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Reviewed, UniProtKB/Swiss-Prot Q8N4C6 (NIN_HUMAN)

Last modified February 9, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ninein
      Short name=hNinein
Alternative name(s):
    Glycogen synthase kinase 3 beta-interacting protein
      Short name=GSK3B-interacting protein
Gene names
Name: NIN
Synonyms: KIAA1565
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2090 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Centrosomal protein required in the positioning and anchorage of the microtubule minus-end in epithelial cells. May also act as a centrosome maturation factor. May play a role in microtubule nucleation. Overexpression does not perturb nucleation or elongation of microtubules but suppresses release of microtubules. Ref.3

Subunit structure

Homooligomer. Interacts with GSK3B (GSK3-beta) via its C-terminus domain. Interacts with C14ORF166, such interaction may prevent its phosphorylation by GSK3-beta. Ref.1 Ref.12 Ref.13

Subcellular location

Cytoplasmcytoskeletoncentrosome. Note: Component of the core centrosome. Arranged in a tubular conformation with an open and a closed end within the centrosome. In the mother centrosome, it localizes at both ends of the centrosome tube, including the site of centrosome duplication, while in the daughter centrosome it is present only at the closed end. Requires PCM1 for centrosome localization. Ref.3 Ref.1 Ref.12 Ref.10 Ref.11

Tissue specificity

Ubiquitous. Highly expressed in heart and skeletal muscle. Isoform 1 is more expressed than isoform 5. Ref.1 Ref.2

Developmental stage

In interphase cells, it is localized in the centrosome. Decreases in metaphase and anaphase and reappears in telophase. Ref.12

Domain

The coiled coil region from Asn-1611 to Pro-1693 is necessary and sufficient for the targeting to centrosome.

Post-translational modification

Phosphorylated by Aurora A (AIK) and PKA kinases but not CK2 or Aurora B (AIM). Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.12 Ref.16 Ref.17 Ref.18

Involvement in disease

Antibodies against NIN are present in sera from patients with autoimmune diseases that developed autoantibodies against centrosomal proteins. Ref.14 Ref.15

Sequence similarities

Contains 5 EF-hand domains.

Sequence caution

The sequence AAH65521.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandGTP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcentrosome localization

Traceable author statement. Source: HGNC

   Cellular componentcentrosome Ref.12

Inferred from direct assay. Source: HGNC

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.12 Ref.13

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C14orf166Q9Y2243EBI-1164022,EBI-1104547
GSK3BP498411EBI-1164022,EBI-373586

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N4C6-1)

Also known as: Lm;

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: Q8N4C6-2)

Also known as: Isotype 3;

The sequence of this isoform differs from the canonical sequence as follows:
     492-508: Missing.
Isoform 3 (identifier: Q8N4C6-3)

Also known as: Isotype 2;

The sequence of this isoform differs from the canonical sequence as follows:
     492-508: Missing.
     2065-2090: VSLPGHLCSPTSHSSFNSSFTSLYCH → LCKNTKADAMVKDLYVENAQVC
Isoform 4 (identifier: Q8N4C6-4)

Also known as: Isotype 1;

The sequence of this isoform differs from the canonical sequence as follows:
     492-508: Missing.
     2027-2046: GNQEQLVTVMEERMIEVEQK → ALLPEQRAVHADSYRRIGHL
     2047-2090: Missing.
Isoform 5 (identifier: Q8N4C6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MDEVEQDQHEARLKELFDSFDTTGTGSLGQEELTD → MAEVTVPRVY...HRKIQHVKNE
Isoform 6 (identifier: Q8N4C6-6)

The sequence of this isoform differs from the canonical sequence as follows:
     800-1512: Missing.
     1555-1555: Missing.
     1960-1988: MQHLRSTATPSPSPHAWDLQLLQQQACPM → NSVVGSSREGCSSLPEIVCEDAAPEVHCDA
     1989-2090: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q8N4C6-7)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     2065-2090: VSLPGHLCSPTSHSSFNSSFTSLYCH → LCKNTKADAM...PLTSTPPLRS
Isoform 8 (identifier: Q8N4C6-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MDEVEQDQHEARLKELFD → SALGAAVPLPPPSPECASGHGSRGGAGRLSPGTQALEAGCRLCGRSGETDR
Note: Incomplete sequence. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20902090Ninein
PRO_0000096844

