Q9NPA3 (M1IP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MID1IP1
Synonyms:	MIG12

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subunit structure	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.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Note: Associated with microtubules By similarity.
Sequence similarities	Belongs to the SPOT14 family.
Caution	It is uncertain whether Met-1 or Met-2 is the initiator.
Sequence caution	The sequence DAA01482.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule depolymerization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of fatty acid biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ligase activity Inferred from sequence or structural similarity. Source: UniProtKB protein polymerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 183	183	Mid1-interacting protein 1		PRO_0000123777
Amino acid modifications
	Modified residue	75	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9NPA3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A62D5924A7B17D5F	FASTA	183	20,202
	10 20 30 40 50 60 MMQICDTYNQ KHSLFNAMNR FIGAVNNMDQ TVMVPSLLRD VPLADPGLDN DVGVEVGGSG 70 80 90 100 110 120 GCLEERTPPV PDSGSANGSF FAPSRDMYSH YVLLKSIRND IEWGVLHQPP PPAGSEEGSA 130 140 150 160 170 180 WKSKDILVDL GHLEGADAGE EDLEQQFHYH LRGLHTVLSK LTRKANILTN RYKQEIGFGN WGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00009730.
RefSeq	NP_001092260.1. NM_001098790.1. NP_001092261.1. NM_001098791.1. NP_067065.1. NM_021242.4.
UniGene	Hs.522605.
3D structure databases
ProteinModelPortal	Q9NPA3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NPA3. 1 interaction.
MINT	MINT-1445333.
STRING	9606.ENSP00000338706.
PTM databases
PhosphoSite	Q9NPA3.
Polymorphism databases
DMDM	21759081.
Proteomic databases
PaxDb	Q9NPA3.
PRIDE	Q9NPA3.
Protocols and materials databases
DNASU	58526.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336949; ENSP00000338706; ENSG00000165175. ENST00000378474; ENSP00000367735; ENSG00000165175. ENST00000457894; ENSP00000416670; ENSG00000165175.
GeneID	58526.
KEGG	hsa:58526.
UCSC	uc004dei.4. human.
Organism-specific databases
CTD	58526.
GeneCards	GC0XP038660.
HGNC	HGNC:20715. MID1IP1.
HPA	HPA038816.
neXtProt	NX_Q9NPA3.
PharmGKB	PA134941916.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42079.
HOGENOM	HOG000001157.
HOVERGEN	HBG002528.
InParanoid	Q9NPA3.
OMA	GFSNWGH.
OrthoDB	EOG4C2HBJ.
PhylomeDB	Q9NPA3.
Gene expression databases
Bgee	Q9NPA3.
CleanEx	HS_MID1IP1.
Genevestigator	Q9NPA3.
GermOnline	ENSG00000165175. Homo sapiens.
Family and domain databases
InterPro	IPR009786. Spot_14. [Graphical view]
PANTHER	PTHR14315. PTHR14315. 1 hit.
Pfam	PF07084. Spot_14. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	58526.
NextBio	65082.

Entry information

Entry name

M1IP1_HUMAN

Accession

Primary (citable) accession number: Q9NPA3
Secondary accession number(s): D3DWB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.