Q8NHV4 · NEDD1_HUMAN
- ProteinProtein NEDD1
- GeneNEDD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids660 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for mitosis progression. Promotes the nucleation of microtubules from the spindle.
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 | apical part of cell | |
Cellular Component | centriole | |
Cellular Component | centrosome | |
Cellular Component | ciliary basal body | |
Cellular Component | cytosol | |
Cellular Component | fibrillar center | |
Cellular Component | nucleoplasm | |
Cellular Component | pericentriolar material | |
Cellular Component | spindle pole | |
Molecular Function | gamma-tubulin binding | |
Biological Process | cell division | |
Biological Process | microtubule nucleation | |
Biological Process | mitotic cell cycle |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein NEDD1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8NHV4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 804 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000051095 | 1-660 | UniProt | Protein NEDD1 | |||
Sequence: MQENLRFASSGDDIKIWDASSMTLVDKFNPHTSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELAEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSVHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVKTISAHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAASGGVQNSGIVREAPATSIATVLPQPMTSAMGKGTVAVQEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFSPIRDDAVVNKGSDESIGKGDGFDFLPQLNSVFPPRKNPVTSSTSVLHSSPLNVFMGSPGKEENENRDLTAESKKIYMGKQESKDSFKQLAKLVTSGAESGNLNTSPSSNQTRNSEKFEKPENEIEAQLICEPPINGSSTPNPKIASSVTAGVASSLSEKIADSIGNNRQNAPLTSIQIRFIQNMIQETLDDFREACHRDIVNLQVEMIKQFHMQLNEMHSLLERYSVNEGLVAEIERLREENKRLRAHF | |||||||
Modified residue | 325 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 382 | UniProt | Phosphothreonine; by PLK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 396 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | Phosphoserine; by PLK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 411 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 411 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 426 | UniProt | Phosphoserine; by PLK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 426 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 468 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 468 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 510 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 516 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 550 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 550 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 637 | UniProt | Phosphoserine; by PLK1 | ||||
Sequence: S |
Post-translational modification
During mitosis, prior phosphorylation on Thr-550 by CDK1 promotes subsequent phosphorylation by PLK1 on Thr-382, Ser-397, Ser-426 and Ser-637. Phosphorylated NEDD1 can interact with gamma-tubulin for targeting the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with FAM29A (PubMed:19029337).
Interacts with HSPA1A and HSPA1B. Interacts with gamma-tubulin in a HSPA1A/B-dependent manner (PubMed:27137183).
Interacts with HSPA1A and HSPA1B. Interacts with gamma-tubulin in a HSPA1A/B-dependent manner (PubMed:27137183).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NHV4 | HAUS6 Q7Z4H7 | 2 | EBI-2555055, EBI-2558196 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 1-31 | WD 1 | ||||
Sequence: MQENLRFASSGDDIKIWDASSMTLVDKFNPH | ||||||
Repeat | 32-71 | WD 2 | ||||
Sequence: TSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPL | ||||||
Repeat | 75-114 | WD 3 | ||||
Sequence: AEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRS | ||||||
Repeat | 117-156 | WD 4 | ||||
Sequence: DHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTP | ||||||
Repeat | 160-200 | WD 5 | ||||
Sequence: GSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHN | ||||||
Repeat | 204-244 | WD 6 | ||||
Sequence: VHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKT | ||||||
Repeat | 246-285 | WD 7 | ||||
Sequence: VADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVK | ||||||
Repeat | 289-332 | WD 8 | ||||
Sequence: AHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAAS | ||||||
Region | 369-411 | Disordered | ||||
Sequence: QEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFS | ||||||
Compositional bias | 375-404 | Polar residues | ||||
Sequence: PRSINTDTLSKETDSGKNQDFSSFDDTGKS | ||||||
Compositional bias | 507-524 | Polar residues | ||||
Sequence: GAESGNLNTSPSSNQTRN | ||||||
Region | 507-532 | Disordered | ||||
Sequence: GAESGNLNTSPSSNQTRNSEKFEKPE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8NHV4-1
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
- Length660
- Mass (Da)71,966
- Last updated2002-10-01 v1
- Checksum12817A567C13098B
Q8NHV4-2
- Name2
- Differences from canonical
- 1-89: Missing
Q8NHV4-3
- Name3
- Differences from canonical
- 1-1: M → MHFTGAVM
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053794 | 1 | in isoform 3 | |||
Sequence: M → MHFTGAVM | ||||||
Alternative sequence | VSP_043411 | 1-89 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 170 | in Ref. 1; BAC04099 | ||||
Sequence: Y → C | ||||||
Compositional bias | 375-404 | Polar residues | ||||
Sequence: PRSINTDTLSKETDSGKNQDFSSFDDTGKS | ||||||
Sequence conflict | 409 | in Ref. 1; BAC04099 | ||||
Sequence: M → V | ||||||
Compositional bias | 507-524 | Polar residues | ||||
Sequence: GAESGNLNTSPSSNQTRN | ||||||
Sequence conflict | 649 | in Ref. 1; BAC04099 | ||||
Sequence: L → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK093221 EMBL· GenBank· DDBJ | BAC04099.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303656 EMBL· GenBank· DDBJ | BAG64657.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315821 EMBL· GenBank· DDBJ | BAF98712.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007564 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC013417 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471054 EMBL· GenBank· DDBJ | EAW97577.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471054 EMBL· GenBank· DDBJ | EAW97579.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471054 EMBL· GenBank· DDBJ | EAW97580.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC027605 EMBL· GenBank· DDBJ | AAH27605.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |