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 24-JAN-2024, entry version 152. 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). Interacts with BBOF1 (By similarity). CC {ECO:0000250|UniProtKB:A3KGV1, ECO:0000269|PubMed:16966375, CC ECO:0000269|PubMed:23400999, ECO:0000269|PubMed:30683861}. CC -!- INTERACTION: CC Q5BJF6; Q96HB5: CCDC120; NbExp=5; IntAct=EBI-8744243, EBI-744556; CC Q5BJF6; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-8744243, EBI-1210753; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 152. DR IntAct; Q5BJF6; 303. DR MINT; Q5BJF6; -. DR STRING; 9606.ENSP00000403453; -. DR MoonProt; Q5BJF6; -. DR GlyGen; Q5BJF6; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000403453; -. DR PeptideAtlas; 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 Pumba; Q5BJF6; -. DR Antibodypedia; 976; 286 antibodies from 34 providers. DR DNASU; 4957; -. DR Ensembl; ENST00000372791.8; 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 AGR; HGNC:8114; -. 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; HVHINDT; -. DR OrthoDB; 2904900at2759; -. 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 SIGNOR; Q5BJF6; -. DR BioGRID-ORCS; 4957; 11 hits in 1157 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 156 other cell types or tissues. DR ExpressionAtlas; Q5BJF6; baseline and differential. 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:HPA. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. 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: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:0030154; P:cell differentiation; IEA:UniProtKB-KW. 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:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR InterPro; IPR026099; Odf2-rel. DR PANTHER; PTHR23162; OUTER DENSE FIBER OF SPERM TAILS 2; 1. DR PANTHER; PTHR23162:SF8; OUTER DENSE FIBER PROTEIN 2; 1. DR Genevisible; Q5BJF6; HS. 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 REGION 537..701 FT /note="Interaction with BBOF1" FT /evidence="ECO:0000250|UniProtKB:A3KGV1" 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 //