O75400 · PR40A_HUMAN
- ProteinPre-mRNA-processing factor 40 homolog A
- GenePRPF40A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids957 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity).
Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing
Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing
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 | membrane | |
Cellular Component | nuclear matrix | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | U1 snRNP | |
Cellular Component | U2-type prespliceosome | |
Molecular Function | RNA binding | |
Biological Process | cell division | |
Biological Process | cell migration | |
Biological Process | cytoskeleton organization | |
Biological Process | mRNA cis splicing, via spliceosome | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | regulation of cell shape | |
Biological Process | regulation of cytokinesis |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePre-mRNA-processing factor 40 homolog A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75400
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with AKAP8L in the nuclear matrix.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 706 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, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000076085 | 1-957 | UniProt | Pre-mRNA-processing factor 40 homolog A | |||
Sequence: MRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGSSLCSGSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNSMDVAAGTASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGSLITKSNLHAMIKAEESSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAAPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ | |||||||
Modified residue | 9 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 17 | UniProt | In isoform O75400-2; Omega-N-methylarginine | ||||
Sequence: M | |||||||
Modified residue | 17 | UniProt | In isoform O75400-5; Omega-N-methylarginine | ||||
Sequence: M | |||||||
Modified residue | 24 | UniProt | In isoform O75400-2; Omega-N-methylarginine | ||||
Sequence: Q | |||||||
Modified residue | 24 | UniProt | In isoform O75400-5; Omega-N-methylarginine | ||||
Sequence: Q | |||||||
Modified residue | 34 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 47 | UniProt | In isoform O75400-2; Omega-N-methylarginine | ||||
Sequence: D | |||||||
Modified residue | 47 | UniProt | In isoform O75400-5; Omega-N-methylarginine | ||||
Sequence: D | |||||||
Modified residue | 151 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 191 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 196 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 241 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 345 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 373 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 375 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 376 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 429 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 723 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 723 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 787 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 787 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 809 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 832 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 834 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 883 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 883 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 885 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 885 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 888 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 888 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 932 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 932 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 933 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 933 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 935 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 935 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 938 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 938 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the brain cortex (at protein level). Widely expressed.
Gene expression databases
Interaction
Subunit
Interacts with the N-terminus of HTT. Interacts with the phosphorylated C-terminal domain of POLR2A. Interacts with AKAP8L, SF1, SRPK1, ENAH, ATBF1 and MECP2 (By similarity).
Interacts through the WW domains with formin proline-rich regions and with WASL/N-WASP (By similarity).
Interacts through the WW domains with formin proline-rich regions and with WASL/N-WASP (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGS | ||||||
Domain | 140-173 | WW 1 | ||||
Sequence: SGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDD | ||||||
Domain | 181-214 | WW 2 | ||||
Sequence: LLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE | ||||||
Region | 243-263 | Disordered | ||||
Sequence: EESSKQEECTTTSTAPVPTTE | ||||||
Compositional bias | 249-263 | Polar residues | ||||
Sequence: EECTTTSTAPVPTTE | ||||||
Compositional bias | 337-367 | Polar residues | ||||
Sequence: EEQAQLTSTPAIQDQSVEVSSNTGEETSKQE | ||||||
Region | 337-386 | Disordered | ||||
Sequence: EEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVADFTPKKEEEESQPAKK | ||||||
Compositional bias | 368-386 | Basic and acidic residues | ||||
Sequence: TVADFTPKKEEEESQPAKK | ||||||
Domain | 393-447 | FF 1 | ||||
Sequence: KEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ | ||||||
Domain | 460-514 | FF 2 | ||||
Sequence: YKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFF | ||||||
Domain | 527-587 | FF 3 | ||||
Sequence: RKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRA | ||||||
Domain | 607-667 | FF 4 | ||||
Sequence: QRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVED | ||||||
Domain | 672-727 | FF 5 | ||||
Sequence: YHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEK | ||||||
Domain | 742-799 | FF 6 | ||||
Sequence: KMKRKESAFKSMLKQAAPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHV | ||||||
Region | 803-957 | Disordered | ||||
Sequence: ECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ | ||||||
Compositional bias | 807-827 | Basic residues | ||||
Sequence: HHSKNKKHSKKSKKHHRKRSR | ||||||
Compositional bias | 828-866 | Basic and acidic residues | ||||
Sequence: SRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSY | ||||||
Compositional bias | 867-881 | Basic residues | ||||
Sequence: KKSKKHKKKSKKRRH | ||||||
Compositional bias | 882-927 | Basic and acidic residues | ||||
Sequence: KSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDS | ||||||
Compositional bias | 937-957 | Basic and acidic residues | ||||
Sequence: LSEGELEKRRRTLLEQLDDDQ |
Domain
The WW domains are essential for localization to nuclear speckles.
Sequence similarities
Belongs to the PRPF40 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O75400-1
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
- Length957
- Mass (Da)108,805
- Last updated2003-08-22 v2
- Checksum8874D0C1CE1FCDAF
O75400-2
- Name2
O75400-3
- Name3
- Differences from canonical
- 220-237: Missing
O75400-5
- Name5
- NoteProbable target of nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7N4I394 | A0A7N4I394_HUMAN | PRPF40A | 994 | ||
H0YG38 | H0YG38_HUMAN | PRPF40A | 367 | ||
H7BXZ7 | H7BXZ7_HUMAN | PRPF40A | 109 | ||
H7C2N3 | H7C2N3_HUMAN | PRPF40A | 157 | ||
A0A8V8TM61 | A0A8V8TM61_HUMAN | PRPF40A | 934 | ||
A0A8V8TM87 | A0A8V8TM87_HUMAN | PRPF40A | 931 | ||
A0A8Q3SIG7 | A0A8Q3SIG7_HUMAN | PRPF40A | 915 | ||
F5H578 | F5H578_HUMAN | PRPF40A | 972 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_040781 | 1 | in isoform 2 and isoform 5 | |||
Sequence: M → MCSGSGRRRSSLSPTM | ||||||
Alternative sequence | VSP_008047 | 14-55 | in isoform 2 and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_040782 | 127-128 | in isoform 5 | |||
Sequence: PG → LN | ||||||
Alternative sequence | VSP_040783 | 129-957 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008048 | 220-237 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 249-263 | Polar residues | ||||
Sequence: EECTTTSTAPVPTTE | ||||||
Compositional bias | 337-367 | Polar residues | ||||
Sequence: EEQAQLTSTPAIQDQSVEVSSNTGEETSKQE | ||||||
Compositional bias | 368-386 | Basic and acidic residues | ||||
Sequence: TVADFTPKKEEEESQPAKK | ||||||
Sequence conflict | 372-373 | in Ref. 5; AAB93495 | ||||
Sequence: FT → LL | ||||||
Sequence conflict | 433 | in Ref. 3; AAC27501/AAC27506 | ||||
Sequence: K → N | ||||||
Sequence conflict | 787 | in Ref. 1; BAA91277 | ||||
Sequence: S → P | ||||||
Compositional bias | 807-827 | Basic residues | ||||
Sequence: HHSKNKKHSKKSKKHHRKRSR | ||||||
Compositional bias | 828-866 | Basic and acidic residues | ||||
Sequence: SRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSY | ||||||
Compositional bias | 867-881 | Basic residues | ||||
Sequence: KKSKKHKKKSKKRRH | ||||||
Compositional bias | 882-927 | Basic and acidic residues | ||||
Sequence: KSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDS | ||||||
Compositional bias | 937-957 | Basic and acidic residues | ||||
Sequence: LSEGELEKRRRTLLEQLDDDQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC012443 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC079344 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK000592 EMBL· GenBank· DDBJ | BAA91277.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK024810 EMBL· GenBank· DDBJ | BAB15016.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AF049523 EMBL· GenBank· DDBJ | AAC27501.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF049524 EMBL· GenBank· DDBJ | AAC27502.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF049528 EMBL· GenBank· DDBJ | AAC27506.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC011788 EMBL· GenBank· DDBJ | AAH11788.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC027178 EMBL· GenBank· DDBJ | AAH27178.1 EMBL· GenBank· DDBJ | mRNA | ||
U70667 EMBL· GenBank· DDBJ | AAB93495.1 EMBL· GenBank· DDBJ | mRNA | ||
AF155096 EMBL· GenBank· DDBJ | AAD42862.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AF151059 EMBL· GenBank· DDBJ | AAF36145.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |