ID MA7D3_HUMAN Reviewed; 876 AA. AC Q8IWC1; A2A2J0; A6NCZ7; A6NHR4; B4DWD2; H7BY77; Q5JXI5; Q5JXI6; Q6P2S1; AC Q9H9M8; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 27-MAR-2024, entry version 154. DE RecName: Full=MAP7 domain-containing protein 3; GN Name=MAP7D3; Synonyms=MDP3 {ECO:0000303|PubMed:22142902}; 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 [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 701-876 (ISOFORMS 1/2/3). RC TISSUE=Synovium, and Teratocarcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cervix; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP ALA-502 AND ARG-628. RC TISSUE=Brain, and Prostate; 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 [6] RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15561729; DOI=10.1074/mcp.m400158-mcp200; RA Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W.; RT "Proteome analysis of the human mitotic spindle."; RL Mol. Cell. Proteomics 4:35-43(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-457; SER-461 AND RP SER-524, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION, INTERACTION WITH MICROTUBULES AND TUBULIN, INDUCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=22142902; DOI=10.4161/cc.10.22.18106; RA Sun X., Shi X., Liu M., Li D., Zhang L., Liu X., Zhou J.; RT "Mdp3 is a novel microtubule-binding protein that regulates microtubule RT assembly and stability."; RL Cell Cycle 10:3929-3937(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-441; SER-461; RP SER-490; SER-817 AND SER-832, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [16] RP INTERACTION WITH MICROTUBULES AND TUBULIN, AND FUNCTION. RX PubMed=24927501; DOI=10.1371/journal.pone.0099539; RA Yadav S., Verma P.J., Panda D.; RT "C-terminal region of MAP7 domain containing protein 3 (MAP7D3) promotes RT microtubule polymerization by binding at the C-terminal tail of tubulin."; RL PLoS ONE 9:E99539-E99539(2014). RN [17] RP VARIANT ARG-561. RX PubMed=26506222; DOI=10.1002/ana.24550; RA Park H.J., Hong Y.B., Choi Y.C., Lee J., Kim E.J., Lee J.S., Mo W.M., RA Ki S.M., Kim H.I., Kim H.J., Hyun Y.S., Hong H.D., Nam K., Jung S.C., RA Kim S.B., Kim S.H., Kim D.H., Oh K.W., Kim S.H., Yoo J.H., Lee J.E., RA Chung K.W., Choi B.O.; RT "ADSSL1 mutation relevant to autosomal recessive adolescent onset distal RT myopathy."; RL Ann. Neurol. 79:231-243(2016). CC -!- FUNCTION: Promotes the assembly and stability of microtubules. CC {ECO:0000269|PubMed:22142902, ECO:0000269|PubMed:24927501}. CC -!- SUBUNIT: Interacts (via N-terminus coiled coil domains) with tubulin CC and microtubules. {ECO:0000269|PubMed:22142902, CC ECO:0000269|PubMed:24927501}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:15561729}. Note=Localizes to the microtubules CC throughout mitosis. {ECO:0000269|PubMed:22142902}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8IWC1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IWC1-2; Sequence=VSP_028499; CC Name=3; CC IsoId=Q8IWC1-3; Sequence=VSP_028498; CC Name=4; CC IsoId=Q8IWC1-4; Sequence=VSP_045008; CC -!- INDUCTION: Expression is cell cycle dependent with the highest levels CC during G1, S, and M phases, and low level in G2 phase. CC {ECO:0000269|PubMed:22142902}. CC -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH64350.