ID MA6D1_HUMAN Reviewed; 199 AA. AC Q9H9H5; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 10-FEB-2021, entry version 125. DE RecName: Full=MAP6 domain-containing protein 1; DE AltName: Full=21 kDa STOP-like protein; DE Short=SL21; GN Name=MAP6D1; 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]. 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]. RC TISSUE=Lung; 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 [3] RP PALMITOYLATION AT CYS-5; CYS-10 AND CYS-11, AND MUTAGENESIS OF CYS-5; RP CYS-10 AND CYS-11. RX PubMed=16837464; DOI=10.1074/jbc.m603380200; RA Gory-Faure S., Windscheid V., Bosc C., Peris L., Proietto D., Franck R., RA Denarier E., Job D., Andrieux A.; RT "STOP-like protein 21 is a novel member of the STOP family, revealing a RT Golgi localization of STOP proteins."; RL J. Biol. Chem. 281:28387-28396(2006). CC -!- FUNCTION: May have microtubule-stabilizing activity. {ECO:0000250}. CC -!- SUBUNIT: Interacts with calmodulin. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, cytoskeleton CC {ECO:0000250}. Note=Colocalizes with microtubules. {ECO:0000250}. CC -!- PTM: Palmitoylated. Palmitoylation enhances association with CC microtubules. {ECO:0000269|PubMed:16837464}. CC -!- SIMILARITY: Belongs to the STOP family. {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; AK022810; BAB14254.1; -; mRNA. DR EMBL; BC006434; AAH06434.1; -; mRNA. DR CCDS; CCDS3247.1; -. DR RefSeq; NP_079147.1; NM_024871.2. DR IntAct; Q9H9H5; 1. DR STRING; 9606.ENSP00000314560; -. DR PhosphoSitePlus; Q9H9H5; -. DR BioMuta; MAP6D1; -. DR DMDM; 74734016; -. DR jPOST; Q9H9H5; -. DR MassIVE; Q9H9H5; -. DR PaxDb; Q9H9H5; -. DR PeptideAtlas; Q9H9H5; -. DR PRIDE; Q9H9H5; -. DR ProteomicsDB; 81323; -. DR Antibodypedia; 50914; 19 antibodies. DR Ensembl; ENST00000318631; ENSP00000314560; ENSG00000180834. DR GeneID; 79929; -. DR KEGG; hsa:79929; -. DR UCSC; uc003fmc.3; human. DR CTD; 79929; -. DR DisGeNET; 79929; -. DR GeneCards; MAP6D1; -. DR HGNC; HGNC:25753; MAP6D1. DR HPA; ENSG00000180834; Group enriched (brain, skeletal muscle). DR MIM; 610593; gene. DR neXtProt; NX_Q9H9H5; -. DR OpenTargets; ENSG00000180834; -. DR PharmGKB; PA142671480; -. DR VEuPathDB; HostDB:ENSG00000180834.7; -. DR eggNOG; ENOG502RXB9; Eukaryota. DR GeneTree; ENSGT00530000063947; -. DR HOGENOM; CLU_089524_0_0_1; -. DR InParanoid; Q9H9H5; -. DR OMA; QRDFGVW; -. DR OrthoDB; 1408472at2759; -. DR PhylomeDB; Q9H9H5; -. DR TreeFam; TF338320; -. DR PathwayCommons; Q9H9H5; -. DR BioGRID-ORCS; 79929; 5 hits in 874 CRISPR screens. DR ChiTaRS; MAP6D1; human. DR GenomeRNAi; 79929; -. DR Pharos; Q9H9H5; Tdark. DR PRO; PR:Q9H9H5; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H9H5; protein. DR Bgee; ENSG00000180834; Expressed in C1 segment of cervical spinal cord and 189 other tissues. DR ExpressionAtlas; Q9H9H5; baseline and differential. DR Genevisible; Q9H9H5; HS. DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central. DR GO; GO:0005798; C:Golgi-associated vesicle; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro. DR GO; GO:0018009; P:N-terminal peptidyl-L-cysteine N-palmitoylation; IEA:Ensembl. DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl. DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central. DR InterPro; IPR007882; MAP6. DR PANTHER; PTHR14759; PTHR14759; 1. PE 1: Evidence at protein level; KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Golgi apparatus; Lipoprotein; KW Palmitate; Phosphoprotein; Reference proteome. FT CHAIN 1..199 FT /note="MAP6 domain-containing protein 1" FT /id="PRO_0000271915" FT MOD_RES 38 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14BB9" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14BB9" FT LIPID 5 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:16837464" FT LIPID 10 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:16837464" FT LIPID 11 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:16837464" FT MUTAGEN 5 FT /note="C->G: Loss of Golgi colocalization and gain of FT microtubule colocalization; when associated with C-10 and FT C-11." FT /evidence="ECO:0000269|PubMed:16837464" FT MUTAGEN 10 FT /note="C->G: Loss of Golgi colocalization and gain of FT microtubule colocalization; when associated with C-5 and C- FT 11." FT /evidence="ECO:0000269|PubMed:16837464" FT MUTAGEN 11 FT /note="C->G: Loss of Golgi colocalization and gain of FT microtubule colocalization; when associated with C-5 and C- FT 10." FT /evidence="ECO:0000269|PubMed:16837464" SQ SEQUENCE 199 AA; 21005 MW; 36AF2D2B9C60C5A3 CRC64; MAWPCISRLC CLARRWNQLD RSDVAVPLTL HGYSDLDSEE PGTGGAASRR GQPPAGARDS GRDVPLTQYQ RDFGLWTTPA GPKDPPPGRG PGAGGRRGKS SAQSSAPPAP GARGVYVLPI GDADAAAAVT TSYRQEFQAW TGVKPSRSTK TKPARVITTH TSGWDSSPGA GFQVPEVRKK FTPNPSAIFQ ASAPRILNV //