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Protein

Ninein-like protein

Gene

NINL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the microtubule organization in interphase cells. Overexpression induces the fragmentation of the Golgi, and causes lysosomes to disperse toward the cell periphery; it also interferes with mitotic spindle assembly. May play a role in ovarian carcinogenesis.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi246 – 25712PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
SIGNORiQ9Y2I6.

Names & Taxonomyi

Protein namesi
Recommended name:
Ninein-like protein
Gene namesi
Name:NINL
Synonyms:KIAA0980, NLP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:29163. NINL.

Subcellular locationi

  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • Cytoplasm 1 Publication

  • Note: In interphase cells, NINL is transported to the centrosomes by the dynein-dynactin motor complex (PubMed:16254247). During centrosome maturation, PLK1 directly phosphorylates NINL resulting in its release into the cytoplasm (PubMed:16254247).

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi495 – 4973KEN → AAA: Disrupts binding to CDC20 and FZR1 and prevents ubiquitination and subsequent degradation of NINL; when associated with 633-A--A-636. 1 Publication
Mutagenesisi633 – 6364RTQL → AAAA: Disrupts binding to CDC20 and FZR1 and prevents ubiquitination and subsequent degradation of NINL; when associated with 495-A--A-497. 1 Publication

Organism-specific databases

PharmGKBiPA165392435.

Polymorphism and mutation databases

BioMutaiNINL.
DMDMi118601093.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13821382Ninein-like proteinPRO_0000259714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PLK1 which disrupts its centrosome association and interaction with gamma-tubulin.2 Publications
Ubiquitinated by the APC/C complex leading to its degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y2I6.
MaxQBiQ9Y2I6.
PaxDbiQ9Y2I6.
PRIDEiQ9Y2I6.

PTM databases

iPTMnetiQ9Y2I6.
PhosphoSiteiQ9Y2I6.

Expressioni

Tissue specificityi

Expressed in KYSE-150 esophageal carcinoma, HeLa cervical carcinoma and U2OS osteosarcoma cells. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase (at protein level). Expressed in fetal heart, skeletal muscle, liver, lung and cochlea, and in adult brain, testis, kidney and retina.2 Publications

Gene expression databases

BgeeiQ9Y2I6.
ExpressionAtlasiQ9Y2I6. baseline and differential.
GenevisibleiQ9Y2I6. HS.

Organism-specific databases

HPAiHPA000686.

Interactioni

Subunit structurei

Interacts with gamma-tubulin and TUBGCP4. Interacts with anaphase promoting complex/cyclosome (APC/C). Interacts with CDC20 and FZR1. Isoform 2 interacts with LCA5 and USH2A.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC146Q8IYE0-23EBI-719716,EBI-10247802
CCHCR1Q8TD31-33EBI-719716,EBI-10175300
FAM161AQ3B8203EBI-719716,EBI-719941
HAUS1Q96CS23EBI-719716,EBI-2514791
KAT5Q929933EBI-719716,EBI-399080
L3MBTL4Q8NA193EBI-719716,EBI-8833581
RBM41Q96IZ53EBI-719716,EBI-740773
RCOR3Q9P2K34EBI-719716,EBI-743428
SH2D4AQ9H7883EBI-719716,EBI-747035
ZNF417Q8TAU34EBI-719716,EBI-740727

Protein-protein interaction databases

BioGridi116630. 211 interactions.
IntActiQ9Y2I6. 198 interactions.
MINTiMINT-1408864.
STRINGi9606.ENSP00000278886.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2I6.
SMRiQ9Y2I6. Positions 9-70, 198-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 4236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini41 – 7636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini196 – 23136EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini233 – 26836EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili384 – 42441Sequence analysisAdd
BLAST
Coiled coili484 – 57996Sequence analysisAdd
BLAST
Coiled coili616 – 69984Sequence analysisAdd
BLAST
Coiled coili1046 – 1375330Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi495 – 4973KEN box
Motifi633 – 6419D-box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi296 – 2994Poly-Thr
Compositional biasi805 – 8106Poly-Glu

Domaini

The KEN and D (destructive) boxes are required for the cell cycle-controlled NINL degradation by the APC/C pathway.1 Publication

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IEH8. Eukaryota.
ENOG41128SZ. LUCA.
GeneTreeiENSGT00660000095541.
InParanoidiQ9Y2I6.
KOiK16477.
OMAiGIQNGRE.
OrthoDBiEOG7MWGWC.
PhylomeDBiQ9Y2I6.
TreeFamiTF325139.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2I6-1) [UniParc]FASTAAdd to basket

Also known as: A

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.

« Hide

        10         20         30         40         50
MDEEENHYVS QLREVYSSCD TTGTGFLDRQ ELTQLCLKLH LEQQLPVLLQ
60 70 80 90 100
TLLGNDHFAR VNFEEFKEGF VAVLSSNAGV RPSDEDSSSL ESAASSAIPP
110 120 130 140 150
KYVNGSKWYG RRSRPELCDA ATEARRVPEQ QTQASLKSHL WRSASLESVE
160 170 180 190 200
SPKSDEEAES TKEAQNELFE AQGQLQTWDS EDFGSPQKSC SPSFDTPESQ
210 220 230 240 250
IRGVWEELGV GSSGHLSEQE LAVVCQSVGL QGLEKEELED LFNKLDQDGD
260 270 280 290 300
GKVSLEEFQL GLFSHEPALL LESSTRVKPS KAWSHYQVPE ESGCHTTTTS
310 320 330 340 350
SLVSLCSSLR LFSSIDDGSG FAFPDQVLAM WTQEGIQNGR EILQSLDFSV
360 370 380 390 400
DEKVNLLELT WALDNELMTV DSAVQQAALA CYHQELSYQQ GQVEQLARER
410 420 430 440 450
DKARQDLERA EKRNLEFVKE MDDCHSTLEQ LTEKKIKHLE QGYRERLSLL
460 470 480 490 500
RSEVEAEREL FWEQAHRQRA ALEWDVGRLQ AEEAGLREKL TLALKENSRL
510 520 530 540 550
QKEIVEVVEK LSDSERLALK LQKDLEFVLK DKLEPQSAEL LAQEERFAAV
560 570 580 590 600
LKEYELKCRD LQDRNDELQA ELEGLWARLP KNRHSPSWSP DGRRRQLPGL
610 620 630 640 650
GPAGISFLGN SAPVSIETEL MMEQVKEHYQ DLRTQLETKV NYYEREIAAL
660 670 680 690 700
KRNFEKERKD MEQARRREVS VLEGQKADLE ELHEKSQEVI WGLQEQLQDT
710 720 730 740 750
ARGPEPEQMG LAPCCTQALC GLALRHHSHL QQIRREAEAE LSGELSGLGA
760 770 780 790 800
LPARRDLTLE LEEPPQGPLP RGSQRSEQLE LERALKLQPC ASEKRAQMCV
810 820 830 840 850
SLALEEEELE LARGKRVDGP SLEAEMQALP KDGLVAGSGQ EGTRGLLPLR
860 870 880 890 900
PGCGERPLAW LAPGDGRESE EAAGAGPRRR QAQDTEATQS PAPAPAPASH
910 920 930 940 950
GPSERWSRMQ PCGVDGDIVP KEPEPFGASA AGLEQPGARE LPLLGTERDA
960 970 980 990 1000
SQTQPRMWEP PLRPAASCRG QAERLQAIQE ERARSWSRGT QEQASEQQAR
1010 1020 1030 1040 1050
AEGALEPGCH KHSVEVARRG SLPSHLQLAD PQGSWQEQLA APEEGETKIA
1060 1070 1080 1090 1100
LEREKDDMET KLLHLEDVVR ALEKHVDLRE NDRLEFHRLS EENTLLKNDL
1110 1120 1130 1140 1150
GRVRQELEAA ESTHDAQRKE IEVLKKDKEK ACSEMEVLNR QNQNYKDQLS
1160 1170 1180 1190 1200
QLNVRVLQLG QEASTHQAQN EEHRVTIQML TQSLEEVVRS GQQQSDQIQK
1210 1220 1230 1240 1250
LRVELECLNQ EHQSLQLPWS ELTQTLEESQ DQVQGAHLRL RQAQAQHLQE
1260 1270 1280 1290 1300
VRLVPQDRVA ELHRLLSLQG EQARRRLDAQ REEHEKQLKA TEERVEEAEM
1310 1320 1330 1340 1350
ILKNMEMLLQ EKVDKLKEQF EKNTKSDLLL KELYVENAHL VRALQATEEK
1360 1370 1380
QRGAEKQSRL LEEKVRALNK LVSRIAPAAL SV
Length:1,382
Mass (Da):156,344
Last modified:October 31, 2006 - v2
Checksum:i7AB4D464D56A9F28
GO
Isoform 2 (identifier: Q9Y2I6-2) [UniParc]FASTAAdd to basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     735-1083: Missing.

Show »
Length:1,033
Mass (Da):118,447
Checksum:i21759D299ECD5265
GO

Sequence cautioni

The sequence BAA76824.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAH11644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAH11644.1 differs from that shown. Reason: Erroneous termination at position 405. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031V → L in BAH11644 (PubMed:14702039).Curated
Sequence conflicti958 – 9592Missing in AAH36380 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791G → V.
Corresponds to variant rs6115203 [ dbSNP | Ensembl ].
VAR_059700
Natural varianti191 – 1911S → R.
Corresponds to variant rs34585177 [ dbSNP | Ensembl ].
VAR_059701
Natural varianti276 – 2761R → W.
Corresponds to variant rs13044759 [ dbSNP | Ensembl ].
VAR_059702
Natural varianti296 – 2961T → A.
Corresponds to variant rs379538 [ dbSNP | Ensembl ].
VAR_059703
Natural varianti969 – 9691R → G.1 Publication
Corresponds to variant rs6115193 [ dbSNP | Ensembl ].
VAR_058509
Natural varianti973 – 9731E → K.
Corresponds to variant rs428801 [ dbSNP | Ensembl ].
VAR_059704
Natural varianti1077 – 10771D → N.
Corresponds to variant rs35666277 [ dbSNP | Ensembl ].
VAR_061688
Natural varianti1276 – 12761R → C.
Corresponds to variant rs41310175 [ dbSNP | Ensembl ].
VAR_061689
Natural varianti1366 – 13661R → H.1 Publication
Corresponds to variant rs17857107 [ dbSNP | Ensembl ].
VAR_058510

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei735 – 1083349Missing in isoform 2. 1 PublicationVSP_037883Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU718622 mRNA. Translation: ACE78295.1.
AB023197 mRNA. Translation: BAA76824.1. Different initiation.
AL031672 Genomic DNA. Translation: CAI43018.1.
AL161802 Genomic DNA. No translation available.
BC036380 mRNA. Translation: AAH36380.1.
AK293991 mRNA. Translation: BAH11644.1. Sequence problems.
CCDSiCCDS33452.1. [Q9Y2I6-1]
RefSeqiNP_001305155.1. NM_001318226.1. [Q9Y2I6-2]
NP_079452.3. NM_025176.5. [Q9Y2I6-1]
UniGeneiHs.631508.

Genome annotation databases

EnsembliENST00000278886; ENSP00000278886; ENSG00000101004. [Q9Y2I6-1]
ENST00000422516; ENSP00000410431; ENSG00000101004. [Q9Y2I6-2]
GeneIDi22981.
KEGGihsa:22981.
UCSCiuc002wux.3. human. [Q9Y2I6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU718622 mRNA. Translation: ACE78295.1.
AB023197 mRNA. Translation: BAA76824.1. Different initiation.
AL031672 Genomic DNA. Translation: CAI43018.1.
AL161802 Genomic DNA. No translation available.
BC036380 mRNA. Translation: AAH36380.1.
AK293991 mRNA. Translation: BAH11644.1. Sequence problems.
CCDSiCCDS33452.1. [Q9Y2I6-1]
RefSeqiNP_001305155.1. NM_001318226.1. [Q9Y2I6-2]
NP_079452.3. NM_025176.5. [Q9Y2I6-1]
UniGeneiHs.631508.

