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Q9NPA3

- M1IP1_HUMAN

UniProt

Q9NPA3 - M1IP1_HUMAN

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Protein

Mid1-interacting protein 1

Gene
MID1IP1, MIG12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules By similarity.

GO - Biological processi

  1. lipid metabolic process Source: UniProtKB-KW
  2. negative regulation of microtubule depolymerization Source: UniProtKB
  3. positive regulation of fatty acid biosynthetic process Source: UniProtKB
  4. positive regulation of ligase activity Source: UniProtKB
  5. protein polymerization Source: UniProtKB
  6. regulation of lipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Mid1-interacting protein 1
Alternative name(s):
Gastrulation-specific G12-like protein
Mid1-interacting G12-like protein
Protein STRAIT11499
Spot 14-related protein
Short name:
S14R
Short name:
Spot 14-R
Gene namesi
Name:MID1IP1
Synonyms:MIG12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:20715. MID1IP1.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity
Note: Associated with microtubules By similarity.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. microtubule Source: UniProtKB-KW
  3. microtubule cytoskeleton Source: UniProtKB
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134941916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Mid1-interacting protein 1PRO_0000123777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei75 – 751Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NPA3.
PaxDbiQ9NPA3.
PRIDEiQ9NPA3.

PTM databases

PhosphoSiteiQ9NPA3.

Expressioni

Gene expression databases

BgeeiQ9NPA3.
CleanExiHS_MID1IP1.
GenevestigatoriQ9NPA3.

Organism-specific databases

HPAiHPA038816.

Interactioni

Subunit structurei

Homodimer in the absence of THRSP. Heterodimer with THRSP. The homodimer interacts with ACACA and ACACB. Promotes polymerization of Acetyl-CoA carboxylase to form complexes that contain MID1IP1 and ACACA and/or ACACB. Interaction with THRSP interferes with ACACA binding By similarity.

Protein-protein interaction databases

BioGridi121846. 5 interactions.
IntActiQ9NPA3. 2 interactions.
MINTiMINT-1445333.
STRINGi9606.ENSP00000338706.

Structurei

3D structure databases

ProteinModelPortaliQ9NPA3.
SMRiQ9NPA3. Positions 11-177.

Family & Domainsi

Sequence similaritiesi

Belongs to the SPOT14 family.

Phylogenomic databases

eggNOGiNOG42079.
HOGENOMiHOG000001157.
HOVERGENiHBG002528.
InParanoidiQ9NPA3.
OMAiGFSNWGH.
OrthoDBiEOG7K6PW4.
PhylomeDBiQ9NPA3.
TreeFamiTF326826.

Family and domain databases

InterProiIPR009786. Spot_14.
[Graphical view]
PANTHERiPTHR14315. PTHR14315. 1 hit.
PfamiPF07084. Spot_14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NPA3-1 [UniParc]FASTAAdd to Basket

« Hide

MMQICDTYNQ KHSLFNAMNR FIGAVNNMDQ TVMVPSLLRD VPLADPGLDN    50
DVGVEVGGSG GCLEERTPPV PDSGSANGSF FAPSRDMYSH YVLLKSIRND 100
IEWGVLHQPP PPAGSEEGSA WKSKDILVDL GHLEGADAGE EDLEQQFHYH 150
LRGLHTVLSK LTRKANILTN RYKQEIGFGN WGH 183
Length:183
Mass (Da):20,202
Last modified:October 1, 2000 - v1
Checksum:iA62D5924A7B17D5F
GO

Sequence cautioni

The sequence DAA01482.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ272057 mRNA. Translation: CAB89113.1.
AK001248 mRNA. Translation: BAA91580.1.
CR457220 mRNA. Translation: CAG33501.1.
CH471141 Genomic DNA. Translation: EAW59435.1.
CH471141 Genomic DNA. Translation: EAW59436.1.
BC008908 mRNA. Translation: AAH08908.1.
BC019332 mRNA. Translation: AAH19332.1.
BK001260 mRNA. Translation: DAA01482.1. Different initiation.
CCDSiCCDS14249.1.
RefSeqiNP_001092260.1. NM_001098790.1.
NP_001092261.1. NM_001098791.1.
NP_067065.1. NM_021242.5.
UniGeneiHs.522605.
Hs.662789.

Genome annotation databases

EnsembliENST00000336949; ENSP00000338706; ENSG00000165175.
ENST00000378474; ENSP00000367735; ENSG00000165175.
ENST00000457894; ENSP00000416670; ENSG00000165175.
GeneIDi58526.
KEGGihsa:58526.
UCSCiuc004dei.4. human.

Polymorphism databases

DMDMi21759081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ272057 mRNA. Translation: CAB89113.1 .
AK001248 mRNA. Translation: BAA91580.1 .
CR457220 mRNA. Translation: CAG33501.1 .
CH471141 Genomic DNA. Translation: EAW59435.1 .
CH471141 Genomic DNA. Translation: EAW59436.1 .
BC008908 mRNA. Translation: AAH08908.1 .
BC019332 mRNA. Translation: AAH19332.1 .
BK001260 mRNA. Translation: DAA01482.1 . Different initiation.
CCDSi CCDS14249.1.
RefSeqi NP_001092260.1. NM_001098790.1.
NP_001092261.1. NM_001098791.1.
NP_067065.1. NM_021242.5.
UniGenei Hs.522605.
Hs.662789.

3D structure databases

ProteinModelPortali Q9NPA3.
SMRi Q9NPA3. Positions 11-177.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121846. 5 interactions.
IntActi Q9NPA3. 2 interactions.
MINTi MINT-1445333.
STRINGi 9606.ENSP00000338706.

PTM databases

PhosphoSitei Q9NPA3.

Polymorphism databases

DMDMi 21759081.

Proteomic databases

MaxQBi Q9NPA3.
PaxDbi Q9NPA3.
PRIDEi Q9NPA3.

Protocols and materials databases

DNASUi 58526.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336949 ; ENSP00000338706 ; ENSG00000165175 .
ENST00000378474 ; ENSP00000367735 ; ENSG00000165175 .
ENST00000457894 ; ENSP00000416670 ; ENSG00000165175 .
GeneIDi 58526.
KEGGi hsa:58526.
UCSCi uc004dei.4. human.

Organism-specific databases

CTDi 58526.
GeneCardsi GC0XP038660.
HGNCi HGNC:20715. MID1IP1.
HPAi HPA038816.
neXtProti NX_Q9NPA3.
PharmGKBi PA134941916.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42079.
HOGENOMi HOG000001157.
HOVERGENi HBG002528.
InParanoidi Q9NPA3.
OMAi GFSNWGH.
OrthoDBi EOG7K6PW4.
PhylomeDBi Q9NPA3.
TreeFami TF326826.

Miscellaneous databases

GenomeRNAii 58526.
NextBioi 65082.
PROi Q9NPA3.

Gene expression databases

Bgeei Q9NPA3.
CleanExi HS_MID1IP1.
Genevestigatori Q9NPA3.

Family and domain databases

InterProi IPR009786. Spot_14.
[Graphical view ]
PANTHERi PTHR14315. PTHR14315. 1 hit.
Pfami PF07084. Spot_14. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Full-length sequencing of some human and murine muscular transcripts (Telethon Italy project B41)."
    Frigimelica E., Lanfranchi G.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph and Placenta.
  6. "Mig12, a novel Opitz syndrome gene product partner, is expressed in the embryonic ventral midline and co-operates with Mid1 to bundle and stabilize microtubules."
    Berti C., Fontanella B., Ferrentino R., Meroni G.
    BMC Cell Biol. 5:9-9(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiM1IP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NPA3
Secondary accession number(s): D3DWB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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