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Q80YV2 (NIPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:Zc3hc1
Synonyms:Nipa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Protein modification; protein ubiquitination.

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 501500Nuclear-interacting partner of ALK
PRO_0000096850

Regions

Zinc finger102 – 15655C3HC-type
Region170 – 21041F-box-like
Motif395 – 4017Nuclear localization signal By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue241Phosphoserine By similarity
Modified residue281Phosphothreonine By similarity
Modified residue581Phosphoserine By similarity
Modified residue621Phosphoserine Ref.4
Modified residue3201Phosphoserine By similarity
Modified residue3281Phosphoserine By similarity
Modified residue3321Phosphothreonine By similarity
Modified residue3341Phosphoserine By similarity
Modified residue3371Phosphoserine By similarity
Modified residue3431Phosphoserine By similarity
Modified residue3531Phosphoserine By similarity
Modified residue3581Phosphoserine By similarity
Modified residue3691Phosphoserine By similarity
Modified residue3831Phosphothreonine By similarity
Modified residue3941Phosphoserine By similarity

Natural variations

Alternative sequence480 – 50122SLSEK…SSSSS → LK in isoform 2.
VSP_015219

Experimental info

Sequence conflict651A → S in CAD61162. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1FB522C93F8A8178

FASTA50155,196
        10         20         30         40         50         60 
MAATSEGPLF AASIEKTWGS VVRSPEGTPQ KVRELIDEGI VPEEGGTEPK DTAATFQSVD 

        70         80         90        100        110        120 
GSPQAEQSPL ESTSKEAFFH RVETFSSLKW AGKPPELSPL ICAKYGWVTV ECDMLKCSSC 

       130        140        150        160        170        180 
QAFLCASLQP TFDFGRYKER CAELKKSLCS AHEKFCFWPD SPSPDRFGML PLGEPAVLIS 

       190        200        210        220        230        240 
EFLDRFQSLC HLDLQLPSLR PEDLKTMCLT EDAVSALLHL LEDELDFHAD DRKTTSKLGS 

       250        260        270        280        290        300 
DVQVQATACV LSLCGWACSS LEPTQLSLIT CYQCMRKVGL WGFQQIESSM TDLEASFGLT 

       310        320        330        340        350        360 
SSPIPGVEGR PEHFPLVPES PRRMMTRSQD ATVSPGSEQS EKSPGPIVSR TRSWESSSPV 

       370        380        390        400        410        420 
DRPELEAASP TTRSRPVTRS MGTGDSAGVE VPSSPLRRTK RARLCSSSSS DTSPRSFFDP 

       430        440        450        460        470        480 
TSQHRDWCPW VNITLVKETK ENGETEVDAC TPAEPGWKAV LTILLAHKRS NQPAETDSMS 

       490        500 
LSEKSRKVFR IFRQWESSSS S 

« Hide

Isoform 2 [UniParc].

Checksum: F173139617A1A3AD
Show »

FASTA48152,824

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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+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.
CCDSCCDS19970.1. [Q80YV2-2]
RefSeqNP_766323.1. NM_172735.2. [Q80YV2-2]
XP_006505126.1. XM_006505063.1. [Q80YV2-1]
XP_006505127.1. XM_006505064.1. [Q80YV2-2]
UniGeneMm.29780.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80YV2. 1 interaction.
MINTMINT-4112467.

PTM databases

PhosphoSiteQ80YV2.

Proteomic databases

MaxQBQ80YV2.
PaxDbQ80YV2.
PRIDEQ80YV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080812; ENSMUSP00000079627; ENSMUSG00000039130. [Q80YV2-1]
ENSMUST00000102992; ENSMUSP00000100057; ENSMUSG00000039130. [Q80YV2-2]
GeneID232679.
KEGGmmu:232679.
UCSCuc009bfc.1. mouse. [Q80YV2-1]
uc009bfd.1. mouse. [Q80YV2-2]

Organism-specific databases

CTD51530.
MGIMGI:1916023. Zc3hc1.

Phylogenomic databases

eggNOGNOG246473.
GeneTreeENSGT00390000006086.
HOGENOMHOG000039985.
HOVERGENHBG082030.
InParanoidQ80YV2.
OMAKWAGKPS.
OrthoDBEOG7TXKGG.
PhylomeDBQ80YV2.
TreeFamTF314674.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ80YV2.
BgeeQ80YV2.
CleanExMM_ZC3HC1.
GenevestigatorQ80YV2.

Family and domain databases

InterProIPR013909. NIPA/Rsm1.
IPR012935. Znf_C3HC-like.
[Graphical view]
PfamPF08600. Rsm1. 1 hit.
PF07967. zf-C3HC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381189.
PROQ80YV2.
SOURCESearch...

Entry information

Entry nameNIPA_MOUSE
AccessionPrimary (citable) accession number: Q80YV2
Secondary accession number(s): Q3TJE6 expand/collapse secondary AC list , Q80Z11, Q8BTW5, Q8CI56, Q8R3U7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot