ODFP2_HUMAN
ID ODFP2_HUMAN Reviewed; 829 AA.
AC Q5BJF6; B1AND3; B4DRK4; B4DX73; B4DZ02; E7EWL2; F5H6J4; O14721; O60631;
AC Q1W2J6; Q6UN26; Q7Z5I6; Q96FN2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Outer dense fiber protein 2;
DE AltName: Full=Cenexin;
DE AltName: Full=Outer dense fiber of sperm tails protein 2;
GN Name=ODF2;
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 5), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 18-829 (ISOFORM 6), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10381817; DOI=10.1093/molehr/5.7.627;
RA Petersen C., Fuezesi L., Hoyer-Fender S.;
RT "Outer dense fibre proteins from human sperm tail: molecular cloning and
RT expression analyses of two cDNA transcripts encoding proteins of
RT approximately 70 kDa.";
RL Mol. Hum. Reprod. 5:627-635(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, ALTERNATIVE SPLICING, AND INTERACTION WITH PLK1.
RX PubMed=16966375; DOI=10.1128/mcb.00671-06;
RA Soung N.-K., Kang Y.H., Kim K., Kamijo K., Yoon H., Seong Y.S., Kuo Y.-L.,
RA Miki T., Kim S.R., Kuriyama R., Giam C.-Z., Ahn C.H., Lee K.S.;
RT "Requirement of hCenexin for proper mitotic functions of polo-like kinase 1
RT at the centrosomes.";
RL Mol. Cell. Biol. 26:8316-8335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 6).
RC TISSUE=Testis;
RA Xu Z.Y., Huang X.Y., Yin L.L., Xu M., Lu L., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning and characterization of the outer dense fiber protein in
RT spermatogenesis.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 10).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP INTERACTION WITH MARK4, AND SUBCELLULAR LOCATION.
RX PubMed=23400999; DOI=10.1083/jcb.201206013;
RA Kuhns S., Schmidt K.N., Reymann J., Gilbert D.F., Neuner A., Hub B.,
RA Carvalho R., Wiedemann P., Zentgraf H., Erfle H., Klingmuller U.,
RA Boutros M., Pereira G.;
RT "The microtubule affinity regulating kinase MARK4 promotes axoneme
RT extension during early ciliogenesis.";
RL J. Cell Biol. 200:505-522(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP INTERACTION WITH QRICH2.
RX PubMed=30683861; DOI=10.1038/s41467-018-08182-x;
RA Shen Y., Zhang F., Li F., Jiang X., Yang Y., Li X., Li W., Wang X.,
RA Cheng J., Liu M., Zhang X., Yuan G., Pei X., Cai K., Hu F., Sun J., Yan L.,
RA Tang L., Jiang C., Tu W., Xu J., Wu H., Kong W., Li S., Wang K., Sheng K.,
RA Zhao X., Yue H., Yang X., Xu W.;
RT "Loss-of-function mutations in QRICH2 cause male infertility with multiple
RT morphological abnormalities of the sperm flagella.";
RL Nat. Commun. 10:433-433(2019).
CC -!- FUNCTION: Seems to be a major component of sperm tail outer dense
CC fibers (ODF). ODFs are filamentous structures located on the outside of
CC the axoneme in the midpiece and principal piece of the mammalian sperm
CC tail and may help to maintain the passive elastic structures and
CC elastic recoil of the sperm tail. May have a modulating influence on
CC sperm motility. Functions as a general scaffold protein that is
CC specifically localized at the distal/subdistal appendages of mother
CC centrioles. Component of the centrosome matrix required for the
CC localization of PLK1 and NIN to the centrosomes. Required for the
CC formation and/or maintenance of normal CETN1 assembly.
CC {ECO:0000269|PubMed:16966375}.
CC -!- SUBUNIT: Self-associates. Associates with microtubules and forms a
CC fibrillar structure partially linked to the microtubule network.
