View interactors in UniProtKB
View CPX-2511 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-51Disordered
Compositional bias7-27Basic and acidic residues
Compositional bias39-51Basic and acidic residues
Domain154-206KH
Compositional bias250-262Basic residues
Region250-278Disordered
Region309-338Disordered

Sequence similarities

Belongs to the KRR1 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q13601-1

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
    381
  • Mass (Da)
    43,665
  • Last updated
    2007-01-23 v4
  • MD5 Checksum
    98FA37659747C1072800599B8F609FFF
MASPSLERPEKGAGKSEFRNQKPKPENQDESELLTVPDGWKEPAFSKEDNPRGLLEESSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNIKSLMIKRELAKDSELRSQSWERFLPQFKHKNVNKRKEPKKKTVKKEYTPFPPPQPESQIDKELASGEYFLKANQKKRQKMEAIKAKQAEAISKRQEERNKAFIPPKEKPIVKPKEASTETKIDVASIKEKVKKAKNKKLGALTAEEIALKMEADEKKKKKKK

Q13601-2

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

Sequence caution

The sequence AAB00557.1 differs from that shown. Reason: Frameshift
The sequence AAH05225.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.

Features

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

Type
IDPosition(s)Description
Compositional bias7-27Basic and acidic residues
Sequence conflict13in Ref. 1; ABJ97679
Compositional bias39-51Basic and acidic residues
Sequence conflict57in Ref. 2; BAG36436
Sequence conflict69in Ref. 4; AAH16778
Sequence conflict161in Ref. 1; ABJ97679
Sequence conflict165in Ref. 1; ABJ97679
Sequence conflict206in Ref. 4; AAH26107
Alternative sequenceVSP_042223221-277in isoform 2
Compositional bias250-262Basic residues
Sequence conflict275in Ref. 4; AAH33887
Sequence conflict339in Ref. 1; ABJ97679 and 4; AAH33887
Sequence conflict353in Ref. 4; AAH05225

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF010919
EMBL· GenBank· DDBJ
ABJ97679.1
EMBL· GenBank· DDBJ
mRNA
AK313687
EMBL· GenBank· DDBJ
BAG36436.1
EMBL· GenBank· DDBJ
mRNA
AC022507
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC121761
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC005225
EMBL· GenBank· DDBJ
AAH05225.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC016778
EMBL· GenBank· DDBJ
AAH16778.1
EMBL· GenBank· DDBJ
mRNA
BC026107
EMBL· GenBank· DDBJ
AAH26107.1
EMBL· GenBank· DDBJ
mRNA
BC033887
EMBL· GenBank· DDBJ
AAH33887.1
EMBL· GenBank· DDBJ
mRNA
U55766
EMBL· GenBank· DDBJ
AAB00557.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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