Regions

Domain8 – 4336EF-hand 1
Domain42 – 7736EF-hand 2
Domain182 – 21736EF-hand 3
Domain219 – 25234EF-hand 4
Domain317 – 35236EF-hand 5
Nucleotide binding245 – 2528GTP Potential
Nucleotide binding300 – 3045GTP Potential
Nucleotide binding420 – 4234GTP Potential
Coiled coil357 – 570214 Potential
Coiled coil625 – 1027403 Potential
Coiled coil1068 – 109932 Potential
Coiled coil1181 – 1341161 Potential
Coiled coil1441 – 1816376 Potential
Coiled coil1854 – 188532 Potential
Coiled coil1922 – 2067146 Potential

Amino acid modifications

Modified residue15501Phosphoserine Ref.16 Ref.17 Ref.18

Natural variations

Alternative sequence1 – 3535MDEVE…EELTD → MAEVTVPRVYVVFGIHCIMA KASSDVQVSGFHRKIQHVKN E in isoform 5.
VSP_010950
Alternative sequence1 – 1818MDEVE…KELFD → SALGAAVPLPPPSPECASGH GSRGGAGRLSPGTQALEAGC RLCGRSGETDR in isoform 8.
VSP_010951
Alternative sequence492 – 50817Missing in isoform 2, isoform 3 and isoform 4.
VSP_010952
Alternative sequence800 – 1512713Missing in isoform 6.
VSP_010953
Alternative sequence15551Missing in isoform 6.
VSP_010954
Alternative sequence1960 – 198829MQHLR…QACPM → NSVVGSSREGCSSLPEIVCE DAAPEVHCDA in isoform 6.
VSP_010955
Alternative sequence1989 – 2090102Missing in isoform 6.
VSP_010956
Alternative sequence2027 – 204620GNQEQ…EVEQK → ALLPEQRAVHADSYRRIGHL in isoform 4.
VSP_010957
Alternative sequence2047 – 209044Missing in isoform 4.
VSP_010958
Alternative sequence2065 – 209026VSLPG…SLYCH → LCKNTKADAMVKDLYVENAQ VC in isoform 3.
VSP_010959
Alternative sequence2065 – 209026VSLPG…SLYCH → LCKNTKADAMVKDLYVENAQ LLKALEVTEQRQKTAEKKNY LLEEKIASLSNIVRNLTPAP LTSTPPLRS in isoform 7.
VSP_010960
Natural variant11111P → A: dbSNP rs2236316.
VAR_019453
Natural variant11251P → Q: dbSNP rs12882191.
VAR_051235
Natural variant13201E → G: dbSNP rs2073347. Ref.19
VAR_019454
Natural variant18371S → T: dbSNP rs12717411.
VAR_019455
Natural variant19341Q → E: dbSNP rs2295847.
VAR_051236

