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Q9H8S9 (MOB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MOB kinase activator 1A
Alternative name(s):
Mob1 alpha
Short name=Mob1A
Mob1 homolog 1B
Mps one binder kinase activator-like 1B
Gene names
Name:MOB1A
Synonyms:C2orf6, MOB4B, MOBK1B, MOBKL1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38. Ref.7 Ref.9 Ref.10

Subunit structure

Binds STK38 and STK38L. Interacts with LATS1 and LATS2. Forms a tripartite complex with STK38 and STK3/MST2. Ref.7 Ref.9 Ref.10

Tissue specificity

Adrenal gland, bone marrow, brain, placenta, prostate, salivary gland, skeletal muscle, testis, thymus, thyroid gland, heart, spinal cord, fetal brain and fetal liver. Ref.10

Post-translational modification

Phosphorylated by STK3/MST2 and STK4/MST1 and this phosphorylation enhances its binding to LATS1. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the MOB1/phocein family.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H8S9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H8S9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     138-148: VPFPKNFMSVA → ELTLSKYSFFF
     149-216: Missing.
Note: May be due to an intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 216215MOB kinase activator 1A
PRO_0000193566

Sites

Metal binding791Zinc
Metal binding841Zinc
Metal binding1611Zinc
Metal binding1661Zinc

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.11
Modified residue121Phosphothreonine Ref.8
Modified residue351Phosphothreonine Ref.8
Modified residue741Phosphothreonine; by STK3/MST2 Ref.9
Modified residue1811Phosphothreonine Ref.9

Natural variations

Alternative sequence138 – 14811VPFPKNFMSVA → ELTLSKYSFFF in isoform 2.
VSP_012295
Alternative sequence149 – 21668Missing in isoform 2.
VSP_012296

Experimental info

Sequence conflict51F → L in BAB14525. Ref.3
Sequence conflict1761E → G in BAA91810. Ref.3

Secondary structure

........................... 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 58043AECAD1F5987

FASTA21625,080
        10         20         30         40         50         60 
MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG EDLNEWIAVN 

        70         80         90        100        110        120 
TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG TNIKKPIKCS APKYIDYLMT 

       130        140        150        160        170        180 
WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN 

       190        200        210 
TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LGSKDR 

« Hide

Isoform 2 [UniParc].

Checksum: 70F00C42359120F2
Show »

FASTA14816,928

References

« Hide 'large scale' references
[1]"Human MOB1."
Kagaya S., Kotani S., Todokoro K.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of the human Mob-1 like proteins."
Florindo C.S., Tavares A.A.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Embryo and Ovary.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 1).
Tissue: Placenta.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8, ACETYLATION AT SER-2.
Tissue: Platelet.
[7]"Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
J. Biol. Chem. 279:35228-35235(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STK38 AND STK38L.
[8]"MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation."
Praskova M., Xia F., Avruch J.
Curr. Biol. 18:311-321(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-12 AND THR-35 BY STK3/MST2 AND STK4/MST1.
[9]"Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, INTERACTION WITH STK38 AND STK3/MST2.
[10]"Molecular characterization of human homologs of yeast MOB1."
Chow A., Hao Y., Yang X.
Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LATS1 AND LATS2, TISSUE SPECIFICITY.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Crystal structure of a human Mob1 protein: toward understanding Mob-regulated cell cycle pathways."
Stavridi E.S., Harris K.G., Huyen Y., Bothos J., Verwoerd P.-M., Stayrook S.E., Pavletich N.P., Jeffrey P.D., Luca F.C.
Structure 11:1163-1170(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-216, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ZINC-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016839 mRNA. Translation: BAB19058.1.
AJ577474 mRNA. Translation: CAE12093.1.
AK001650 mRNA. Translation: BAA91810.1.
AK021657 mRNA. Translation: BAB13868.1.
AK023321 mRNA. Translation: BAB14525.1.
AC073263 Genomic DNA. Translation: AAX93060.1.
BC003398 mRNA. Translation: AAH03398.1.
CCDSCCDS46340.1. [Q9H8S9-1]
RefSeqNP_060691.2. NM_018221.3. [Q9H8S9-1]
UniGeneHs.602092.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PI1X-ray2.00A33-216[»]
4JIZX-ray2.10A40-211[»]
ProteinModelPortalQ9H8S9.
SMRQ9H8S9. Positions 33-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120527. 46 interactions.
DIPDIP-36594N.
IntActQ9H8S9. 39 interactions.
MINTMINT-197366.
STRING9606.ENSP00000379364.

PTM databases

PhosphoSiteQ9H8S9.

Polymorphism databases

DMDM56749356.

2D gel databases

OGPQ9H8S9.

Proteomic databases

MaxQBQ9H8S9.
PaxDbQ9H8S9.
PRIDEQ9H8S9.

Protocols and materials databases

DNASU55233.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396049; ENSP00000379364; ENSG00000114978. [Q9H8S9-1]
GeneID55233.
KEGGhsa:55233.
UCSCuc002skh.4. human. [Q9H8S9-1]
uc002ski.2. human. [Q9H8S9-2]

Organism-specific databases

CTD55233.
GeneCardsGC02M074382.
HGNCHGNC:16015. MOB1A.
MIM609281. gene.
neXtProtNX_Q9H8S9.
PharmGKBPA25894.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287143.
HOGENOMHOG000164685.
HOVERGENHBG052489.
InParanoidQ9H8S9.
KOK06685.
OMAFEYRWAD.
OrthoDBEOG7N0C5K.
PhylomeDBQ9H8S9.
TreeFamTF300789.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9H8S9.
BgeeQ9H8S9.
CleanExHS_MOBKL1B.
GenevestigatorQ9H8S9.

Family and domain databases

Gene3D1.20.140.30. 1 hit.
InterProIPR005301. Mob1_phocein.
[Graphical view]
PANTHERPTHR22599. PTHR22599. 1 hit.
PfamPF03637. Mob1_phocein. 1 hit.
[Graphical view]
SUPFAMSSF101152. SSF101152. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9H8S9.
GeneWikiMOBKL1B.
GenomeRNAi55233.
NextBio59245.
PROQ9H8S9.
SOURCESearch...

Entry information

Entry nameMOB1A_HUMAN
AccessionPrimary (citable) accession number: Q9H8S9
Secondary accession number(s): Q53S34 expand/collapse secondary AC list , Q9H3T5, Q9HAI0, Q9NVE2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM