MA6D1_HUMAN
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 03-AUG-2022, entry version 131.
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}.
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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 AlphaFoldDB; Q9H9H5; -.
DR BioGRID; 123004; 1.
DR IntAct; Q9H9H5; 1.
DR STRING; 9606.ENSP00000314560; -.
DR GlyGen; Q9H9H5; 1 site, 1 O-linked glycan (1 site).
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; 18 antibodies from 10 providers.
DR DNASU; 79929; -.
DR Ensembl; ENST00000318631.8; ENSP00000314560.4; ENSG00000180834.8.
DR GeneID; 79929; -.
DR KEGG; hsa:79929; -.
DR MANE-Select; ENST00000318631.8; ENSP00000314560.4; NM_024871.4; NP_079147.1.
DR UCSC; uc003fmc.3; human.
DR CTD; 79929; -.
DR DisGeNET; 79929; -.
DR GeneCards; MAP6D1; -.
DR HGNC; HGNC:25753; MAP6D1.
DR HPA; ENSG00000180834; Tissue enhanced (brain, choroid plexus, skeletal muscle).
DR MIM; 610593; gene.
DR neXtProt; NX_Q9H9H5; -.
DR OpenTargets; ENSG00000180834; -.
DR PharmGKB; PA142671480; -.
DR VEuPathDB; HostDB:ENSG00000180834; -.
DR eggNOG; ENOG502RXB9; Eukaryota.
DR GeneTree; ENSGT00530000063947; -.
DR HOGENOM; CLU_089524_0_0_1; -.
DR InParanoid; Q9H9H5; -.
DR OMA; PREDYQP; -.
DR OrthoDB; 1408472at2759; -.
DR PhylomeDB; Q9H9H5; -.
DR TreeFam; TF338320; -.
DR PathwayCommons; Q9H9H5; -.
DR SignaLink; Q9H9H5; -.
DR BioGRID-ORCS; 79929; 12 hits in 1072 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 94 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 REGION 33..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