Experimental info

Sequence conflict4 – 52VE → LD in AAK00628. Ref.3
Sequence conflict4 – 52VE → LD in AAK00629. Ref.3
Sequence conflict10 – 112EA → G in AAK00628. Ref.3
Sequence conflict10 – 112EA → G in AAK00629. Ref.3
Sequence conflict151E → D in AAK00628. Ref.3
Sequence conflict151E → D in AAK00629. Ref.3
Sequence conflict151E → D in AAK00630. Ref.3
Sequence conflict1351P → A in AAK00628. Ref.3
Sequence conflict1351P → A in AAK00629. Ref.3
Sequence conflict1351P → A in AAK00630. Ref.3
Sequence conflict1371H → Y Ref.1
Sequence conflict1371H → Y Ref.2
Sequence conflict1771S → F in AAF23015. Ref.1
Sequence conflict2031N → D in AAG33512. Ref.2
Sequence conflict2231M → I in AAG33512. Ref.2
Sequence conflict264 – 2685LKRHL → TKKAPF in AAK00628. Ref.3
Sequence conflict264 – 2685LKRHL → TKKAPF in AAK00629. Ref.3
Sequence conflict2951F → I in AAG33512. Ref.2
Sequence conflict3481N → Y in AAK00628. Ref.3
Sequence conflict3481N → Y in AAK00629. Ref.3
Sequence conflict3481N → Y in AAK00630. Ref.3
Sequence conflict3571I → T in AAK00628. Ref.3
Sequence conflict3571I → T in AAK00629. Ref.3
Sequence conflict3571I → T in AAK00630. Ref.3
Sequence conflict3691I → V in AAG33512. Ref.2
Sequence conflict3991L → S in AAG33512. Ref.2
Sequence conflict5681L → F in AAG33512. Ref.2
Sequence conflict8091R → I in AAF23015. Ref.1
Sequence conflict8121S → T in AAG33512. Ref.2
Sequence conflict9321L → M in AAK00628. Ref.3
Sequence conflict9321L → M in AAK00629. Ref.3
Sequence conflict9321L → M in AAK00630. Ref.3
Sequence conflict9451K → I in AAG33512. Ref.2
Sequence conflict9771D → A in AAG33512. Ref.2
Sequence conflict9801R → G in AAF23015. Ref.1
Sequence conflict10341S → N in AAK00628. Ref.3
Sequence conflict10341S → N in AAK00629. Ref.3
Sequence conflict10341S → N in AAK00630. Ref.3
Sequence conflict10541Q → H in AAG33512. Ref.2
Sequence conflict10671L → F in AAG33512. Ref.2
Sequence conflict10701L → Q in AAF23015. Ref.1
Sequence conflict11501D → G in AAF23015. Ref.1
Sequence conflict11681V → A in AAK00628. Ref.3
Sequence conflict11681V → A in AAK00629. Ref.3
Sequence conflict11681V → A in AAK00630. Ref.3
Sequence conflict12371M → I in AAF23015. Ref.1
Sequence conflict1548 – 15558NGSQEEMW → YWNSGRMR in AAK00628. Ref.3
Sequence conflict18591L → S in AAK00628. Ref.3
Sequence conflict18591L → S in AAK00629. Ref.3
Sequence conflict18591L → S in AAK00630. Ref.3
Sequence conflict1865 – 18695NTKAE → EHQSR in AAK00630. Ref.3

Sequences

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

Last modified July 19, 2004. Version 3.
Checksum: F71E610FF9B7792E

FASTA2,090243,290
        10         20         30         40         50         60 
MDEVEQDQHE ARLKELFDSF DTTGTGSLGQ EELTDLCHML SLEEVAPVLQ QTLLQDNLLG 

        70         80         90        100        110        120 
RVHFDQFKEA LILILSRTLS NEEHFQEPDC SLEAQPKYVR GGKRYGRRSL PEFQESVEEF 

       130        140        150        160        170        180 
PEVTVIEPLD EEARPSHIPA GDCSEHWKTQ RSEEYEAEGQ LRFWNPDDLN ASQSGSSPPQ 

       190        200        210        220        230        240 
DWIEEKLQEV CEDLGITRDG HLNRKKLVSI CEQYGLQNVD GEMLEEVFHN LDPDGTMSVE 

       250        260        270        280        290        300 
DFFYGLFKNG KSLTPSASTP YRQLKRHLSM QSFDESGRRT TTSSAMTSTI GFRVFSCLDD 

       310        320        330        340        350        360 
GMGHASVERI LDTWQEEGIE NSQEILKALD FSLDGNINLT ELTLALENEL LVTKNSIHQA 

       370        380        390        400        410        420 
ALASFKAEIR HLLERVDQVV REKEKLRSDL DKAEKLKSLM ASEVDDHHAA IERRNEYNLR 

       430        440        450        460        470        480 
KLDEEYKERI AALKNELRKE REQILQQAGK QRLELEQEIE KAKTEENYIR DRLALSLKEN 

       490        500        510        520        530        540 
SRLENELLEN AEKLAEYENL TNKLQRNLEN VLAEKFGDLD PSSAEFFLQE ERLTQMRNEY 

       550        560        570        580        590        600 
ERQCRVLQDQ VDELQSELEE YRAQGRVLRL PLKNSPSEEV EANSGGIEPE HGLGSEECNP 

       610        620        630        640        650        660 
LNMSIEAELV IEQMKEQHHR DICCLRLELE DKVRHYEKQL DETVVSCKKA QENMKQRHEN 

       670        680        690        700        710        720 
ETHTLEKQIS DLKNEIAELQ GQAAVLKEAH HEATCRHEEE KKQLQVKLEE EKTHLQEKLR 

       730        740        750        760        770        780 
LQHEMELKAR LTQAQASFER EREGLQSSAW TEEKVRGLTQ ELEQFHQEQL TSLVEKHTLE 

       790        800        810        820        830        840 
KEELRKELLE KHQRELQEGR EKMETECNRR TSQIEAQFQS DCQKVTERCE SALQSLEGRY 

       850        860        870        880        890        900 
RQELKDLQEQ QREEKSQWEF EKDELTQECA EAQELLKETL KREKTTSLVL TQEREMLEKT 

       910        920        930        940        950        960 
YKEHLNSMVV ERQQLLQDLE DLRNVSETQQ SLLSDQILEL KSSHKRELRE REEVLCQAGA 

       970        980        990       1000       1010       1020 
SEQLASQRLE RLEMEHDQER QEMMSKLLAM ENIHKATCET ADRERAEMST EISRLQSKIK 

      1030       1040       1050       1060       1070       1080 
EMQQATSPLS MLQSGCQVIG EEEVEGDGAL SLLQQGEQLL EENGDVLLSL QRAHEQAVKE 

      1090       1100       1110       1120       1130       1140 
NVKMATEISR LQQRLQKLEP GLVMSSCLDE PATEFFGNTA EQTEPFLQQN RTKQVEGVTR 

      1150       1160       1170       1180       1190       1200 
RHVLSDLEDD EVRDLGSTGT SSVQRQEVKI EESEASVEGF SELENSEETR TESWELKNQI 

      1210       1220       1230       1240       1250       1260 
SQLQEQLMML CADCDRASEK KQDLLFDVSV LKKKLKMLER IPEASPKYKL LYEDVSREND 

      1270       1280       1290       1300       1310       1320 
CLQEELRMME TRYDEALENN KELTAEVFRL QDELKKMEEV TETFLSLEKS YDEVKIENEE 

      1330       1340       1350       1360       1370       1380 
LNVLVLRLQG KIEKLQESVV QRCDCCLWEA SLENLEIEPD GNILQLNQTL EECVPRVRSV 

      1390       1400       1410       1420       1430       1440 
HHVIEECKQE NQYLEGNTQL LEKVKAHEIA WLHGTIQTHQ ERPRVQNQVI LEENTTLLGF 

      1450       1460       1470       1480       1490       1500 
QDKHFQHQAT IAELELEKTK LQELTRKLKE RVTILVKQKD VLSHGEKEEE LKAMMHDLQI 

      1510       1520       1530       1540       1550       1560 
TCSEMQQKVE LLRYESEKLQ QENSILRNEI TTLNEEDSIS NLKLGTLNGS QEEMWQKTET 

      1570       1580       1590       1600       1610       1620 
VKQENAAVQK MVENLKKQIS ELKIKNQQLD LENTELSQKN SQNQEKLQEL NQRLTEMLCQ 

      1630       1640       1650       1660       1670       1680 
KEKEPGNSAL EEREQEKFNL KEELERCKVQ SSTLVSSLEA ELSEVKIQTH IVQQENHLLK 

      1690       1700       1710       1720       1730       1740 
DELEKMKQLH RCPDLSDFQQ KISSVLSYNE KLLKEKEALS EELNSCVDKL AKSSLLEHRI 

      1750       1760       1770       1780       1790       1800 
ATMKQEQKSW EHQSASLKSQ LVASQEKVQN LEDTVQNVNL QMSRMKSDLR VTQQEKEALK 

      1810       1820       1830       1840       1850       1860 
QEVMSLHKQL QNAGGKSWAP EIATHPSGLH NQQKRLSWDK LDHLMNEEQQ LLWQENERLQ 

      1870       1880       1890       1900       1910       1920 
TMVQNTKAEL THSREKVRQL ESNLLPKHQK HLNPSGTMNP TEQEKLSLKR ECDQFQKEQS 

      1930       1940       1950       1960       1970       1980 
PANRKVSQMN SLEQELETIH LENEGLKKKQ VKLDEQLMEM QHLRSTATPS PSPHAWDLQL 

      1990       2000       2010       2020       2030       2040 
LQQQACPMVP REQFLQLQRQ LLQAERINQH LQEELENRTS ETNTPQGNQE QLVTVMEERM 

      2050       2060       2070       2080       2090 
IEVEQKLKLV KRLLQEKVNQ LKEQVSLPGH LCSPTSHSSF NSSFTSLYCH 

« Hide

Isoform 2 (Isotype 3).

Checksum: DE8238722E9D83F9
Show »

FASTA2,073241,232
Isoform 3 (Isotype 2).

Checksum: 607083A99006772F
Show »

FASTA2,069240,892
Isoform 4 (Isotype 1).

Checksum: A3C86C82FE273FA2
Show »

FASTA2,029236,176
Isoform 5.

Checksum: 949937215250D157
Show »

FASTA2,096243,930
Isoform 6.

Checksum: A34D34D74D9B861C
Show »

FASTA1,275147,799
Isoform 7 (B).

Checksum: 4772D23E47C8EF23
Show »

FASTA2,133248,235
Isoform 8.

Checksum: DB76830A02798077
Show »

FASTA2,123245,974

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta."
Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K., Howng S.-L.
Biochim. Biophys. Acta 1492:513-516(2000) [PubMed: 11004522] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH GSK3B.
Tissue: Fetal liver.
[2]"Genomic organization and molecular characterization of the human ninein gene."
Hong Y.-R., Chen C.-H., Chuo M.-H., Liou S.-Y., Howng S.-L.
Biochem. Biophys. Res. Commun. 279:989-995(2000) [PubMed: 11162463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"Human ninein is a centrosomal autoantigen recognized by CREST patient sera and plays a regulatory role in microtubule nucleation."
Stillwell E.E., Zhou J., Joshi H.C.
Cell Cycle 3:923-930(2004) [PubMed: 15190203] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
Tissue: Thymus.
[4]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed: 10997877] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed: 12508121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] OF 1-434 (ISOFORM 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1877-2090 (ISOFORM 4).
Tissue: Lymph.
[8]"3' isoforms of human ninein."
Choquette M.C., de Medicis E.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1561-2090 (ISOFORM 7).
Tissue: Bone marrow.
[9]"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] OF 1928-2090 (ISOFORM 7).
Tissue: Hepatoma.
[10]"CEP110 and ninein are located in a specific domain of the centrosome associated with centrosome maturation."
Ou Y.Y., Mack G.J., Zhang M., Rattner J.B.
J. Cell Sci. 115:1825-1835(2002) [PubMed: 11956314] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Assembly of centrosomal proteins and microtubule organization depends on PCM-1."
Dammermann A., Merdes A.
J. Cell Biol. 159:255-266(2002) [PubMed: 12403812] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Molecular characterization of human ninein protein: two distinct subdomains required for centrosomal targeting and regulating signals in cell cycle."
Chen C.-H., Howng S.-L., Cheng T.-S., Chou M.-H., Huang C.-Y., Hong Y.-R.
Biochem. Biophys. Res. Commun. 308:975-983(2003) [PubMed: 12927815] [Abstract]
Cited for: HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
[13]"A novel ninein-interaction protein, CGI-99, blocks ninein phosphorylation by GSK3beta and is highly expressed in brain tumors."
Howng S.-L., Hsu H.-C., Cheng T.-S., Lee Y.-L., Chang L.-K., Lu P.-J., Hong Y.-R.
FEBS Lett. 566:162-168(2004) [PubMed: 15147888] [Abstract]
Cited for: INTERACTION WITH C14ORF166.
[14]"Autoantibodies to a group of centrosomal proteins in human autoimmune sera reactive with the centrosome."
Mack G.J., Rees J., Sandblom O., Balczon R., Fritzler M.J., Rattner J.B.
Arthritis Rheum. 41:551-558(1998) [PubMed: 9506584] [Abstract]
Cited for: DISEASE.
[15]"Spectrum of centrosome autoantibodies in childhood varicella and post-varicella acute cerebellar ataxia."
Fritzler M.J., Zhang M., Stinton L.M., Rattner J.B.
BMC Pediatr. 3:11-11(2003) [PubMed: 14503922] [Abstract]
Cited for: DISEASE.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1550, MASS SPECTROMETRY.
[17]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1550, MASS SPECTROMETRY.
[18]"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-1550, MASS SPECTROMETRY.
Tissue: T-cell.
[19]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed: 18987736] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-1320.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF212162 mRNA. Translation: AAF23015.2.
AF302773 mRNA. Translation: AAG33512.2.
AF223937 mRNA. Translation: AAK00628.1.
AF223938 mRNA. Translation: AAK00629.1.
AF223939 mRNA. Translation: AAK00630.1.
AB046785 mRNA. Translation: BAB13391.2. Different initiation.
AL133485 Genomic DNA. No translation available.
AL606834 Genomic DNA. No translation available.
BC034708 mRNA. Translation: AAH34708.2.
BC065521 mRNA. Translation: AAH65521.1. Sequence problems.
AY027794 mRNA. Translation: AAK27375.1.
AY027795 mRNA. Translation: AAK27376.1.
AY027796 mRNA. Translation: AAK27377.1.
AF186776 mRNA. Translation: AAG17027.1.
AK027054 mRNA. Translation: BAB15640.1. Different initiation.
IPIIPI00171791.
IPI00329695.
IPI00441952.
IPI00441955.
IPI00441959.
IPI00441960.
IPI00883941.
IPI00921003.
RefSeqNP_057434.3.
NP_065972.3.
NP_891989.2.
NP_891991.1.
UniGeneHs.310429

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8N4C6. 2 interactions.
STRINGQ8N4C6.

PTM databases

PhosphoSiteQ8N4C6.

Proteomic databases

PRIDEQ8N4C6.

Genome annotation databases

EnsemblENST00000382041; ENSP00000371472; ENSG00000100503; Homo sapiens. [Genome view]
GeneID51199.
KEGGhsa:51199.
UCSCuc001wyi.1. human.
uc001wym.1. human.
uc010anx.1. human.

Organism-specific databases

CTD51199.
GeneCardsGC14M050256.
H-InvDBHIX0011645.
HGNCHGNC:14906. NIN.
MIM608684. gene.
PharmGKBPA31630.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8N4C6.

Gene expression databases

ArrayExpressQ8N4C6.
BgeeQ8N4C6.
GenevestigatorQ8N4C6.
GermOnlineENSG00000100503. Homo sapiens.

Family and domain databases

InterProIPR018249. EF_HAND_2.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio54220.
SOURCESearch...

Entry information

Entry nameNIN_HUMAN
AccessionPrimary (citable) accession number: Q8N4C6
Secondary accession number(s): Q6P0P6 expand/collapse secondary AC list , Q9BWU6, Q9C012, Q9C013, Q9C014, Q9H5I6, Q9HAT7, Q9HBY5, Q9HCK7, Q9UH61
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents