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Q9BPZ7 (SIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·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
Short name=mSIN1
Gene names
Name:MAPKAP1
Synonyms:MIP1, SIN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. Ref.2 Ref.10 Ref.12 Ref.13 Ref.14 Ref.17

Subunit structure

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 IFNAR2 and SGK1. Isoform 2 interacts with NBN. Isoform 1 interacts with CCDC28B. Ref.2 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17

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 processStress response
   Cellular componentCell membrane
Cytoplasmic vesicle
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

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

innate immune response

Traceable author statement. Source: Reactome

negative regulation of Ras protein signal transduction

Inferred from mutant phenotype Ref.14. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.14. Source: UniProtKB

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 direct assay Ref.14. Source: UniProtKB

   Molecular_functionRas GTPase binding

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidic acid binding

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidylinositol-3,5-bisphosphate binding

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.14. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 522521Target of rapamycin complex 2 subunit MAPKAP1
PRO_0000218768

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue5101Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 192192Missing in isoform 4.
VSP_033202
Alternative sequence321 – 438118Missing in isoform 5.
VSP_033203
Alternative sequence321 – 35636Missing in isoform 2.
VSP_006098
Alternative sequence357 – 40347Missing in isoform 3.
VSP_033204
Alternative sequence357 – 37216SRADG…QIDIA → TLAASLHARFVRCKLA in isoform 6.
VSP_033205
Alternative sequence373 – 522150Missing in isoform 6.
VSP_033206
Alternative sequence442 – 52281Missing in isoform 5.
VSP_033207

Experimental info

Sequence conflict76 – 8611WDFGIRRRSNT → ADPARSVEAAS in AAA36551. Ref.9
Sequence conflict1781D → N in AAT46480. Ref.2
Sequence conflict1781D → N in AAT46478. Ref.2
Sequence conflict1781D → N in AAT46479. Ref.2
Sequence conflict3051L → F in BAF82749. Ref.3
Sequence conflict4781I → T in CAH56311. Ref.4
Sequence conflict4911S → N in AAT46478. Ref.2
Sequence conflict4911S → N in AAT46479. Ref.2
Sequence conflict5021Q → K in AAA36551. Ref.9

Secondary structure

...................... 522
Helix Strand Turn

Details...

Sequences

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

Last modified August 14, 2001. Version 2.
Checksum: E3B808C6E58F7C48

FASTA52259,123
        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 

« Hide

Isoform 2 (alpha) (beta) [UniParc].

Checksum: C880D5047EEEC4A0
Show »

FASTA48654,971
Isoform 3 [UniParc].

Checksum: AC1274FBE11ED04E
Show »

FASTA47553,744
Isoform 4 [UniParc].

Checksum: E9ABF4B32E394142
Show »

FASTA33037,320
Isoform 5 (alpha) [UniParc].

Checksum: FECEC53E16862340
Show »

FASTA32336,237
Isoform 6 (gamma) [UniParc].

Checksum: 228CE1A0DB9E2CD8
Show »

FASTA37241,838

References

« Hide '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. 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 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific domains."
Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.
PLoS ONE 8:E65586-E65586(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NBN.
[17]"The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2 function and interacts with SIN1 to control cilia length independently of the mTOR complex."
Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N., Beales P.L., Badano J.L.
Hum. Mol. Genet. 22:4031-4042(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CILIOGENESIS, INTERACTION WITH CCDC28B.
+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.
PIRC38637.
RefSeqNP_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.
UniGeneHs.495138.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VOQX-ray2.00A/B372-493[»]
ProteinModelPortalQ9BPZ7.
SMRQ9BPZ7. Positions 371-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122551. 19 interactions.
IntActQ9BPZ7. 18 interactions.
MINTMINT-1454116.

PTM databases

PhosphoSiteQ9BPZ7.

Polymorphism databases

DMDM15214282.

Proteomic databases

PaxDbQ9BPZ7.
PRIDEQ9BPZ7.

Protocols and materials databases

DNASU79109.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265960; ENSP00000265960; ENSG00000119487. [Q9BPZ7-1]
ENST00000350766; ENSP00000265961; ENSG00000119487. [Q9BPZ7-2]
ENST00000373498; ENSP00000362597; ENSG00000119487. [Q9BPZ7-1]
ENST00000373503; ENSP00000362602; ENSG00000119487. [Q9BPZ7-4]
ENST00000373511; ENSP00000362610; ENSG00000119487. [Q9BPZ7-3]
ENST00000394060; ENSP00000377624; ENSG00000119487. [Q9BPZ7-5]
ENST00000394063; ENSP00000377627; ENSG00000119487. [Q9BPZ7-4]
GeneID79109.
KEGGhsa:79109.
UCSCuc004bpv.3. human. [Q9BPZ7-1]
uc004bpy.3. human. [Q9BPZ7-2]
uc004bpz.3. human. [Q9BPZ7-3]
uc004bqa.3. human. [Q9BPZ7-5]

Organism-specific databases

CTD79109.
GeneCardsGC09M128199.
HGNCHGNC:18752. MAPKAP1.
HPAHPA029091.
HPA029092.
MIM610558. gene.
neXtProtNX_Q9BPZ7.
PharmGKBPA38674.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303753.
HOVERGENHBG023148.
InParanoidQ9BPZ7.
OMALCACDLV.
OrthoDBEOG7GXPBF.
PhylomeDBQ9BPZ7.
TreeFamTF315174.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9BPZ7.
BgeeQ9BPZ7.
GenevestigatorQ9BPZ7.

Family and domain databases

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

Other

GeneWikiMAPKAP1.
GenomeRNAi79109.
NextBio67979.
PROQ9BPZ7.
SOURCESearch...

Entry information

Entry nameSIN1_HUMAN
AccessionPrimary (citable) accession number: Q9BPZ7
Secondary accession number(s): A8K1Z5 expand/collapse secondary AC list , 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: April 16, 2014
This is version 111 of the entry and version 2 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 9

Human chromosome 9: entries, gene names and cross-references to MIM