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Q8BKH7 (SIN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Target of rapamycin complex 2 subunit MAPKAP1

Short name=TORC2 subunit MAPKAP1
Alternative name(s):
Mitogen-activated protein kinase 2-associated protein 1
Stress-activated map kinase-interacting protein 1
Short name=SAPK-interacting protein 1
Gene names
Name:Mapkap1
Synonyms:Mip1, Sin1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Isoform 1 is involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. Ref.4

Subunit structure

All isoforms except isoform 4can be incorporated into the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts with ATF2, MAP3K2 and MAPK8. Interacts with GTP-bound HRAS and KRAS. Interacts with IFNAR2 and SGK1. Isoform 2 interacts with NBN. Isoform 1 interacts with CCDC28B. Ref.6

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Cytoplasmic vesicle By similarity. Nucleus By similarity.

Tissue specificity

Uniquitously expresseed, with highest levels in testis, kidney and liver. Present in renal tubule cells (at protein level). Ref.5

Disruption phenotype

Death during early embryonic stages. Ref.4

Sequence similarities

Belongs to the SIN1 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BKH7-1)

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: Q8BKH7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     321-356: Missing.
Isoform 3 (identifier: Q8BKH7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-192: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 522521Target of rapamycin complex 2 subunit MAPKAP1
PRO_0000328033

Regions

Region2 – 267266Interaction with NBN By similarity
Region2 – 184183Interaction with MAP3K2 By similarity
Region468 – 52255Interaction with ATF2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue5101Phosphoserine By similarity

Natural variations

Alternative sequence2 – 192191Missing in isoform 3.
VSP_033208
Alternative sequence321 – 35636Missing in isoform 2.
VSP_033209

Experimental info

Sequence conflict5161E → K in AAH43296. Ref.3

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: 994C669D04065926

FASTA52259,009
        10         20         30         40         50         60 
MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK THPPSVPGDS GSEVQGSSGE 

        70         80         90        100        110        120 
TQGYIYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL 

       130        140        150        160        170        180 
KSLFEKKSLK EKPPSSGKQS ILSVRLEQCP LQLNNPFNEY SKFDGKGHVG TTATKKIDVY 

       190        200        210        220        230        240 
LPLHSSQDRL LPMTVVTMAS ARVQDLIGLI CWQYTSEGRE PKLNDNVSAY CLHIAEDDGE 

       250        260        270        280        290        300 
VDTDFPPLDS NEPIHKFGFS TLALVEKYSS PGLTSKESLF VRINAAHGFS LIQVDNTKVT 

       310        320        330        340        350        360 
MKEILLKAVK RRKGSQKISG PQYRLEKQSE PNIAVDLEST LESQNAWEFC LVRENSSRAD 

       370        380        390        400        410        420 
GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV QLGISGDKVE IDPVTNQKAS 

       430        440        450        460        470        480 
TKFWIKQKPI SIDCDLLCAC DLAEEKSPSH AVFKLTYLSS HDYKHLYFES DAATVSEIVL 

       490        500        510        520 
KVNYILESRA STARADYLAQ KQRKLNRRTS FSFQKEKKSG QQ 

« Hide

Isoform 2 [UniParc].

Checksum: F42F6C1899858727
Show »

FASTA48654,802
Isoform 3 [UniParc].

Checksum: CB7495E7C17E147F
Show »

FASTA33137,434

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo, Eye and Placenta.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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).
Strain: C57BL/6 and FVB/N.
Tissue: Brain, Mammary tumor and Olfactory epithelium.
[4]"SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity."
Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q., Qin J., Su B.
Cell 127:125-137(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Sin1 binds to both ATF-2 and p38 and enhances ATF-2-dependent transcription in an SAPK signaling pathway."
Makino C., Sano Y., Shinagawa T., Millar J.B., Ishii S.
Genes Cells 11:1239-1251(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein complex and is required for selective activation of the epithelial sodium channel."
Lu M., Wang J., Ives H.E., Pearce D.
J. Biol. Chem. 286:30647-30654(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027932 mRNA. Translation: BAC25671.1.
AK052045 mRNA. Translation: BAC34838.1.
AK132263 mRNA. Translation: BAE21066.1.
AL845262, AL808102 Genomic DNA. Translation: CAM15450.1.
AL845262, AL808102 Genomic DNA. Translation: CAM15451.1.
AL845262, AL808102 Genomic DNA. Translation: CAM15454.1.
AL808102, AL845262 Genomic DNA. Translation: CAM17090.1.
AL808102, AL845262 Genomic DNA. Translation: CAM17091.1.
AL808102, AL845262 Genomic DNA. Translation: CAM17094.1.
BC027377 mRNA. Translation: AAH27377.1.
BC031579 mRNA. Translation: AAH31579.1.
BC043296 mRNA. Translation: AAH43296.1.
BC090644 mRNA. Translation: AAH90644.1.
BC096618 mRNA. Translation: AAH96618.1.
CCDSCCDS15948.1. [Q8BKH7-1]
RefSeqNP_001277554.1. NM_001290625.1. [Q8BKH7-1]
NP_001277555.1. NM_001290626.1.
NP_796319.1. NM_177345.4. [Q8BKH7-1]
XP_006498036.1. XM_006497973.1. [Q8BKH7-1]
XP_006498038.1. XM_006497975.1. [Q8BKH7-1]
XP_006498039.1. XM_006497976.1. [Q8BKH7-1]
XP_006498041.1. XM_006497978.1. [Q8BKH7-2]
UniGeneMm.270866.
Mm.487284.

3D structure databases

ProteinModelPortalQ8BKH7.
SMRQ8BKH7. Positions 371-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-57240N.
IntActQ8BKH7. 7 interactions.

PTM databases

PhosphoSiteQ8BKH7.

Proteomic databases

PRIDEQ8BKH7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113124; ENSMUSP00000108749; ENSMUSG00000038696. [Q8BKH7-2]
ENSMUST00000113126; ENSMUSP00000108751; ENSMUSG00000038696. [Q8BKH7-1]
ENSMUST00000147337; ENSMUSP00000116494; ENSMUSG00000038696. [Q8BKH7-1]
GeneID227743.
KEGGmmu:227743.
UCSCuc008jil.1. mouse. [Q8BKH7-1]

Organism-specific databases

CTD79109.
MGIMGI:2444554. Mapkap1.

Phylogenomic databases

eggNOGNOG303753.
GeneTreeENSGT00390000000642.
HOVERGENHBG023148.
InParanoidQ8BKH7.
OMALCACDLV.
PhylomeDBQ8BKH7.
TreeFamTF315174.

Gene expression databases

ArrayExpressQ8BKH7.
BgeeQ8BKH7.
GenevestigatorQ8BKH7.

Family and domain databases

InterProIPR008828. SIN1.
[Graphical view]
PANTHERPTHR13335. PTHR13335. 1 hit.
PfamPF05422. SIN1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPKAP1. mouse.
NextBio378816.
PROQ8BKH7.
SOURCESearch...

Entry information

Entry nameSIN1_MOUSE
AccessionPrimary (citable) accession number: Q8BKH7
Secondary accession number(s): A2AN72 expand/collapse secondary AC list , A2AN74, A2AR13, A2AR16, Q80UY4, Q8BMV5, Q8R2N9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot