M1IP1_HUMAN
ID M1IP1_HUMAN Reviewed; 183 AA.
AC Q9NPA3; D3DWB2;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mid1-interacting protein 1;
DE AltName: Full=Gastrulation-specific G12-like protein;
DE AltName: Full=Mid1-interacting G12-like protein;
DE AltName: Full=Protein STRAIT11499;
DE AltName: Full=Spot 14-related protein;
DE Short=S14R;
DE Short=Spot 14-R;
GN Name=MID1IP1; Synonyms=MIG12;
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].
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Lanfranchi G.;
RT "Full-length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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].
RC TISSUE=Lymph, and Placenta;
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 IDENTIFICATION.
RX PubMed=15070402; DOI=10.1186/1471-2121-5-9;
RA Berti C., Fontanella B., Ferrentino R., Meroni G.;
RT "Mig12, a novel Opitz syndrome gene product partner, is expressed in the
RT embryonic ventral midline and co-operates with Mid1 to bundle and stabilize
RT microtubules.";
RL BMC Cell Biol. 5:9-9(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Plays a role in the regulation of lipogenesis in liver. Up-
CC regulates ACACA enzyme activity. Required for efficient lipid
CC biosynthesis, including triacylglycerol, diacylglycerol and
CC phospholipid. Involved in stabilization of microtubules (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer in the absence of THRSP. Heterodimer with THRSP. The
CC homodimer interacts with ACACA and ACACB. Promotes polymerization of
CC Acetyl-CoA carboxylase to form complexes that contain MID1IP1 and ACACA
CC and/or ACACB. Interaction with THRSP interferes with ACACA binding (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NPA3; Q96MA6: AK8; NbExp=3; IntAct=EBI-750096, EBI-8466265;
CC Q9NPA3; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-750096, EBI-10172526;
CC Q9NPA3; P16473: TSHR; NbExp=2; IntAct=EBI-750096, EBI-13939599;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9CQ20}. Note=Associated with microtubules.
CC {ECO:0000250|UniProtKB:Q9CQ20}.
CC -!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA01482.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ272057; CAB89113.1; -; mRNA.
DR EMBL; AK001248; BAA91580.1; -; mRNA.
DR EMBL; CR457220; CAG33501.1; -; mRNA.
DR EMBL; CH471141; EAW59435.1; -; Genomic_DNA.
DR EMBL; CH471141; EAW59436.1; -; Genomic_DNA.
DR EMBL; BC008908; AAH08908.1; -; mRNA.
DR EMBL; BC019332; AAH19332.1; -; mRNA.
DR EMBL; BK001260; DAA01482.1; ALT_INIT; mRNA.
DR CCDS; CCDS14249.1; -.
DR RefSeq; NP_001092260.1; NM_001098790.1.
DR RefSeq; NP_001092261.1; NM_001098791.1.
DR RefSeq; NP_067065.1; NM_021242.5.
DR AlphaFoldDB; Q9NPA3; -.
DR SMR; Q9NPA3; -.
DR BioGRID; 121846; 71.
DR IntAct; Q9NPA3; 23.
DR MINT; Q9NPA3; -.
DR STRING; 9606.ENSP00000483547; -.
DR GlyGen; Q9NPA3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPA3; -.
DR PhosphoSitePlus; Q9NPA3; -.
DR BioMuta; MID1IP1; -.
DR DMDM; 21759081; -.
DR EPD; Q9NPA3; -.
DR jPOST; Q9NPA3; -.
DR MassIVE; Q9NPA3; -.
DR MaxQB; Q9NPA3; -.
DR PaxDb; Q9NPA3; -.
DR PeptideAtlas; Q9NPA3; -.
DR PRIDE; Q9NPA3; -.
DR ProteomicsDB; 81950; -.
DR Antibodypedia; 24940; 187 antibodies from 33 providers.
DR DNASU; 58526; -.
DR Ensembl; ENST00000336949.7; ENSP00000338706.6; ENSG00000165175.17.
DR Ensembl; ENST00000378474.3; ENSP00000367735.3; ENSG00000165175.17.
DR Ensembl; ENST00000457894.5; ENSP00000416670.1; ENSG00000165175.17.
DR Ensembl; ENST00000614558.3; ENSP00000483547.1; ENSG00000165175.17.
DR GeneID; 58526; -.
DR KEGG; hsa:58526; -.
DR MANE-Select; ENST00000614558.3; ENSP00000483547.1; NM_021242.6; NP_067065.1.
DR UCSC; uc004dei.5; human.
DR CTD; 58526; -.
DR DisGeNET; 58526; -.
DR GeneCards; MID1IP1; -.
DR HGNC; HGNC:20715; MID1IP1.
DR HPA; ENSG00000165175; Tissue enhanced (brain, skeletal muscle).
DR MIM; 300961; gene.
DR neXtProt; NX_Q9NPA3; -.
DR OpenTargets; ENSG00000165175; -.
DR PharmGKB; PA134941916; -.
DR VEuPathDB; HostDB:ENSG00000165175; -.
DR eggNOG; ENOG502S0KR; Eukaryota.
DR GeneTree; ENSGT00500000044890; -.
DR HOGENOM; CLU_066079_1_0_1; -.
DR InParanoid; Q9NPA3; -.
DR OMA; RRDMYSH; -.
DR OrthoDB; 1326063at2759; -.
DR PhylomeDB; Q9NPA3; -.
DR TreeFam; TF326826; -.
DR PathwayCommons; Q9NPA3; -.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR SignaLink; Q9NPA3; -.
DR SIGNOR; Q9NPA3; -.
DR BioGRID-ORCS; 58526; 13 hits in 711 CRISPR screens.
DR ChiTaRS; MID1IP1; human.
DR GenomeRNAi; 58526; -.
DR Pharos; Q9NPA3; Tbio.
DR PRO; PR:Q9NPA3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NPA3; protein.
DR Bgee; ENSG00000165175; Expressed in C1 segment of cervical spinal cord and 185 other tissues.
DR Genevisible; Q9NPA3; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051351; P:positive regulation of ligase activity; ISS:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; ISS:UniProtKB.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR009786; Spot_14.
DR PANTHER; PTHR14315; PTHR14315; 1.
DR Pfam; PF07084; Spot_14; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Lipid biosynthesis; Lipid metabolism;
KW Microtubule; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..183
FT /note="Mid1-interacting protein 1"
FT /id="PRO_0000123777"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 183 AA; 20202 MW; A62D5924A7B17D5F CRC64;
MMQICDTYNQ KHSLFNAMNR FIGAVNNMDQ TVMVPSLLRD VPLADPGLDN DVGVEVGGSG
GCLEERTPPV PDSGSANGSF FAPSRDMYSH YVLLKSIRND IEWGVLHQPP PPAGSEEGSA
WKSKDILVDL GHLEGADAGE EDLEQQFHYH LRGLHTVLSK LTRKANILTN RYKQEIGFGN
WGH
