Q80YV2 (NIPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nuclear-interacting partner of ALK Alternative name(s): Nuclear-interacting partner of anaplastic lymphoma kinase Short name=mNIPA Zinc finger C3HC-type protein 1 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Essential component of an SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry By similarity. Overexpression may be able to protect from apoptosis induced by IL-3 withdrawal. Ref.1 |
| Pathway | |
| Subunit structure | Interacts with SKP1. Component of a SCF(NIPA) E3 complex with SKP1, RBX1 and CUL1 when not phosphorylated on Ser-353. Interacts with CCNB1 By similarity. |
| Subcellular location | Nucleus By similarity. |
| Domain | The F-box-like region is required for the interaction with SKP1 By similarity. |
| Post-translational modification | Phosphorylated. Phosphorylated on Ser residues at G2/M phase, but not during S and G0 phases. May also be weakly phosphorylated on Tyr residues. Ser-353 phosphorylation, a major site during the course of cell-cycle-dedendent phosphorylation, results in its dissociation from the SCF(NIPA) complex, thereby preventing CCNB1 degradation leading to mitotic entry By similarity. |
| Sequence similarities | Contains 1 C3HC-type zinc finger. |
| Sequence caution | The sequence AAH37445.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Mitosis Ubl conjugation pathway |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Zinc-finger |
| Ligand | Metal-binding Zinc |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosisInferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic processInferred from direct assay Ref.1. Source: MGI protein ubiquitinationInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | nuclear membrane Inferred from electronic annotation. Source: Compara nucleusInferred from direct assay Ref.1. Source: MGI |
| Molecular_function | zinc ion binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q80YV2-1) 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. | ||||||
| Isoform 2 (identifier: Q80YV2-2) The sequence of this isoform differs from the canonical sequence as follows: 480-501: SLSEKSRKVFRIFRQWESSSSS → LK | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 501 | 501 | Nuclear-interacting partner of ALK | PRO_0000096850 | |||||
Regions | |||||||||
| Zinc finger | 102 – 156 | 55 | C3HC-type | ||||||
| Region | 170 – 210 | 41 | F-box-like | ||||||
| Motif | 395 – 401 | 7 | Nuclear localization signal By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 24 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 28 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 58 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 62 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 320 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 328 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 332 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 334 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 337 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 343 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 353 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 358 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 369 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 383 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 394 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 480 – 501 | 22 | SLSEK…SSSSS → LK in isoform 2. | VSP_015219 | |||||
Experimental info | |||||||||
| Sequence conflict | 65 | 1 | A → S in CAD61162. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification and characterization of a nuclear interacting partner of anaplastic lymphoma kinase (NIPA)." Ouyang T., Bai R.-Y., Bassermann F., von Klitzing C., Klumpen S., Miething C., Morris S.W., Peschel C., Duyster J. J. Biol. Chem. 278:30028-30036(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE FUNCTION. Strain: Swiss Webster. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J and NOD. Tissue: Bone marrow, Placenta and Thymus. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J, FVB/N and FVB/N-3. Tissue: Embryo and Mammary tumor. |
| [4] | "Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Embryonic brain. |
| [5] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-369, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ537495 mRNA. Translation: CAD61162.1. AK088527 mRNA. Translation: BAC40404.1. AK151694 mRNA. Translation: BAE30618.1. AK167465 mRNA. Translation: BAE39549.1. BC024560 mRNA. Translation: AAH24560.1. BC037445 mRNA. Translation: AAH37445.1. Different initiation. BC050141 mRNA. Translation: AAH50141.1. |
| IPI | IPI00465879. IPI00649674. |
| RefSeq | NP_766323.1. NM_172735.2. |
| UniGene | Mm.29780. Mm.474686. |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q80YV2. |
Proteomic databases | |
| PaxDb | Q80YV2. |
| PRIDE | Q80YV2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000080812; ENSMUSP00000079627; ENSMUSG00000039130. ENSMUST00000102992; ENSMUSP00000100057; ENSMUSG00000039130. |
| GeneID | 232679. |
| KEGG | mmu:232679. |
| UCSC | uc009bfc.1. mouse. uc009bfd.1. mouse. |
Organism-specific databases | |
| CTD | 51530. |
| MGI | MGI:1916023. Zc3hc1. |
Phylogenomic databases | |
| eggNOG | NOG246473. |
| GeneTree | ENSGT00390000006086. |
| HOGENOM | HOG000039985. |
| HOVERGEN | HBG082030. |
| InParanoid | Q80YV2. |
| OMA | FWPDSPC. |
Enzyme and pathway databases | |
| UniPathway | UPA00143. |
Gene expression databases | |
| ArrayExpress | Q80YV2. |
| Bgee | Q80YV2. |
| CleanEx | MM_ZC3HC1. |
| Genevestigator | Q80YV2. |
| GermOnline | ENSMUSG00000039130. Mus musculus. |
Family and domain databases | |
| InterPro | IPR013909. NIPA/Rsm1. IPR012935. Znf_C3HC-like. [Graphical view] |
| Pfam | PF08600. Rsm1. 1 hit. PF07967. zf-C3HC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 381189. |
| SOURCE | Search... |
Entry information
| Entry name | NIPA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q80YV2 Secondary accession number(s): Q3TJE6 Q8R3U7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