3D structure databases

ProteinModelPortaliQ9Y2I6.
SMRiQ9Y2I6. Positions 9-70, 198-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116630. 211 interactions.
IntActiQ9Y2I6. 198 interactions.
MINTiMINT-1408864.
STRINGi9606.ENSP00000278886.

PTM databases

iPTMnetiQ9Y2I6.
PhosphoSiteiQ9Y2I6.

Polymorphism and mutation databases

BioMutaiNINL.
DMDMi118601093.

Proteomic databases

EPDiQ9Y2I6.
MaxQBiQ9Y2I6.
PaxDbiQ9Y2I6.
PRIDEiQ9Y2I6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278886; ENSP00000278886; ENSG00000101004. [Q9Y2I6-1]
ENST00000422516; ENSP00000410431; ENSG00000101004. [Q9Y2I6-2]
GeneIDi22981.
KEGGihsa:22981.
UCSCiuc002wux.3. human. [Q9Y2I6-1]

Organism-specific databases

CTDi22981.
GeneCardsiNINL.
HGNCiHGNC:29163. NINL.
HPAiHPA000686.
MIMi609580. gene.
neXtProtiNX_Q9Y2I6.
PharmGKBiPA165392435.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEH8. Eukaryota.
ENOG41128SZ. LUCA.
GeneTreeiENSGT00660000095541.
InParanoidiQ9Y2I6.
KOiK16477.
OMAiGIQNGRE.
OrthoDBiEOG7MWGWC.
PhylomeDBiQ9Y2I6.
TreeFamiTF325139.

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
SIGNORiQ9Y2I6.

Miscellaneous databases

ChiTaRSiNINL. human.
GeneWikiiNINL.
GenomeRNAii22981.
NextBioi43807.
PROiQ9Y2I6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2I6.
ExpressionAtlasiQ9Y2I6. baseline and differential.
GenevisibleiQ9Y2I6. HS.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein."
    van Wijk E., Kersten F.F.J., Kartono A., Mans D.A., Brandwijk K., Letteboer S.J.F., Peters T.A., Maerker T., Yan X., Cremers C.W.R.J., Cremers F.P.M., Wolfrum U., Roepman R., Kremer H.
    Hum. Mol. Genet. 18:51-64(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH LCA5 AND USH2A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANTS GLY-969 AND HIS-1366.
    Tissue: Testis.
  5. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-454 (ISOFORMS 1/2).
    Tissue: Cerebellum.
  6. "Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation."
    Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R., Nigg E.A.
    Dev. Cell 5:113-125(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GAMMA-TUBULIN AND TUBGCP4, PHOSPHORYLATION.
  7. "Phosphorylation of Nlp by Plk1 negatively regulates its dynein-dynactin-dependent targeting to the centrosome."
    Casenghi M., Barr F.A., Nigg E.A.
    J. Cell Sci. 118:5101-5108(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  8. "Cell cycle-dependent expression of centrosomal ninein-like protein in human cells is regulated by the anaphase-promoting complex."
    Wang Y., Zhan Q.
    J. Biol. Chem. 282:17712-17719(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APC/C COMPLEX; CDC20 AND FZR1, TISSUE SPECIFICITY, DOMAIN, UBIQUITINATION, MUTAGENESIS OF 495-LYS--ASN-497 AND 633-ARG--LEU-636.
  9. "Increased expression of Nlp, a potential oncogene in ovarian cancer, and its implication in carcinogenesis."
    Qu D., Qu H., Fu M., Zhao X., Liu R., Sui L., Zhan Q.
    Gynecol. Oncol. 110:230-236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiNINL_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2I6
Secondary accession number(s): A6NJN0
, B3V9H6, B7Z1V8, Q5JYP0, Q8NE38, Q9NQE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 11, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.