Q9BPZ7 (SIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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
Short name=mSIN1

Gene names

Name:	MAPKAP1
Synonyms:	MIP1, SIN1

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	522 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.2 Ref.10 Ref.12 Ref.13 Ref.14
Subunit structure	Interacts with IFNAR2 By similarity. All isoforms except isoform 4 can 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 SGK1 By similarity. Ref.2 Ref.10 Ref.11 Ref.12 Ref.14
Subcellular location	Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle. Nucleus Ref.12 Ref.14.
Tissue specificity	Ubiquitously expressed, with highest levels in heart and skeletal muscle. Ref.2
Sequence similarities	Belongs to the SIN1 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cell membrane Cytoplasmic vesicle Membrane Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Ras GTPase binding Non-traceable author statement Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BPZ7-1)

Also known as: beta; gamma;

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: Q9BPZ7-2)

Also known as: alpha; beta;

The sequence of this isoform differs from the canonical sequence as follows:
     321-356: Missing.

Isoform 3 (identifier: Q9BPZ7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     357-403: Missing.

Isoform 4 (identifier: Q9BPZ7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-192: Missing.

Note: Not involved in a TORC2 complex.

Isoform 5 (identifier: Q9BPZ7-5)

Also known as: alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     321-438: Missing.
     442-522: Missing.

Isoform 6 (identifier: Q9BPZ7-6)

Also known as: gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     357-372: SRADGVFEEDSQIDIA → TLAASLHARFVRCKLA
     373-522: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 522

521

Target of rapamycin complex 2 subunit MAPKAP1

PRO_0000218768

Regions

Region

2 – 184

183

Interaction with MAP3K2

Region

468 – 522

55

Interaction with ATF2

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Modified residue

510

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

1 – 192

192

Missing in isoform 4.

VSP_033202

Alternative sequence

321 – 438

118

Missing in isoform 5.

VSP_033203

Alternative sequence

321 – 356

36

Missing in isoform 2.

VSP_006098

Alternative sequence

357 – 403

47

Missing in isoform 3.

VSP_033204

Alternative sequence

357 – 372

16

SRADG…QIDIA → TLAASLHARFVRCKLA in isoform 6.

VSP_033205

Alternative sequence

373 – 522

150

Missing in isoform 6.

VSP_033206

Alternative sequence

442 – 522

81

Missing in isoform 5.

VSP_033207

Experimental info

Sequence conflict

76 – 86

11

WDFGIRRRSNT → ADPARSVEAAS in AAA36551. Ref.9

Sequence conflict

178

1

D → N in AAT46480. Ref.2

Sequence conflict

178

1

D → N in AAT46478. Ref.2

Sequence conflict

178

1

D → N in AAT46479. Ref.2

Sequence conflict

305

1

L → F in BAF82749. Ref.3

Sequence conflict

478

1

I → T in CAH56311. Ref.4

Sequence conflict

491

1

S → N in AAT46478. Ref.2

Sequence conflict

491

1

S → N in AAT46479. Ref.2

Sequence conflict

502

1

Q → K in AAA36551. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

522

Helix Strand Turn

Details...

Helix

372 – 378

7

Turn

379 – 381

3

Beta strand

384 – 392

9

Turn

393 – 395

3

Beta strand

396 – 404

9

Beta strand

406 – 413

8

Beta strand

430 – 433

4

Helix

434 – 436

3

Beta strand

437 – 445

9

Beta strand

447 – 449

3

Beta strand

451 – 459

9

Beta strand

462 – 470

9

Helix

472 – 487

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (beta) (gamma) [UniParc]. Last modified August 14, 2001. Version 2. Checksum: E3B808C6E58F7C48	FASTA	522	59,123
	10 20 30 40 50 60 MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE 70 80 90 100 110 120 TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL 130 140 150 160 170 180 KSLFEKKSLK EKPPISGKQS 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 RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC LVRENSSRAD 370 380 390 400 410 420 GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV QLGISGDKVE IDPVTNQKAS 430 440 450 460 470 480 TKFWIKQKPI SIDSDLLCAC DLAEEKSPSH AIFKLTYLSN HDYKHLYFES DAATVNEIVL 490 500 510 520 KVNYILESRA STARADYFAQ KQRKLNRRTS FSFQKEKKSG QQ
	Isoform 2 (alpha) (beta) [UniParc]. Checksum: C880D5047EEEC4A0	FASTA	486	54,971
	10 20 30 40 50 60 MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE 70 80 90 100 110 120 TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL 130 140 150 160 170 180 KSLFEKKSLK EKPPISGKQS 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 RRKGSQKVSG SRADGVFEED SQIDIATVQD MLSSHHYKSF KVSMIHRLRF 370 380 390 400 410 420 TTDVQLGISG DKVEIDPVTN QKASTKFWIK QKPISIDSDL LCACDLAEEK SPSHAIFKLT 430 440 450 460 470 480 YLSNHDYKHL YFESDAATVN EIVLKVNYIL ESRASTARAD YFAQKQRKLN RRTSFSFQKE KKSGQQ
	Isoform 3 [UniParc]. Checksum: AC1274FBE11ED04E	FASTA	475	53,744
	10 20 30 40 50 60 MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE 70 80 90 100 110 120 TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL 130 140 150 160 170 180 KSLFEKKSLK EKPPISGKQS 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 RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC LVRENSISGD 370 380 390 400 410 420 KVEIDPVTNQ KASTKFWIKQ KPISIDSDLL CACDLAEEKS PSHAIFKLTY LSNHDYKHLY 430 440 450 460 470 FESDAATVNE IVLKVNYILE SRASTARADY FAQKQRKLNR RTSFSFQKEK KSGQQ
	Isoform 4 [UniParc]. Checksum: E9ABF4B32E394142	FASTA	330	37,320
	10 20 30 40 50 60 MTVVTMASAR VQDLIGLICW QYTSEGREPK LNDNVSAYCL HIAEDDGEVD TDFPPLDSNE 70 80 90 100 110 120 PIHKFGFSTL ALVEKYSSPG LTSKESLFVR INAAHGFSLI QVDNTKVTMK EILLKAVKRR 130 140 150 160 170 180 KGSQKVSGPQ YRLEKQSEPN VAVDLDSTLE SQSAWEFCLV RENSSRADGV FEEDSQIDIA 190 200 210 220 230 240 TVQDMLSSHH YKSFKVSMIH RLRFTTDVQL GISGDKVEID PVTNQKASTK FWIKQKPISI 250 260 270 280 290 300 DSDLLCACDL AEEKSPSHAI FKLTYLSNHD YKHLYFESDA ATVNEIVLKV NYILESRAST 310 320 330 ARADYFAQKQ RKLNRRTSFS FQKEKKSGQQ
	Isoform 5 (alpha) [UniParc]. Checksum: FECEC53E16862340	FASTA	323	36,237
	10 20 30 40 50 60 MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE 70 80 90 100 110 120 TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL 130 140 150 160 170 180 KSLFEKKSLK EKPPISGKQS 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 MKEILLKAVK RRKGSQKVSG ACD
	Isoform 6 (gamma) [UniParc]. Checksum: 228CE1A0DB9E2CD8	FASTA	372	41,838
	10 20 30 40 50 60 MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE 70 80 90 100 110 120 TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL 130 140 150 160 170 180 KSLFEKKSLK EKPPISGKQS 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 RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC LVRENSTLAA 370 SLHARFVRCK LA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alternative polyadenylation and splicing of mRNAs transcribed from the human Sin1 gene." Schroder W., Cloonan N., Bushell G., Sculley T. Gene 339:17-23(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5).
[2]	"Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation." Cheng J., Zhang D., Kim K., Zhao Y., Zhao Y., Su B. Mol. Cell. Biol. 25:5955-5964(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 6), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH MAP3K2.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). Tissue: Corpus callosum and Substantia nigra.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Stomach.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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 2). Tissue: Lung.
[8]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-15 AND 257-267, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae." Colicelli J., Nicolette C., Birchmeier C., Rodgers L., Riggs M., Wigler M. Proc. Natl. Acad. Sci. U.S.A. 88:2913-2917(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-502 (ISOFORM 1). Tissue: Glial cell.
[10]	"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: IDENTIFICATION IN THE TORC2 COMPLEX, FUNCTION, MASS SPECTROMETRY.
[11]	"mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s." Frias M.A., Thoreen C.C., Jaffe J.D., Schroder W., Sculley T., Carr S.A., Sabatini D.M. Curr. Biol. 16:1865-1870(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TORC2 COMPLEX.
[12]	"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: INTERACTION WITH ATF2 AND MAPK8, FUNCTION, SUBCELLULAR LOCATION.
[13]	"Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity." Yang Q., Inoki K., Ikenoue T., Guan K.-L. Genes Dev. 20:2820-2832(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling." Schroder W.A., Buck M., Cloonan N., Hancock J.F., Suhrbier A., Sculley T., Bushell G. Cell. Signal. 19:1279-1289(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRAS AND KRAS, FUNCTION, SUBCELLULAR LOCATION.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY524429 mRNA. Translation: AAS90839.1.
AY524430 mRNA. Translation: AAS90840.1.
AY524431 mRNA. Translation: AAS90841.1.
AY524432 mRNA. Translation: AAS90842.1.
AY633624 mRNA. Translation: AAT46478.1.
AY633625 mRNA. Translation: AAT46479.1.
AY633626 mRNA. Translation: AAT46480.1.
AK290060 mRNA. Translation: BAF82749.1.
AK295364 mRNA. Translation: BAH12045.1.
AK316149 mRNA. Translation: BAH14520.1.
AL833042 mRNA. Translation: CAH56311.1.
AL162584, AL359632 Genomic DNA. Translation: CAI39500.1.
AL162584, AL359632 Genomic DNA. Translation: CAI39506.1.
AL162584, AL359632 Genomic DNA. Translation: CAI39507.1.
AL359632, AL162584 Genomic DNA. Translation: CAI39888.1.
AL359632, AL162584 Genomic DNA. Translation: CAI39891.1.
AL359632, AL162584 Genomic DNA. Translation: CAI39892.1.
CH471090 Genomic DNA. Translation: EAW87630.1.
CH471090 Genomic DNA. Translation: EAW87631.1.
CH471090 Genomic DNA. Translation: EAW87632.1.
BC003044 mRNA. Translation: AAH03044.1.
BC002326 mRNA. Translation: AAH02326.1.
M37191 mRNA. Translation: AAA36551.1.

IPI

IPI00028195.
IPI00216277.
IPI00549186.
IPI00549688.
IPI00550208.
IPI00890691.

PIR

C38637.

RefSeq

NP_001006618.1. NM_001006617.1.
NP_001006619.1. NM_001006618.1.
NP_001006620.1. NM_001006619.1.
NP_001006621.1. NM_001006620.1.
NP_001006622.1. NM_001006621.1.
NP_077022.1. NM_024117.3.

UniGene

Hs.495138.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3VOQ	X-ray	2.00	A/B	372-493	[»]

ProteinModelPortal

Q9BPZ7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BPZ7. 13 interactions.

MINT

MINT-1454116.

PTM databases

PhosphoSite

Q9BPZ7.

Polymorphism databases

DMDM

15214282.

Proteomic databases

PaxDb

Q9BPZ7.

PRIDE

Q9BPZ7.

Protocols and materials databases

DNASU

79109.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265960; ENSP00000265960; ENSG00000119487.
ENST00000350766; ENSP00000265961; ENSG00000119487.
ENST00000373498; ENSP00000362597; ENSG00000119487.
ENST00000373503; ENSP00000362602; ENSG00000119487.
ENST00000373511; ENSP00000362610; ENSG00000119487.
ENST00000394060; ENSP00000377624; ENSG00000119487.
ENST00000394063; ENSP00000377627; ENSG00000119487.

GeneID

79109.

KEGG

hsa:79109.

UCSC

uc004bpv.3. human.
uc004bpy.3. human.
uc004bpz.3. human.
uc004bqa.3. human.

Organism-specific databases

CTD

79109.

GeneCards

GC09M128199.

HGNC

HGNC:18752. MAPKAP1.

HPA

HPA029091.
HPA029092.

MIM

610558. gene.

neXtProt

NX_Q9BPZ7.

PharmGKB

PA38674.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG303753.

HOVERGEN

HBG023148.

InParanoid

Q9BPZ7.

OMA

CACDLVE.

OrthoDB

EOG4GXFMK.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9BPZ7.

Bgee

Q9BPZ7.

Genevestigator

Q9BPZ7.

GermOnline

ENSG00000119487. Homo sapiens.

Family and domain databases

InterPro

IPR008828. SIN1.
[Graphical view]

PANTHER

PTHR13335. PTHR13335. 1 hit.

Pfam

PF05422. SIN1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

79109.

NextBio

67979.

SOURCE

Search...

Entry information

Entry name

SIN1_HUMAN

Accession

Primary (citable) accession number: Q9BPZ7
Secondary accession number(s): A8K1Z5 , B1AMA4, B7Z309, Q00426, Q5JSV5, Q5JSV6, Q5JSV9, Q658R0, Q699U1, Q699U2, Q699U3, Q699U4, Q6GVJ0, Q6GVJ1, Q6GVJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 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.