CC Interacts via its C-terminus with PLK1 (PubMed:16966375). Interacts
CC with ODF1 (By similarity). Interacts with MARK4; the interaction is
CC required for localization of ODF2 to centrioles (PubMed:23400999).
CC Interacts with TSSK4 (By similarity). Interacts with AKNA (By
CC similarity). Interacts with QRICH2 (PubMed:30683861). Interacts with
CC CFAP58 (By similarity). {ECO:0000250|UniProtKB:A3KGV1,
CC ECO:0000269|PubMed:16966375, ECO:0000269|PubMed:23400999,
CC ECO:0000269|PubMed:30683861}.
CC -!- INTERACTION:
CC Q5BJF6; Q96HB5: CCDC120; NbExp=5; IntAct=EBI-8744243, EBI-744556;
CC Q5BJF6-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-9090919, EBI-25837549;
CC Q5BJF6-2; P22607: FGFR3; NbExp=3; IntAct=EBI-9090919, EBI-348399;
CC Q5BJF6-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9090919, EBI-8285963;
CC Q5BJF6-2; P04792: HSPB1; NbExp=3; IntAct=EBI-9090919, EBI-352682;
CC Q5BJF6-2; Q8WYH8: ING5; NbExp=3; IntAct=EBI-9090919, EBI-488533;
CC Q5BJF6-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9090919, EBI-10975473;
CC Q5BJF6-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-9090919, EBI-16439278;
CC Q5BJF6-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-9090919, EBI-396669;
CC Q5BJF6-2; Q13573: SNW1; NbExp=3; IntAct=EBI-9090919, EBI-632715;
CC Q5BJF6-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9090919, EBI-5235340;
CC Q5BJF6-2; O00463: TRAF5; NbExp=3; IntAct=EBI-9090919, EBI-523498;
CC Q5BJF6-2; O76024: WFS1; NbExp=3; IntAct=EBI-9090919, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:16966375}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:A3KGV1}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23400999}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:A3KGV1}.
CC Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A3KGV1}.
CC Note=Localized at the microtubule organizing centers in interphase and
CC spindle poles in mitosis. Localized at the distal/subdistal appendages
CC of mother centrioles. {ECO:0000250|UniProtKB:A3KGV1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1;
CC IsoId=Q5BJF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BJF6-2; Sequence=VSP_027665, VSP_027667;
CC Name=3; Synonyms=Cenexin 1;
CC IsoId=Q5BJF6-3; Sequence=VSP_027666, VSP_027667;
CC Name=4; Synonyms=Cenexin 1 variant 1;
CC IsoId=Q5BJF6-4; Sequence=VSP_027666;
CC Name=5; Synonyms=Cenexin 1, ODF2/1;
CC IsoId=Q5BJF6-5; Sequence=VSP_027667, VSP_027668, VSP_027669;
CC Name=6; Synonyms=Isoform 3, ODF2/2;
CC IsoId=Q5BJF6-6; Sequence=VSP_027668, VSP_027669;
CC Name=7;
CC IsoId=Q5BJF6-7; Sequence=VSP_042071, VSP_027668, VSP_027669;
CC Name=8;
CC IsoId=Q5BJF6-8; Sequence=VSP_042070, VSP_027667, VSP_027668,
CC VSP_027669;
CC Name=9;
CC IsoId=Q5BJF6-9; Sequence=VSP_027666, VSP_042072, VSP_027668,
CC VSP_027669;
CC Name=10;
CC IsoId=Q5BJF6-10; Sequence=VSP_044946, VSP_027668, VSP_027669;
CC -!- TISSUE SPECIFICITY: Testis-specific (at protein level). Highly
CC expressed in cytoplasm of step 2 round spermatids. Detected in the
CC middle piece and extends to about half the principal piece of the sperm
CC tails. {ECO:0000269|PubMed:10381817}.
CC -!- PTM: Tyrosine phosphorylated. Phosphorylated by TSSK4 on Ser-95.
CC {ECO:0000250|UniProtKB:A3KGV1, ECO:0000250|UniProtKB:Q2MJU7}.
CC -!- MISCELLANEOUS: [Isoform 5]: Major. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ODF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08409.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF012549; AAB66337.1; -; mRNA.
DR EMBL; AF053970; AAC08409.1; ALT_INIT; mRNA.
DR EMBL; DQ444713; ABE01856.1; -; mRNA.
DR EMBL; DQ444714; ABE01857.1; -; mRNA.
DR EMBL; AY319414; AAP83847.1; -; mRNA.
DR EMBL; AY366499; AAQ73195.1; -; mRNA.
DR EMBL; AK299303; BAG61316.1; -; mRNA.
DR EMBL; AK301842; BAG63285.1; -; mRNA.
DR EMBL; AK302684; BAG63914.1; -; mRNA.
DR EMBL; AL359091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87791.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87793.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87795.1; -; Genomic_DNA.
DR EMBL; BC091500; AAH91500.1; -; mRNA.
DR EMBL; BC010629; AAH10629.1; -; mRNA.
DR CCDS; CCDS56585.1; -. [Q5BJF6-10]
DR CCDS; CCDS56586.1; -. [Q5BJF6-7]
DR CCDS; CCDS56587.1; -. [Q5BJF6-8]
DR CCDS; CCDS56588.1; -. [Q5BJF6-1]
DR CCDS; CCDS56589.1; -. [Q5BJF6-9]
DR CCDS; CCDS56590.1; -. [Q5BJF6-4]
DR CCDS; CCDS6902.1; -. [Q5BJF6-5]
DR PIR; T03791; T03791.
DR RefSeq; NP_001229281.1; NM_001242352.1. [Q5BJF6-4]
DR RefSeq; NP_001229282.1; NM_001242353.1. [Q5BJF6-1]
DR RefSeq; NP_001229283.1; NM_001242354.1. [Q5BJF6-9]
DR RefSeq; NP_002531.3; NM_002540.4. [Q5BJF6-3]
DR RefSeq; NP_702910.1; NM_153432.1. [Q5BJF6-7]
DR RefSeq; NP_702911.1; NM_153433.1. [Q5BJF6-1]
DR RefSeq; NP_702913.1; NM_153435.1.
DR RefSeq; NP_702914.1; NM_153436.1. [Q5BJF6-10]
DR RefSeq; NP_702915.1; NM_153437.2. [Q5BJF6-5]
DR RefSeq; XP_006717189.1; XM_006717126.3.
DR RefSeq; XP_016870261.1; XM_017014772.1.
DR RefSeq; XP_016870262.1; XM_017014773.1.
DR RefSeq; XP_016870263.1; XM_017014774.1.
DR RefSeq; XP_016870264.1; XM_017014775.1.
DR RefSeq; XP_016870265.1; XM_017014776.1.
DR RefSeq; XP_016870266.1; XM_017014777.1.
DR AlphaFoldDB; Q5BJF6; -.
DR SMR; Q5BJF6; -.
DR BioGRID; 111010; 149.
DR IntAct; Q5BJF6; 141.
DR MINT; Q5BJF6; -.
DR STRING; 9606.ENSP00000403453; -.
DR MoonProt; Q5BJF6; -.
DR iPTMnet; Q5BJF6; -.
DR PhosphoSitePlus; Q5BJF6; -.
DR BioMuta; ODF2; -.
DR DMDM; 74736013; -.
DR EPD; Q5BJF6; -.
DR jPOST; Q5BJF6; -.
DR MassIVE; Q5BJF6; -.
DR MaxQB; Q5BJF6; -.
DR PaxDb; Q5BJF6; -.
DR PeptideAtlas; Q5BJF6; -.
DR PRIDE; Q5BJF6; -.
DR ProteomicsDB; 5417; -.
DR ProteomicsDB; 62680; -. [Q5BJF6-1]
DR ProteomicsDB; 62681; -. [Q5BJF6-2]
DR ProteomicsDB; 62682; -. [Q5BJF6-3]
DR ProteomicsDB; 62683; -. [Q5BJF6-4]
DR ProteomicsDB; 62684; -. [Q5BJF6-5]
DR ProteomicsDB; 62685; -. [Q5BJF6-6]
DR ProteomicsDB; 62686; -. [Q5BJF6-7]
DR ProteomicsDB; 62687; -. [Q5BJF6-8]
DR ProteomicsDB; 62688; -. [Q5BJF6-9]
DR Antibodypedia; 976; 256 antibodies from 34 providers.
DR DNASU; 4957; -.
DR Ensembl; ENST00000372791.7; ENSP00000361877.3; ENSG00000136811.17. [Q5BJF6-5]
DR Ensembl; ENST00000372807.10; ENSP00000361893.5; ENSG00000136811.17. [Q5BJF6-4]
DR Ensembl; ENST00000372814.7; ENSP00000361901.3; ENSG00000136811.17. [Q5BJF6-7]
DR Ensembl; ENST00000393533.6; ENSP00000377166.2; ENSG00000136811.17. [Q5BJF6-10]
DR Ensembl; ENST00000434106.7; ENSP00000403453.2; ENSG00000136811.17. [Q5BJF6-1]
DR Ensembl; ENST00000448249.8; ENSP00000396687.2; ENSG00000136811.17. [Q5BJF6-9]
DR Ensembl; ENST00000546203.5; ENSP00000437579.1; ENSG00000136811.17. [Q5BJF6-8]
DR Ensembl; ENST00000604420.5; ENSP00000473949.2; ENSG00000136811.17. [Q5BJF6-1]
DR GeneID; 4957; -.
DR KEGG; hsa:4957; -.
DR UCSC; uc004bva.4; human. [Q5BJF6-1]
DR CTD; 4957; -.
DR DisGeNET; 4957; -.
DR GeneCards; ODF2; -.
DR HGNC; HGNC:8114; ODF2.
DR HPA; ENSG00000136811; Tissue enriched (testis).
DR MIM; 602015; gene.
DR neXtProt; NX_Q5BJF6; -.
DR OpenTargets; ENSG00000136811; -.
DR PharmGKB; PA31902; -.
DR VEuPathDB; HostDB:ENSG00000136811; -.
DR eggNOG; ENOG502QUXQ; Eukaryota.
DR GeneTree; ENSGT00530000063497; -.
DR HOGENOM; CLU_018326_0_0_1; -.
DR InParanoid; Q5BJF6; -.
DR OMA; MEWRYQS; -.
DR OrthoDB; 328077at2759; -.
DR PhylomeDB; Q5BJF6; -.
DR TreeFam; TF328605; -.
DR PathwayCommons; Q5BJF6; -.
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; Q5BJF6; -.
DR BioGRID-ORCS; 4957; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; ODF2; human.
DR GeneWiki; ODF2; -.
DR GenomeRNAi; 4957; -.
DR Pharos; Q5BJF6; Tbio.
DR PRO; PR:Q5BJF6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5BJF6; protein.
DR Bgee; ENSG00000136811; Expressed in sperm and 154 other tissues.
DR ExpressionAtlas; Q5BJF6; baseline and differential.
DR Genevisible; Q5BJF6; HS.
DR GO; GO:0120103; C:centriolar subdistal appendage; IDA:GO_Central.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097539; C:ciliary transition fiber; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0001520; C:outer dense fiber; IEA:Ensembl.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0010457; P:centriole-centriole cohesion; IGI:GO_Central.
DR GO; GO:0044782; P:cilium organization; IGI:ARUK-UCL.
DR GO; GO:0008104; P:protein localization; IMP:GO_Central.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR InterPro; IPR026099; Odf2-rel.
DR PANTHER; PTHR23162; PTHR23162; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Flagellum;
KW Isopeptide bond; Microtubule; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Ubl conjugation.
FT CHAIN 1..829
FT /note="Outer dense fiber protein 2"
FT /id="PRO_0000299455"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..217
FT /evidence="ECO:0000255"
FT COILED 245..423
FT /evidence="ECO:0000255"
FT COILED 461..798
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 95
FT /note="Phosphoserine; by TSSK4"
FT /evidence="ECO:0000250|UniProtKB:A3KGV1"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYX5"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027665"
FT VAR_SEQ 1..41
FT /note="MSASSSGGSPRFPSCGKNGVTSLTQKKVLRAPCGAPSVTVT -> MKDRSST
FT PPLHVHVDENTPVHVHIKKLPKPSATSSQ (in isoform 3, isoform 4 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16966375, ECO:0000303|Ref.3"
FT /id="VSP_027666"
FT VAR_SEQ 1..11
FT /note="MSASSSGGSPR -> MGELPTGCRKRRRKRGGAAARARLHPPRRLHGTTLAS
FT DFNDFIRRRFWAQPCRSW (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_042071"
FT VAR_SEQ 1..11
FT /note="MSASSSGGSPR -> MGRNRYPPACW (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_042070"
FT VAR_SEQ 1..10
FT /note="MSASSSGGSP -> MADQQGPHQN (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044946"
FT VAR_SEQ 65..140
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_042072"
FT VAR_SEQ 65..83
FT /note="Missing (in isoform 2, isoform 3, isoform 5 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:10381817,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16966375,
FT ECO:0000303|Ref.3"
FT /id="VSP_027667"
FT VAR_SEQ 638..657
FT /note="IEHQGDKLEMAREKHQASQK -> VRDWQKGSHELTRAGARIPR (in
FT isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:10381817,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_027668"
FT VAR_SEQ 658..829
FT /note="Missing (in isoform 5, isoform 6, isoform 7, isoform
FT 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:10381817,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_027669"
FT VARIANT 710
FT /note="T -> S (in dbSNP:rs16930426)"
FT /id="VAR_034821"
FT CONFLICT 39
FT /note="T -> A (in Ref. 3; AAP83847)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="I -> R (in Ref. 3; AAP83847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 829 AA; 95401 MW; CF49166AD9003BEB CRC64;
MSASSSGGSP RFPSCGKNGV TSLTQKKVLR APCGAPSVTV TKSHKRGMKG DTVNVRRSVR
VKTKVPWMPP GKSSARPVGC KWENPPHCLE ITPPSSEKLV SVMRLSDLST EDDDSGHCKM
NRYDKKIDSL MNAVGCLKSE VKMQKGERQM AKRFLEERKE ELEEVAHELA ETEHENTVLR
HNIERMKEEK DFTILQKKHL QQEKECLMSK LVEAEMDGAA AAKQVMALKD TIGKLKTEKQ
MTCTDINTLT RQKELLLQKL STFEETNRTL RDLLREQHCK EDSERLMEQQ GALLKRLAEA
DSEKARLLLL LQDKDKEVEE LLQEIQCEKA QAKTASELSK SMESMRGHLQ AQLRSKEAEN
SRLCMQIKNL ERSGNQHKAE VEAIMEQLKE LKQKGDRDKE SLKKAIRAQK ERAEKSEEYA
EQLHVQLADK DLYVAEALST LESWRSRYNQ VVKEKGDLEL EIIVLNDRVT DLVNQQQTLE
EKMREDRDSL VERLHRQTAE YSAFKLENER LKASFAPMED KLNQAHLEVQ QLKASVKNYE
GMIDNYKSQV MKTRLEADEV AAQLERCDKE NKILKDEMNK EIEAARRQFQ SQLADLQQLP
DILKITEAKL AECQDQLQGY ERKNIDLTAI ISDLRSRIEH QGDKLEMARE KHQASQKENK
QLSLKVDELE RKLEATSAQN IEFLQVIAKR EEAIHQSQLR LEEKTRECGT LARQLESAIE
DARRQVEQTK EHALSKERAA QNKILDLETQ LSRTKTELSQ LRRSRDDADR RYQSRLQDLK
DRLEQSESTN RSMQNYVQFL KSSYANVFGD GPYSTFLTSS PIRSRSPPA