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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; AK022711; BAB14195.1; -; mRNA. DR EMBL; AK301478; BAG62994.1; -; mRNA. DR EMBL; AL832120; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL078638; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471150; EAW88475.1; -; Genomic_DNA. DR EMBL; BC040518; AAH40518.1; -; mRNA. DR EMBL; BC064350; AAH64350.1; ALT_SEQ; mRNA. DR CCDS; CCDS44004.1; -. [Q8IWC1-1] DR CCDS; CCDS55508.1; -. [Q8IWC1-3] DR CCDS; CCDS55509.1; -. [Q8IWC1-4] DR RefSeq; NP_001166987.1; NM_001173516.1. [Q8IWC1-4] DR RefSeq; NP_001166988.1; NM_001173517.1. [Q8IWC1-3] DR RefSeq; NP_078873.2; NM_024597.3. [Q8IWC1-1] DR AlphaFoldDB; Q8IWC1; -. DR SMR; Q8IWC1; -. DR BioGRID; 122777; 112. DR IntAct; Q8IWC1; 49. DR MINT; Q8IWC1; -. DR STRING; 9606.ENSP00000318086; -. DR GlyGen; Q8IWC1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8IWC1; -. DR PhosphoSitePlus; Q8IWC1; -. DR BioMuta; MAP7D3; -. DR DMDM; 158705880; -. DR EPD; Q8IWC1; -. DR jPOST; Q8IWC1; -. DR MassIVE; Q8IWC1; -. DR MaxQB; Q8IWC1; -. DR PaxDb; 9606-ENSP00000318086; -. DR PeptideAtlas; Q8IWC1; -. DR ProteomicsDB; 43531; -. DR ProteomicsDB; 70842; -. [Q8IWC1-1] DR ProteomicsDB; 70843; -. [Q8IWC1-2] DR ProteomicsDB; 70844; -. [Q8IWC1-3] DR Pumba; Q8IWC1; -. DR Antibodypedia; 51701; 32 antibodies from 10 providers. DR DNASU; 79649; -. DR Ensembl; ENST00000316077.14; ENSP00000318086.9; ENSG00000129680.16. [Q8IWC1-1] DR Ensembl; ENST00000370661.5; ENSP00000359695.1; ENSG00000129680.16. [Q8IWC1-3] DR Ensembl; ENST00000370663.9; ENSP00000359697.5; ENSG00000129680.16. [Q8IWC1-4] DR GeneID; 79649; -. DR KEGG; hsa:79649; -. DR MANE-Select; ENST00000316077.14; ENSP00000318086.9; NM_024597.4; NP_078873.2. DR UCSC; uc004ezs.4; human. [Q8IWC1-1] DR AGR; HGNC:25742; -. DR CTD; 79649; -. DR DisGeNET; 79649; -. DR GeneCards; MAP7D3; -. DR HGNC; HGNC:25742; MAP7D3. DR HPA; ENSG00000129680; Low tissue specificity. DR MIM; 300930; gene. DR neXtProt; NX_Q8IWC1; -. DR OpenTargets; ENSG00000129680; -. DR PharmGKB; PA162394972; -. DR VEuPathDB; HostDB:ENSG00000129680; -. DR eggNOG; ENOG502SDH7; Eukaryota. DR GeneTree; ENSGT00950000182941; -. DR InParanoid; Q8IWC1; -. DR OMA; CDMKTFR; -. DR OrthoDB; 5362734at2759; -. DR PhylomeDB; Q8IWC1; -. DR TreeFam; TF332273; -. DR PathwayCommons; Q8IWC1; -. DR SignaLink; Q8IWC1; -. DR BioGRID-ORCS; 79649; 13 hits in 782 CRISPR screens. DR ChiTaRS; MAP7D3; human. DR GenomeRNAi; 79649; -. DR Pharos; Q8IWC1; Tbio. DR PRO; PR:Q8IWC1; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8IWC1; Protein. DR Bgee; ENSG00000129680; Expressed in calcaneal tendon and 127 other cell types or tissues. DR ExpressionAtlas; Q8IWC1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0046785; P:microtubule polymerization; IDA:UniProtKB. DR InterPro; IPR008604; MAP7_fam. DR PANTHER; PTHR15073:SF5; MAP7 DOMAIN-CONTAINING PROTEIN 3; 1. DR PANTHER; PTHR15073; MICROTUBULE-ASSOCIATED PROTEIN; 1. DR Pfam; PF05672; MAP7; 1. DR Genevisible; Q8IWC1; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; KW Phosphoprotein; Reference proteome. FT CHAIN 1..876 FT /note="MAP7 domain-containing protein 3" FT /id="PRO_0000306812" FT REGION 72..137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 407..475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 509..533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 613..697 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 723..754 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 802..876 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 65..144 FT /evidence="ECO:0000255" FT COILED 558..640 FT /evidence="ECO:0000255" FT COILED 689..724 FT /evidence="ECO:0000255" FT COMPBIAS 170..211 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..244 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..475 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..818 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 819..835 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 185 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 490 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 524 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 770 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 817 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 832 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..23 FT /note="MMADGAAAGAGGSPSLRELRARM -> MTSPR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045008" FT VAR_SEQ 179..214 FT /note="ANKRSASTEKLEQGTSALIRQMPLSSAGLQNSVAKR -> G (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_028498" FT VAR_SEQ 246..286 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_028499" FT VARIANT 502 FT /note="E -> A (in dbSNP:rs1055497)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_035314" FT VARIANT 561 FT /note="K -> R (in dbSNP:rs748582851)" FT /evidence="ECO:0000269|PubMed:26506222" FT /id="VAR_077003" FT VARIANT 628 FT /note="Q -> R (in dbSNP:rs2273221)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_035315" FT CONFLICT 71 FT /note="L -> S (in Ref. 1; BAG62994)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="K -> R (in Ref. 1; BAG62994)" FT /evidence="ECO:0000305" FT CONFLICT 448 FT /note="A -> T (in Ref. 5; AAH40518)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="R -> Q (in Ref. 2; AL832120)" FT /evidence="ECO:0000305" SQ SEQUENCE 876 AA; 98429 MW; C149899FB0002B39 CRC64; MMADGAAAGA GGSPSLRELR ARMVAAANEI AKERRKQDVV NRVATHSSNI RSTFKPVIDG SMLKNDIKQR LARERREEKR RQQDANKETQ LLEKERKTKL QYEKQMEERQ RKLKERKEKE EQRRIAAEEK RHQKDEAQKE KFTAILYRTL ERRRLADDYQ QKRWSWGGSA MANSESKTAN KRSASTEKLE QGTSALIRQM PLSSAGLQNS VAKRKTDKER SSSLNRRDSN LHSSTDKEQA ERKPRVTGVT NYVMQYVTVP LRKCTSDELR AVMFPMSTMK IPPQTKVEES PLEKVETPPK ASVDAPPQVN VEVFCNTSME ASPKAGVGMA PEVSTDSFPV VSVDVSPVVS TYDSEMSMDA SPELSIEALP KVDLETVPKV SIVASPEASL EAPPEVSLEA LPEVSVEAAP EGSLEAPPKG SAEVAPKESV KGSPKESMEA SPEAMVKASP KTSLEASMEA SPKAKARDAP KKSEMDKQAL IPIAKKRLSS YTECYKWSSS PENACGLPSP ISTNRQIQKN CPPSPLPLIS KQSPQTSFPY KIMPIQHTLS VQSASSTVKK KKETVSKTTN RCEALSQRHM IYEESGNKST AGIMNAEAAT KILTELRRLA REQREKEEEE RQREEMQQRV IKKSKDMAKE AVGGQAEDHL KLKDGQQQNE TKKKKGWLDQ EDQEAPLQKG DAKIKAQEEA DKRKKEHERI MLQNLQERLE RKKRIEEIMK RTRKTDVNAS KVTETSSHDI YEEAEADNEE SDKDSLNEMF PSAILNGTGS PTKFKMPFNN AKKMTHKLVF LEDGTSQVRK EPKTYFNGDL KNFRQKSMKD TSIQEVVSRP SSKRMTSHTT KTRKADETNT TSRSSAQTKS EGFHDILPKS SDTFRQ //