Q149N8 · SHPRH_HUMAN
- ProteinE3 ubiquitin-protein ligase SHPRH
- GeneSHPRH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1683 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
Pathway
Features
Showing features for binding site.
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 | nucleoplasm | |
Cellular Component | nucleosome | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin protein ligase binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | DNA damage response | |
Biological Process | DNA repair | |
Biological Process | nucleosome assembly | |
Biological Process | protein polyubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
SHPRH is a nucleosome-stimulated ATPase and a nucleosome-E3 ubiquitin ligase.
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase SHPRH
- EC number
- Alternative names
Gene names
- Community suggested namesSHPRH
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ149N8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031857 | 438 | in an ovarian cancer cell line; dbSNP:rs1411096648 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_031858 | 460 | in a melanoma cell line | |||
Sequence: S → F | ||||||
Natural variant | VAR_031859 | 1028 | in a melanoma cell line | |||
Sequence: N → Y | ||||||
Natural variant | VAR_064750 | 1222 | found in a renal cell carcinoma sample; somatic mutation | |||
Sequence: V → D | ||||||
Mutagenesis | 1432 | Abolishes E3 activity. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,858 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000284918 | 1-1683 | UniProt | E3 ubiquitin-protein ligase SHPRH | |||
Sequence: MSSRRKRAPPVRVDEEKRQQLHWNMHEDRRNEPIIISDDDEQPCPGSDTSSAHYIILSDSLKEEVAHRDKKRCSKVVSFSKPIEKEETVGIFSPLSVKLNIVISPYHFDNSWKAFLGELTLQLLPAQSLIENFSERSITLMSSESSNQFLIYVHSKGEDVEKQKKEPMSICDKGILVESSFSGEMLEDLGWLQKKRRIKLYQKPEGNHIIKVGIYLLEAGLAKLDFLSDANSRMKKFNQLMKKVMEKLHNSIIPDVLEEDEDDPESEPEGQDIDELYHFVKQTHQQETQSIQVDVQHPALIPVLRPYQREAVNWMLQQECFRSSPATESALHFLWREIVTSEGLKLYYNPYTGCIIREYPNSGPQLLGGILADEMGLGKTVEVLALILTHTRQDVKQDALTLPEGKVVNYFIPSHYFGGKLKKTEIQNIEFEPKEKVQCPPTRVMILTAVKEMNGKKGVSILSIYKYVSSIYRYDVQRNRSLLKRMLKCLIFEGLVKQIKGHGFSGTFTLGKNYKEEDICDKTKKQAVGSPRKIQKETRKSGNKDTDSEYLPSDTSDDDDDPYYYYYKSRRNRSKLRKKLVPSTKKGKSQPFINPDSQGHCPATSDSGITDVAMSKSTCISEFNQEHETEDCAESLNHADSDVPPSNTMSPFNTSDYRFECICGELDQIDRKPRVQCLKCHLWQHAKCVNYDEKNLKIKPFYCPHCLVAMEPVSTRATLIISPSSICHQWVDEINRHVRSSSLRVLVYQGVKKDGFLQPHFLAEQDIVIITYDVLRSELNYVDIPHSNSEDGRRLRNQKRYMAIPSPLVAVEWWRICLDEAQMVECPTVKAAEMAQRLSGINRWCISGTPVQRGLEDLFGLVVFLGIEPYCVKHWWVRLLYRPYCKKNPQHLYSFIAKILWRSAKKDVIDQIQIPPQTEEIHWLHFSPVERHFYHRQHEVCCQDVVVKLRKISDWALKLSSLDRRTVTSILYPLLRLRQACCHPQAVRGEFLPLQKSTMTMEELLTSLQKKCGTECEEAHRQLVCALNGLAGIHIIKGEYALAAELYREVLRSSEEHKGKLKTDSLQRLHATHNLMELLIARHPGIPPTLRDGRLEEEAKQLREHYMSKCNTEVAEAQQALYPVQQTIHELQRKIHSNSPWWLNVIHRAIEFTIDEELVQRVRNEITSNYKQQTGKLSMSEKFRDCRGLQFLLTTQMEELNKCQKLVREAVKNLEGPPSRNVIESATVCHLRPARLPLNCCVFCKADELFTEYESKLFSNTVKGQTAIFEEMIEDEEGLVDDRAPTTTRGLWAISETERSMKAILSFAKSHRFDVEFVDEGSTSMDLFEAWKKEYKLLHEYWMALRNRVSAVDELAMATERLRVRDPREPKPNPPVLHIIEPHEVEQNRIKLLNDKAVATSQLQKKLGQLLYLTNLEKSQDKTSGGVNPEPCPICARQLGKQWAVLTCGHCFCNECISIIIEQYSVGSHRSSIKCAICRQTTSHKEISYVFTSEKANQEEDIPVKGSHSTKVEAVVRTLMKIQLRDPGAKALVFSTWQDVLDIISKALTDNNMEFAQISRVKTFQENLSAFKRDPQINILLLPLHTGSNGLTIIEATHVLLVEPILNPAHELQAIGRVHRIGQTKPTIVHRFLIKATIEERMQAMLKTAERSHTNSSAKHSEASVLTVADLADLFTKETEELE | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 266 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 635 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q149N8 | BORCS6 Q96GS4 | 3 | EBI-714105, EBI-10193358 | |
BINARY | Q149N8 | EDARADD Q8WWZ3 | 3 | EBI-714105, EBI-2949647 | |
BINARY | Q149N8-1 | UBE2N P61088 | 2 | EBI-15612386, EBI-1052908 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, zinc finger, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-43 | Disordered | ||||
Sequence: MSSRRKRAPPVRVDEEKRQQLHWNMHEDRRNEPIIISDDDEQP | ||||||
Compositional bias | 7-37 | Basic and acidic residues | ||||
Sequence: RAPPVRVDEEKRQQLHWNMHEDRRNEPIIIS | ||||||
Domain | 307-389 | Helicase ATP-binding; first part | ||||
Sequence: YQREAVNWMLQQECFRSSPATESALHFLWREIVTSEGLKLYYNPYTGCIIREYPNSGPQLLGGILADEMGLGKTVEVLALILT | ||||||
Domain | 438-512 | H15 | ||||
Sequence: QCPPTRVMILTAVKEMNGKKGVSILSIYKYVSSIYRYDVQRNRSLLKRMLKCLIFEGLVKQIKGHGFSGTFTLGK | ||||||
Compositional bias | 525-551 | Basic and acidic residues | ||||
Sequence: KQAVGSPRKIQKETRKSGNKDTDSEYL | ||||||
Region | 525-607 | Disordered | ||||
Sequence: KQAVGSPRKIQKETRKSGNKDTDSEYLPSDTSDDDDDPYYYYYKSRRNRSKLRKKLVPSTKKGKSQPFINPDSQGHCPATSDS | ||||||
Compositional bias | 570-584 | Basic residues | ||||
Sequence: RRNRSKLRKKLVPST | ||||||
Compositional bias | 587-607 | Polar residues | ||||
Sequence: GKSQPFINPDSQGHCPATSDS | ||||||
Zinc finger | 658-709 | PHD-type | ||||
Sequence: RFECICGELDQIDRKPRVQCLKCHLWQHAKCVNYDEKNLKIKPFYCPHCLVA | ||||||
Domain | 710-868 | Helicase ATP-binding; second part | ||||
Sequence: MEPVSTRATLIISPSSICHQWVDEINRHVRSSSLRVLVYQGVKKDGFLQPHFLAEQDIVIITYDVLRSELNYVDIPHSNSEDGRRLRNQKRYMAIPSPLVAVEWWRICLDEAQMVECPTVKAAEMAQRLSGINRWCISGTPVQRGLEDLFGLVVFLGIE | ||||||
Motif | 819-822 | DEAQ box | ||||
Sequence: DEAQ | ||||||
Zinc finger | 1432-1479 | RING-type | ||||
Sequence: CPICARQLGKQWAVLTCGHCFCNECISIIIEQYSVGSHRSSIKCAICR | ||||||
Domain | 1514-1672 | Helicase C-terminal | ||||
Sequence: AVVRTLMKIQLRDPGAKALVFSTWQDVLDIISKALTDNNMEFAQISRVKTFQENLSAFKRDPQINILLLPLHTGSNGLTIIEATHVLLVEPILNPAHELQAIGRVHRIGQTKPTIVHRFLIKATIEERMQAMLKTAERSHTNSSAKHSEASVLTVADLA |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q149N8-1
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
- Length1,683
- Mass (Da)193,079
- Last updated2007-05-01 v2
- Checksum3EAA1433EF89B232
Q149N8-2
- Name2
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
- Differences from canonical
- 46-156: Missing
- 1039-1040: EY → RR
- 1041-1683: Missing
Q149N8-4
- Name3
- Differences from canonical
- 996-996: K → KSFEQSTFSF
- 1183-1187: Missing
- 1653-1655: HTN → IYI
- 1656-1683: Missing
Q149N8-5
- Name4
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YBI0 | H0YBI0_HUMAN | SHPRH | 97 | ||
Q5JT88 | Q5JT88_HUMAN | SHPRH | 129 | ||
A0A0D9SFM0 | A0A0D9SFM0_HUMAN | SHPRH | 1687 | ||
H7C2W2 | H7C2W2_HUMAN | SHPRH | 449 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-37 | Basic and acidic residues | ||||
Sequence: RAPPVRVDEEKRQQLHWNMHEDRRNEPIIIS | ||||||
Alternative sequence | VSP_024753 | 46-156 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 185 | in Ref. 3; CAH18145 | ||||
Sequence: M → V | ||||||
Sequence conflict | 379 | in Ref. 6; BAC11544 | ||||
Sequence: K → E | ||||||
Sequence conflict | 425 | in Ref. 6; BAC11544 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_024760 | 442-471 | in isoform 4 | |||
Sequence: TRVMILTAVKEMNGKKGVSILSIYKYVSSI → YPFTFSYTCDDTDSCERNEWKKRSVHPFHL | ||||||
Alternative sequence | VSP_024761 | 472-1683 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 525-551 | Basic and acidic residues | ||||
Sequence: KQAVGSPRKIQKETRKSGNKDTDSEYL | ||||||
Sequence conflict | 560 | in Ref. 3; CAH18145 | ||||
Sequence: D → G | ||||||
Compositional bias | 570-584 | Basic residues | ||||
Sequence: RRNRSKLRKKLVPST | ||||||
Compositional bias | 587-607 | Polar residues | ||||
Sequence: GKSQPFINPDSQGHCPATSDS | ||||||
Alternative sequence | VSP_024756 | 996 | in isoform 3 | |||
Sequence: K → KSFEQSTFSF | ||||||
Alternative sequence | VSP_024757 | 1039-1040 | in isoform 2 | |||
Sequence: EY → RR | ||||||
Alternative sequence | VSP_024758 | 1041-1683 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_024759 | 1183-1187 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1398 | in Ref. 5; AAI17687 | ||||
Sequence: V → F | ||||||
Alternative sequence | VSP_024762 | 1653-1655 | in isoform 3 | |||
Sequence: HTN → IYI | ||||||
Alternative sequence | VSP_024763 | 1656-1683 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY161136 EMBL· GenBank· DDBJ | AAO26201.1 EMBL· GenBank· DDBJ | mRNA | ||
AY163808 EMBL· GenBank· DDBJ | AAO06907.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749290 EMBL· GenBank· DDBJ | CAH18145.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AL356599 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL451145 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC113089 EMBL· GenBank· DDBJ | AAI13090.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC117685 EMBL· GenBank· DDBJ | AAI17686.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC117686 EMBL· GenBank· DDBJ | AAI17687.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075318 EMBL· GenBank· DDBJ | BAC11544.1 EMBL· GenBank· DDBJ | mRNA | ||
AK094944 EMBL· GenBank· DDBJ | BAC04459.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB095943 EMBL· GenBank· DDBJ | BAC23119.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |