NINL_HUMAN
ID NINL_HUMAN Reviewed; 1382 AA.
AC Q9Y2I6; A6NJN0; B3V9H6; B7Z1V8; Q5JYP0; Q8NE38; Q9NQE3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ninein-like protein;
GN Name=NINL; Synonyms=KIAA0980, NLP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH LCA5 AND USH2A,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18826961; DOI=10.1093/hmg/ddn312;
RA van Wijk E., Kersten F.F.J., Kartono A., Mans D.A., Brandwijk K.,
RA Letteboer S.J.F., Peters T.A., Maerker T., Yan X., Cremers C.W.R.J.,
RA Cremers F.P.M., Wolfrum U., Roepman R., Kremer H.;
RT "Usher syndrome and Leber congenital amaurosis are molecularly linked via a
RT novel isoform of the centrosomal ninein-like protein.";
RL Hum. Mol. Genet. 18:51-64(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-969
RP AND HIS-1366.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-454 (ISOFORMS 1/2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP FUNCTION, INTERACTION WITH GAMMA-TUBULIN AND TUBGCP4, AND PHOSPHORYLATION.
RX PubMed=12852856; DOI=10.1016/s1534-5807(03)00193-x;
RA Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R., Nigg E.A.;
RT "Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
RT microtubule nucleation.";
RL Dev. Cell 5:113-125(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=16254247; DOI=10.1242/jcs.02622;
RA Casenghi M., Barr F.A., Nigg E.A.;
RT "Phosphorylation of Nlp by Plk1 negatively regulates its dynein-dynactin-
RT dependent targeting to the centrosome.";
RL J. Cell Sci. 118:5101-5108(2005).
RN [8]
RP INTERACTION WITH APC/C COMPLEX; CDC20 AND FZR1, TISSUE SPECIFICITY, DOMAIN,
RP UBIQUITINATION, AND MUTAGENESIS OF 495-LYS--ASN-497 AND 633-ARG--LEU-636.
RX PubMed=17403670; DOI=10.1074/jbc.m701350200;
RA Wang Y., Zhan Q.;
RT "Cell cycle-dependent expression of centrosomal ninein-like protein in
RT human cells is regulated by the anaphase-promoting complex.";
RL J. Biol. Chem. 282:17712-17719(2007).
RN [9]
RP FUNCTION.
RX PubMed=18538832; DOI=10.1016/j.ygyno.2008.04.015;
RA Qu D., Qu H., Fu M., Zhao X., Liu R., Sui L., Zhan Q.;
RT "Increased expression of Nlp, a potential oncogene in ovarian cancer, and
RT its implication in carcinogenesis.";
RL Gynecol. Oncol. 110:230-236(2008).
CC -!- FUNCTION: Involved in the microtubule organization in interphase cells.
CC Overexpression induces the fragmentation of the Golgi, and causes
CC lysosomes to disperse toward the cell periphery; it also interferes
CC with mitotic spindle assembly. May play a role in ovarian
CC carcinogenesis. {ECO:0000269|PubMed:12852856,
CC ECO:0000269|PubMed:16254247, ECO:0000269|PubMed:18538832}.
CC -!- SUBUNIT: Interacts with gamma-tubulin and TUBGCP4. Interacts with
CC anaphase promoting complex/cyclosome (APC/C). Interacts with CDC20 and
CC FZR1. Isoform 2 interacts with LCA5 and USH2A.
CC {ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:17403670,
CC ECO:0000269|PubMed:18826961}.
CC -!- INTERACTION:
CC Q9Y2I6; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-719716, EBI-10247802;
CC Q9Y2I6; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-719716, EBI-10175300;
CC Q9Y2I6; Q3B820: FAM161A; NbExp=3; IntAct=EBI-719716, EBI-719941;
CC Q9Y2I6; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-719716, EBI-2514791;
CC Q9Y2I6; Q92993: KAT5; NbExp=3; IntAct=EBI-719716, EBI-399080;
CC Q9Y2I6; Q8NA19: L3MBTL4; NbExp=3; IntAct=EBI-719716, EBI-8833581;
CC Q9Y2I6; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-719716, EBI-740773;
CC Q9Y2I6; Q9P2K3: RCOR3; NbExp=4; IntAct=EBI-719716, EBI-743428;
CC Q9Y2I6; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-719716, EBI-747035;
CC Q9Y2I6; Q8TAU3: ZNF417; NbExp=4; IntAct=EBI-719716, EBI-740727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:16254247}. Cytoplasm
CC {ECO:0000269|PubMed:16254247}. Note=In interphase cells, NINL is
CC transported to the centrosomes by the dynein-dynactin motor complex
CC (PubMed:16254247). During centrosome maturation, PLK1 directly
CC phosphorylates NINL resulting in its release into the cytoplasm
CC (PubMed:16254247).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q9Y2I6-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9Y2I6-2; Sequence=VSP_037883;
CC -!- TISSUE SPECIFICITY: Expressed in KYSE-150 esophageal carcinoma, HeLa
CC cervical carcinoma and U2OS osteosarcoma cells. Expression is regulated
CC in a cell cycle-dependent manner and peaks during G2/M phase (at
CC protein level). Expressed in fetal heart, skeletal muscle, liver, lung
CC and cochlea, and in adult brain, testis, kidney and retina.
CC {ECO:0000269|PubMed:17403670, ECO:0000269|PubMed:18826961}.
CC -!- DOMAIN: The KEN and D (destructive) boxes are required for the cell
CC cycle-controlled NINL degradation by the APC/C pathway.
CC {ECO:0000269|PubMed:17403670}.
CC -!- PTM: Phosphorylated by PLK1 which disrupts its centrosome association
CC and interaction with gamma-tubulin. {ECO:0000269|PubMed:12852856,
CC ECO:0000269|PubMed:16254247}.
CC -!- PTM: Ubiquitinated by the APC/C complex leading to its degradation.
CC {ECO:0000269|PubMed:17403670}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAH11644.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH11644.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU718622; ACE78295.1; -; mRNA.
DR EMBL; AB023197; BAA76824.1; ALT_INIT; mRNA.
DR EMBL; AL031672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036380; AAH36380.1; -; mRNA.
DR EMBL; AK293991; BAH11644.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33452.1; -. [Q9Y2I6-1]
DR CCDS; CCDS82605.1; -. [Q9Y2I6-2]
DR RefSeq; NP_001305155.1; NM_001318226.1. [Q9Y2I6-2]
DR RefSeq; NP_079452.3; NM_025176.5. [Q9Y2I6-1]
DR AlphaFoldDB; Q9Y2I6; -.
DR SMR; Q9Y2I6; -.
DR BioGRID; 116630; 459.
DR ELM; Q9Y2I6; -.
DR IntAct; Q9Y2I6; 216.
DR MINT; Q9Y2I6; -.
DR STRING; 9606.ENSP00000278886; -.
DR GlyGen; Q9Y2I6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2I6; -.
DR PhosphoSitePlus; Q9Y2I6; -.
DR BioMuta; NINL; -.
DR DMDM; 118601093; -.
DR EPD; Q9Y2I6; -.
DR jPOST; Q9Y2I6; -.
DR MassIVE; Q9Y2I6; -.
DR MaxQB; Q9Y2I6; -.
DR PaxDb; Q9Y2I6; -.
DR PeptideAtlas; Q9Y2I6; -.
DR PRIDE; Q9Y2I6; -.
DR ProteomicsDB; 85799; -. [Q9Y2I6-1]
DR ProteomicsDB; 85800; -. [Q9Y2I6-2]
DR Antibodypedia; 628; 61 antibodies from 16 providers.
DR DNASU; 22981; -.
DR Ensembl; ENST00000278886.11; ENSP00000278886.6; ENSG00000101004.15. [Q9Y2I6-1]
DR Ensembl; ENST00000422516.5; ENSP00000410431.1; ENSG00000101004.15. [Q9Y2I6-2]
DR GeneID; 22981; -.
DR KEGG; hsa:22981; -.
DR MANE-Select; ENST00000278886.11; ENSP00000278886.6; NM_025176.6; NP_079452.3.
DR UCSC; uc002wux.3; human. [Q9Y2I6-1]
DR CTD; 22981; -.
DR DisGeNET; 22981; -.
DR GeneCards; NINL; -.
DR HGNC; HGNC:29163; NINL.
DR HPA; ENSG00000101004; Low tissue specificity.
DR MIM; 609580; gene.
DR neXtProt; NX_Q9Y2I6; -.
DR OpenTargets; ENSG00000101004; -.
DR PharmGKB; PA165392435; -.
DR VEuPathDB; HostDB:ENSG00000101004; -.
DR eggNOG; ENOG502R2VA; Eukaryota.
DR GeneTree; ENSGT00660000095541; -.
DR HOGENOM; CLU_001462_0_0_1; -.
DR InParanoid; Q9Y2I6; -.
DR OMA; TEIMVEQ; -.
DR OrthoDB; 95801at2759; -.
DR PhylomeDB; Q9Y2I6; -.
DR TreeFam; TF325139; -.
DR PathwayCommons; Q9Y2I6; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9Y2I6; -.
DR SIGNOR; Q9Y2I6; -.
DR BioGRID-ORCS; 22981; 13 hits in 1080 CRISPR screens.
DR ChiTaRS; NINL; human.
DR GeneWiki; NINL; -.
DR GenomeRNAi; 22981; -.
DR Pharos; Q9Y2I6; Tbio.
DR PRO; PR:Q9Y2I6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y2I6; protein.
DR Bgee; ENSG00000101004; Expressed in renal medulla and 164 other tissues.
DR ExpressionAtlas; Q9Y2I6; baseline and differential.
DR Genevisible; Q9Y2I6; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1382
FT /note="Ninein-like protein"
FT /id="PRO_0000259714"
FT DOMAIN 7..42
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 41..76
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 196..231
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 233..268
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 384..424
FT /evidence="ECO:0000255"
FT COILED 484..579
FT /evidence="ECO:0000255"
FT COILED 616..699
FT /evidence="ECO:0000255"
FT COILED 1046..1375
FT /evidence="ECO:0000255"
FT MOTIF 495..497
FT /note="KEN box"
FT MOTIF 633..641
FT /note="D-box"
FT COMPBIAS 149..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ12"
FT VAR_SEQ 735..1083
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18826961"
FT /id="VSP_037883"
FT VARIANT 79
FT /note="G -> V (in dbSNP:rs6115203)"
FT /id="VAR_059700"
FT VARIANT 191
FT /note="S -> R (in dbSNP:rs34585177)"
FT /id="VAR_059701"
FT VARIANT 276
FT /note="R -> W (in dbSNP:rs13044759)"
FT /id="VAR_059702"
FT VARIANT 296
FT /note="T -> A (in dbSNP:rs379538)"
FT /id="VAR_059703"
FT VARIANT 969
FT /note="R -> G (in dbSNP:rs6115193)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058509"
FT VARIANT 973
FT /note="E -> K (in dbSNP:rs428801)"
FT /id="VAR_059704"
FT VARIANT 1077
FT /note="D -> N (in dbSNP:rs35666277)"
FT /id="VAR_061688"
FT VARIANT 1276
FT /note="R -> C (in dbSNP:rs41310175)"
FT /id="VAR_061689"
FT VARIANT 1366
FT /note="R -> H (in dbSNP:rs17857107)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058510"
FT MUTAGEN 495..497
FT /note="KEN->AAA: Disrupts binding to CDC20 and FZR1 and
FT prevents ubiquitination and subsequent degradation of NINL;
FT when associated with 633-A--A-636."
FT /evidence="ECO:0000269|PubMed:17403670"
FT MUTAGEN 633..636
FT /note="RTQL->AAAA: Disrupts binding to CDC20 and FZR1 and
FT prevents ubiquitination and subsequent degradation of NINL;
FT when associated with 495-A--A-497."
FT /evidence="ECO:0000269|PubMed:17403670"
FT CONFLICT 303
FT /note="V -> L (in Ref. 5; BAH11644)"
FT /evidence="ECO:0000305"
FT CONFLICT 958..959
FT /note="Missing (in Ref. 4; AAH36380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1382 AA; 156344 MW; 7AB4D464D56A9F28 CRC64;
MDEEENHYVS QLREVYSSCD TTGTGFLDRQ ELTQLCLKLH LEQQLPVLLQ TLLGNDHFAR
VNFEEFKEGF VAVLSSNAGV RPSDEDSSSL ESAASSAIPP KYVNGSKWYG RRSRPELCDA
ATEARRVPEQ QTQASLKSHL WRSASLESVE SPKSDEEAES TKEAQNELFE AQGQLQTWDS
EDFGSPQKSC SPSFDTPESQ IRGVWEELGV GSSGHLSEQE LAVVCQSVGL QGLEKEELED
LFNKLDQDGD GKVSLEEFQL GLFSHEPALL LESSTRVKPS KAWSHYQVPE ESGCHTTTTS
SLVSLCSSLR LFSSIDDGSG FAFPDQVLAM WTQEGIQNGR EILQSLDFSV DEKVNLLELT
WALDNELMTV DSAVQQAALA CYHQELSYQQ GQVEQLARER DKARQDLERA EKRNLEFVKE
MDDCHSTLEQ LTEKKIKHLE QGYRERLSLL RSEVEAEREL FWEQAHRQRA ALEWDVGRLQ
AEEAGLREKL TLALKENSRL QKEIVEVVEK LSDSERLALK LQKDLEFVLK DKLEPQSAEL
LAQEERFAAV LKEYELKCRD LQDRNDELQA ELEGLWARLP KNRHSPSWSP DGRRRQLPGL
GPAGISFLGN SAPVSIETEL MMEQVKEHYQ DLRTQLETKV NYYEREIAAL KRNFEKERKD
MEQARRREVS VLEGQKADLE ELHEKSQEVI WGLQEQLQDT ARGPEPEQMG LAPCCTQALC
GLALRHHSHL QQIRREAEAE LSGELSGLGA LPARRDLTLE LEEPPQGPLP RGSQRSEQLE
LERALKLQPC ASEKRAQMCV SLALEEEELE LARGKRVDGP SLEAEMQALP KDGLVAGSGQ
EGTRGLLPLR PGCGERPLAW LAPGDGRESE EAAGAGPRRR QAQDTEATQS PAPAPAPASH
GPSERWSRMQ PCGVDGDIVP KEPEPFGASA AGLEQPGARE LPLLGTERDA SQTQPRMWEP
PLRPAASCRG QAERLQAIQE ERARSWSRGT QEQASEQQAR AEGALEPGCH KHSVEVARRG
SLPSHLQLAD PQGSWQEQLA APEEGETKIA LEREKDDMET KLLHLEDVVR ALEKHVDLRE
NDRLEFHRLS EENTLLKNDL GRVRQELEAA ESTHDAQRKE IEVLKKDKEK ACSEMEVLNR
QNQNYKDQLS QLNVRVLQLG QEASTHQAQN EEHRVTIQML TQSLEEVVRS GQQQSDQIQK
LRVELECLNQ EHQSLQLPWS ELTQTLEESQ DQVQGAHLRL RQAQAQHLQE VRLVPQDRVA
ELHRLLSLQG EQARRRLDAQ REEHEKQLKA TEERVEEAEM ILKNMEMLLQ EKVDKLKEQF
EKNTKSDLLL KELYVENAHL VRALQATEEK QRGAEKQSRL LEEKVRALNK LVSRIAPAAL
SV
