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Q86WB0 (NIPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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=hNIPA
Zinc finger C3HC-type protein 1
Gene names
Name:ZC3HC1
Synonyms:NIPA
ORF Names:HSPC216
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length502 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. May have an antiapoptotic role in NPM-ALK-mediated signaling events. Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with the NPM-ALK fusion protein in a tyrosine phosphorylation-dependent manner. Interacts with SKP1. Component of a SCF(NIPA) E3 complex with SKP1, RBX1 and CUL1 when not phosphorylated on Ser-354. Interacts with CCNB1. Ref.1 Ref.6

Subcellular location

Nucleus Ref.1.

Tissue specificity

Widely expressed. Highly expressed in heart, skeletal muscle and testis. Expressed in brain, placenta, lung, kidney, liver, pancreas, spleen, thymus, prostate, ovary small intestine and colon. Weakly or not expressed in leukocytes. Ref.1

Developmental stage

Weakly expressed in G0/G1 phases, abundant during S and G2/M phases, and strongly decreases thereafter. Ref.6

Domain

The F-box-like region is required for the interaction with SKP1. Ref.6

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-354 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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Sequence similarities

Contains 1 C3HC-type zinc finger.

Caution

Reported to contain a F-box domain (Ref.6). Such domain is however not predicted by any detection method.

Sequence caution

The sequence AAF36136.1 differs from that shown. Reason: Frameshift at positions 93, 187 and 220.

The sequence AAH28917.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAS07546.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAS07547.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnuclear membrane

Inferred from direct assay. Source: HPA

   Molecular functionprotein kinase binding

Inferred from physical interaction. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86WB0-1)

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: Q86WB0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MAAPCEGQAF...IAPEEGGVDA → MRGLPRKREAWTQPHPLEALYESLRVLE
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86WB0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     341-411: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 502501Nuclear-interacting partner of ALK
PRO_0000096849

Regions

Zinc finger102 – 15655C3HC-type
Region170 – 21041F-box-like
Motif396 – 4027Nuclear localization signal Ref.1

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue241Phosphoserine Ref.7 Ref.8 Ref.10 Ref.13
Modified residue281Phosphothreonine Ref.7 Ref.8 Ref.13
Modified residue581Phosphoserine Ref.14 Ref.16
Modified residue621Phosphoserine Ref.14 Ref.16
Modified residue841Phosphothreonine Ref.10
Modified residue3211Phosphoserine Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
Modified residue3331Phosphothreonine Ref.13
Modified residue3351Phosphoserine Ref.13 Ref.14 Ref.16
Modified residue3381Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16
Modified residue3441Phosphoserine Ref.13 Ref.14 Ref.16
Modified residue3541Phosphoserine Ref.1 Ref.7 Ref.13 Ref.16
Modified residue3571Phosphoserine Ref.13
Modified residue3591Phosphoserine Ref.16
Modified residue3701Phosphoserine Ref.9 Ref.13 Ref.16
Modified residue3841Phosphothreonine Ref.13
Modified residue3871Phosphothreonine Ref.13 Ref.14 Ref.16
Modified residue3941Phosphoserine Ref.13
Modified residue3951Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.16

Natural variations

Alternative sequence1 – 4949MAAPC…GGVDA → MRGLPRKREAWTQPHPLEAL YESLRVLE in isoform 2.
VSP_015217
Alternative sequence341 – 41171Missing in isoform 3.
VSP_015218
Natural variant2711T → A. Ref.5
Corresponds to variant rs1464890 [ dbSNP | Ensembl ].
VAR_023312
Natural variant3631R → H. Ref.5
Corresponds to variant rs11556924 [ dbSNP | Ensembl ].
VAR_023313

Experimental info

Mutagenesis1051Y → F: Does not strongly affect phosphorylation status; when associated with F-137. Ref.1
Mutagenesis1371Y → F: Does not strongly affect phosphorylation status; when associated with F-105. Ref.1
Mutagenesis170 – 1712LP → FM: Abolishes interaction with SKP1.
Mutagenesis3541S → A: Strongly reduces phosphorylation and induces the formation of a constitutive SCF(NIPA) E3 complex that degrades CCNB1 at G2/M phase and delays mitotic entry. Ref.1 Ref.6
Mutagenesis398 – 4014RKAK → AAAA: Induces a complete cytoplasmic redistribution. Ref.1
Mutagenesis3991K → P: Induces a partial cytoplasmic redistribution. Ref.1
Sequence conflict1791V → I in BAB14024. Ref.3
Sequence conflict2781K → R in AAF36136. Ref.2

Sequences

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

Last modified June 1, 2003. Version 1.
Checksum: D5DEDF9E30070586

FASTA50255,262
        10         20         30         40         50         60 
MAAPCEGQAF AVGVEKNWGA VVRSPEGTPQ KIRQLIDEGI APEEGGVDAK DTSATSQSVN 

        70         80         90        100        110        120 
GSPQAEQPSL ESTSKEAFFS RVETFSSLKW AGKPFELSPL VCAKYGWVTV ECDMLKCSSC 

       130        140        150        160        170        180 
QAFLCASLQP AFDFDRYKQR CAELKKALCT AHEKFCFWPD SPSPDRFGML PLDEPAILVS 

       190        200        210        220        230        240 
EFLDRFQSLC HLDLQLPSLR PEDLKTMCLT EDKISLLLHL LEDELDHRTD ERKTTIKLGS 

       250        260        270        280        290        300 
DIQVHVTACI LSVCGWACSS SLESMQLSLI TCSQCMRKVG LWGFQQIESS MTDLDASFGL 

       310        320        330        340        350        360 
TSSPIPGLEG RPERLPLVPE SPRRMMTRSQ DATFSPGSEQ AEKSPGPIVS RTRSWDSSSP 

       370        380        390        400        410        420 
VDRPEPEAAS PTTRTRPVTR SMGTGDTPGL EVPSSPLRKA KRARLCSSSS SDTSSRSFFD 

       430        440        450        460        470        480 
PTSQHRDWCP WVNITLGKES RENGGTEPDA SAPAEPGWKA VLTILLAHKQ SSQPAETDSM 

       490        500 
SLSEKSRKVF RIFRQWESLC SC 

« Hide

Isoform 2 [UniParc].

Checksum: B0EF4F07386A8554
Show »

FASTA48153,559
Isoform 3 [UniParc].

Checksum: EC1DCB8077C127C7
Show »

FASTA43147,771

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: 12748172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH NPM-ALK FUSION PROTEIN, PHOSPHORYLATION AT SER-354, MUTAGENESIS OF TYR-105; TYR-137; SER-354; LYS-399 AND 398-ARG--LYS-401.
[2]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Umbilical cord blood.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Mammary gland.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ALA-271 AND HIS-363.
Tissue: Kidney and Mammary gland.
[6]"NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry."
Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J.
Cell 122:45-57(2005) [PubMed: 16009132] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, DOMAIN, INTERACTION WITH SKP1 AND CCNB1, IDENTIFICATION IN SCF(NIPA) COMPLEX WITH SKP1; CUL1 AND RBX1, MUTAGENESIS OF 170-LEU-PRO-171 AND SER-354.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-321 AND SER-354, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28 AND SER-321, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-84, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-395, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-395, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-321; THR-333; SER-335; SER-338; SER-344; SER-354; SER-357; SER-370; THR-384; THR-387; SER-394 AND SER-395, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-62; SER-321; SER-335; SER-338; SER-344; THR-387 AND SER-395, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, MASS SPECTROMETRY.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-62; SER-321; SER-335; SER-338; SER-344; SER-354; SER-359; SER-370; THR-387 AND SER-395, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ537494 mRNA. Translation: CAD61161.1.
AF151050 mRNA. Translation: AAF36136.1. Frameshift.
AK001317 mRNA. Translation: BAA91619.1.
AK022373 mRNA. Translation: BAB14024.1.
AC073320 Genomic DNA. Translation: AAS07546.1. Sequence problems.
AC073320 Genomic DNA. Translation: AAS07547.1. Sequence problems.
AC087071 Genomic DNA. No translation available.
BC011551 mRNA. Translation: AAH11551.1.
BC028917 mRNA. Translation: AAH28917.1. Different initiation.
IPIIPI00301421.
IPI00339382.
IPI00479595.
RefSeqNP_057562.3. NM_016478.3.
UniGeneHs.194157.

3D structure databases

ProteinModelPortalQ86WB0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ86WB0.

PTM databases

PhosphoSiteQ86WB0.

Polymorphism databases

DMDM73921220.

Proteomic databases

PRIDEQ86WB0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358303; ENSP00000351052; ENSG00000091732.
GeneID51530.
KEGGhsa:51530.
UCSCuc003vph.1. human.
uc003vpi.1. human.
uc010lma.1. human.

Organism-specific databases

CTD51530.
GeneCardsGC07M129658.
H-InvDBHIX0007070.
HGNCHGNC:29913. ZC3HC1.
HPAHPA019089.
HPA024023.
neXtProtNX_Q86WB0.
PharmGKBPA134931869.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00390000006086.
HOVERGENHBG082030.
InParanoidQ86WB0.
OMARFPLVPE.
OrthoDBEOG4B2SXH.

Gene expression databases

ArrayExpressQ86WB0.
BgeeQ86WB0.
CleanExHS_ZC3HC1.
GenevestigatorQ86WB0.
GermOnlineENSG00000091732. Homo sapiens.

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

NextBio55270.

Entry information

Entry nameNIPA_HUMAN
AccessionPrimary (citable) accession number: Q86WB0
Secondary accession number(s): A6NH66 expand/collapse secondary AC list , Q75MF3, Q75MF4, Q8N330, Q96F75, Q9HA34, Q9NVX4, Q9P0R0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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