Q13601 · KRR1_HUMAN
- ProteinKRR1 small subunit processome component homolog
- GeneKRR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids381 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | intercellular bridge | |
Cellular Component | membrane | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | small-subunit processome | |
Molecular Function | RNA binding | |
Biological Process | ribosomal small subunit biogenesis | |
Biological Process | rRNA processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKRR1 small subunit processome component homolog
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13601
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | VAR_049680 | 134 | in dbSNP:rs11540407 | ||
Variants
![](/variants.8e7f84.jpg)
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.
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 | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | |||
Modified residue | 2 | UniProt | N-acetylalanine | |||
Chain | PRO_0000050114 | 2-381 | UniProt | KRR1 small subunit processome component homolog | ||
Modified residue | 3 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | |||
Modified residue | 5 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | |||
Cross-link | 24 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 267 | PRIDE | Phosphothreonine | |||
Cross-link | 340 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | |||
Cross-link | 369 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Keywords
- PTM
Proteomic databases
PTM 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
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q13601 | RPS14 P62263 | 6 | EBI-744525, EBI-352783 | |
BINARY | Q13601 | SRPK1 Q96SB4 | 2 | EBI-744525, EBI-539478 | |
BINARY | Q13601 | ZBP1 Q9H171 | 3 | EBI-744525, EBI-6264672 |
Complex viewer
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-51 | Disordered | |||
Compositional bias | 7-27 | Basic and acidic residues | |||
Compositional bias | 39-51 | Basic and acidic residues | |||
Domain | 154-206 | KH | |||
Compositional bias | 250-262 | Basic residues | |||
Region | 250-278 | Disordered | |||
Region | 309-338 | Disordered | |||
Sequence similarities
Belongs to the KRR1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length381
- Mass (Da)43,665
- Last updated2007-01-23 v4
- MD5 Checksum98FA37659747C1072800599B8F609FFF
Q13601-2
- Name2
- Differences from canonical
- 221-277: Missing
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 7-27 | Basic and acidic residues | |||
Sequence conflict | 13 | in Ref. 1; ABJ97679 | |||
Compositional bias | 39-51 | Basic and acidic residues | |||
Sequence conflict | 57 | in Ref. 2; BAG36436 | |||
Sequence conflict | 69 | in Ref. 4; AAH16778 | |||
Sequence conflict | 161 | in Ref. 1; ABJ97679 | |||
Sequence conflict | 165 | in Ref. 1; ABJ97679 | |||
Sequence conflict | 206 | in Ref. 4; AAH26107 | |||
Alternative sequence | VSP_042223 | 221-277 | in isoform 2 | ||
Compositional bias | 250-262 | Basic residues | |||
Sequence conflict | 275 | in Ref. 4; AAH33887 | |||
Sequence conflict | 339 | in Ref. 1; ABJ97679 and 4; AAH33887 | |||
Sequence conflict | 353 | in Ref. 4; AAH05225 | |||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |