Q6ZP01 · RBM44_HUMAN
- ProteinRNA-binding protein 44
- GeneRBM44
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1051 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Component of intercellular bridges during meiosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells. Not required for fertility (By similarity).
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 | catalytic step 2 spliceosome | |
Cellular Component | cytoplasm | |
Cellular Component | intercellular bridge | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | mRNA splicing, via spliceosome |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-binding protein 44
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6ZP01
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected in the intercellular bridges.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057247 | 51 | in dbSNP:rs13393001 | |||
Sequence: D → H | ||||||
Natural variant | VAR_033147 | 52 | in dbSNP:rs13393001 | |||
Sequence: D → H | ||||||
Natural variant | VAR_033148 | 892 | in dbSNP:rs10186505 | |||
Sequence: N → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,152 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000294174 | 1-1051 | RNA-binding protein 44 | |||
Sequence: MQATAVVETASGKGYHSNGGNLQKDKPSNPKKENLLLSSNGCDEVKLTFPDDDWNSSTLEQRANNKEISNIDKMDLLEPFFSVSQDTNTESTQFQSSELEDSTDYAFLNKTYSIPYSESKLKKESLTPLSSELDPEVQKKEEVFFNILEHQDKTVGLERIYNISDANYRESAEDTQKHDTDEDSQQEYHSAEEQEYISNHLSFDQTKALDISNPEVVELGNSGYEVKCASNVEDNRVNSGSGSIISFDSLDVYGQEESLHVSKFQNSVMLREYHDLKHEKYKEQETNSMYHTVFDGSVLRSNSPGNQESQSKSGSLSPQKVLKMKIYTENMKSQINEGKDFCGNKIVENKILLHLENPSTLPQDKALETLLQPCKDCQTSWTSVFDDSIISACGYYESLQNTADSALDFSAMLPKIAVRDNQAIEDNTSLKVAHSSTTKKTCFHNIGEMCTKSLTDAASCTVTINQTVDVSTDFRACFTTSRATSARPSVVSTSSNTEITMMNKKRPDEWQNEKQKSVACSTDWSYSEDCIDTQMAITKGSGKSLSVDSLKPNGNFLNKDFLELRKACGITDLKKHPEREFQLFKDTEKDLPSMCCQKIMQRAIKAELHLLNVHYQMCRRHCCDIYKLVMENREGLNMNLSSNSAKKELGSALLSLLGDLKVRYVTLKEKIHKGIPLEELPPLSLESKLLSTFSTFASRLMKKETHVFSEADAEQDNQRAHDVDVSSNLKKTLSQMSLSSDNSHATQNISPKKDDFKNGDINADFSQLKLGDKDCRHYQETSEDWSDAKESLTGVDVSGTQGNQVEQDTWNLDLTGEMKNVEPSQRDKGYLIHVGGLCPSVSEADLRSHFQKYQVSEISIYDSTNYRYASLAFTKNSDAKIAVKEMNGIEINGKSVNVWPVKILGEYTSPLSSKNGNRISSNNLEKSTNKQIHSEFSISRLPRTRPRQLGSEQDSEVFPSDQGVKKNCKQIESAKLLPDTPVQFIPPNTLNLRSFTKIIKRLAELHPEVSRDHIINALQEVRIRHKGFLNGLSITTIVEMTSSLLKNSASS | ||||||
Modified residue | 388 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 391 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 546 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 726 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MQATAVVETASGKGYHSNGGNLQKDKPSNPKKENLL | ||||||
Region | 169-190 | Disordered | ||||
Sequence: RESAEDTQKHDTDEDSQQEYHS | ||||||
Compositional bias | 170-190 | Basic and acidic residues | ||||
Sequence: ESAEDTQKHDTDEDSQQEYHS | ||||||
Region | 296-318 | Disordered | ||||
Sequence: GSVLRSNSPGNQESQSKSGSLSP | ||||||
Region | 735-758 | Disordered | ||||
Sequence: QMSLSSDNSHATQNISPKKDDFKN | ||||||
Domain | 830-903 | RRM | ||||
Sequence: YLIHVGGLCPSVSEADLRSHFQKYQVSEISIYDSTNYRYASLAFTKNSDAKIAVKEMNGIEINGKSVNVWPVKI | ||||||
Region | 939-964 | Disordered | ||||
Sequence: SRLPRTRPRQLGSEQDSEVFPSDQGV | ||||||
Compositional bias | 944-960 | Polar residues | ||||
Sequence: TRPRQLGSEQDSEVFPS |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,051
- Mass (Da)117,985
- Last updated2022-05-25 v4
- Checksum45400796EEAF1415
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 170-190 | Basic and acidic residues | ||||
Sequence: ESAEDTQKHDTDEDSQQEYHS | ||||||
Compositional bias | 944-960 | Polar residues | ||||
Sequence: TRPRQLGSEQDSEVFPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC012076 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC126111 EMBL· GenBank· DDBJ | AAI26112.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK130316 EMBL· GenBank· DDBJ | BAC85324.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |