Q9UHA4 (LTOR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ragulator complex protein LAMTOR3

Alternative name(s):
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3
MEK-binding partner 1
Short name=Mp1
Mitogen-activated protein kinase kinase 1-interacting protein 1
Mitogen-activated protein kinase scaffold protein 1

Gene names

Name:	LAMTOR3
Synonyms:	MAP2K1IP1, MAPKSP1
ORF Names:	PRO2783

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	124 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, recruits the Rag GTPases and the mTORC1 complex to lysosomes, a key step in activation of the TOR signaling cascade by amino acids. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. Ref.6
Subunit structure	Interacts with MAP2K1/MEK1 and MAPK2. Interacts with MORG1 By similarity. Part of the Ragulator complex composed of LAMTOR1, LAMTOR2 and LAMTOR3. Interacts with LAMTOR1; the interaction is direct.
Subcellular location	Late endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the LAMTOR3 family.

Ontologies

Keywords
Cellular component	Endosome Membrane
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular protein localization Inferred from mutant phenotype Ref.6. Source: UniProtKB cellular response to amino acid stimulus Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of TOR signaling cascade Inferred from mutant phenotype Ref.6. Source: UniProtKB
Cellular component	Ragulator complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LAMTOR2	Q9Y2Q5	3	EBI-1038192,EBI-2643704

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 124

124

Ragulator complex protein LAMTOR3

PRO_0000221005

Regions

Region

57 – 70

14

Required for interaction with LAMTOR2 By similarity

Experimental info

Sequence conflict

49

1

F → L in AAG35540. Ref.2

Secondary structure

1

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124

Helix Strand Turn

Details...

Helix

2 – 12

11

Helix

13 – 15

3

Beta strand

19 – 25

7

Beta strand

31 – 36

6

Helix

42 – 45

4

Helix

47 – 60

14

Beta strand

63 – 65

3

Beta strand

68 – 85

18

Beta strand

88 – 95

8

Helix

100 – 115

16

Sequences

	Sequence		Length	Mass (Da)
	Q9UHA4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 0A5196CF41D83D13	FASTA	124	13,623
	10 20 30 40 50 60 MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDNA PEHALRPGFL STFALATDQG 70 80 90 100 110 120 SKLGLSKNKS IICYYNTYQV VQFNRLPLVV SFIASSSANT GLIVSLEKEL APLFEELRQV VEVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel genes expressed in human dendritic cells." Li Y., Huang C., Ren S., Tu Y., Gu W., Wang Y., Han Z., Chen Z. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Dendritic cell.
[2]	"Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal liver.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[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 (JUL-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids." Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M. Cell 141:290-303(2010) [PubMed: 20381137] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN RAGULATOR COMPLEX.
[7]	"The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal MAP kinase signaling." Lunin V.V., Munger C., Wagner J., Ye Z., Cygler M., Sacher M. J. Biol. Chem. 279:23422-23430(2004) [PubMed: 15016825] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-124 IN COMPLEX WITH LAMTOR2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF201947 mRNA. Translation: AAF17239.1.
AF130115 mRNA. Translation: AAG35540.1.
AK311755 mRNA. Translation: BAG34698.1.
CH471057 Genomic DNA. Translation: EAX06112.1.
BC026245 mRNA. Translation: AAH26245.1.

IPI

IPI00030919.

RefSeq

NP_068805.1. NM_021970.3.

UniGene

Hs.433332.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SKO	X-ray	2.00	A	2-124	[»]
2ZL1	X-ray	2.00	A	2-124	[»]
3CPT	X-ray	1.90	A	2-124	[»]

ProteinModelPortal

Q9UHA4.

SMR

Q9UHA4. Positions 3-121.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHA4. 8 interactions.

STRING

Q9UHA4.

Polymorphism databases

DMDM

24418562.

Proteomic databases

PeptideAtlas

Q9UHA4.

PRIDE

Q9UHA4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000226522; ENSP00000226522; ENSG00000109270.

GeneID

8649.

KEGG

hsa:8649.

UCSC

uc003hvg.1. human.

Organism-specific databases

CTD

8649.

GeneCards

GC04M100800.

H-InvDB

HIX0004402.

HGNC

HGNC:15606. LAMTOR3.

HPA

HPA026858.

MIM

603296. gene.

neXtProt

NX_Q9UHA4.

PharmGKB

PA164722189.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000013159.

HOGENOM

HBG281183.

HOVERGEN

HBG052480.

InParanoid

Q9UHA4.

OMA

CNTGHIL.

OrthoDB

EOG4J9N1B.

PhylomeDB

Q9UHA4.

Gene expression databases

ArrayExpress

Q9UHA4.

Bgee

Q9UHA4.

CleanEx

HS_MAPKSP1.

Genevestigator

Q9UHA4.

GermOnline

ENSG00000109270. Homo sapiens.

Family and domain databases

InterPro

IPR015019. MAPKK1_Int.
[Graphical view]

KO

K04370.

PANTHER

PTHR13378. MAPKK1_Int. 1 hit.

Pfam

PF08923. MAPKK1_Int. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

32431.

SOURCE

Search...

Entry information

Entry name

LTOR3_HUMAN

Accession

Primary (citable) accession number: Q9UHA4
Secondary accession number(s): B2R4A1, Q9H364

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 89 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.