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Q9BPZ7

- SIN1_HUMAN

UniProt

Q9BPZ7 - SIN1_HUMAN

Protein

Target of rapamycin complex 2 subunit MAPKAP1

Gene

MAPKAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    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.6 Publications

    GO - Molecular functioni

    1. phosphatidic acid binding Source: UniProtKB
    2. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    3. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
    4. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
    5. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. Ras GTPase binding Source: UniProtKB

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. negative regulation of Ras protein signal transduction Source: UniProtKB
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. phosphatidylinositol-mediated signaling Source: Reactome
    8. substantia nigra development Source: UniProt
    9. T cell costimulation Source: Reactome

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_75829. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:MAPKAP1
    Synonyms:MIP1, SIN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:18752. MAPKAP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. Golgi apparatus Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38674.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 522521Target of rapamycin complex 2 subunit MAPKAP1PRO_0000218768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei510 – 5101Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BPZ7.
    PaxDbiQ9BPZ7.
    PRIDEiQ9BPZ7.

    PTM databases

    PhosphoSiteiQ9BPZ7.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9BPZ7.
    BgeeiQ9BPZ7.
    GenevestigatoriQ9BPZ7.

    Organism-specific databases

    HPAiHPA029091.
    HPA029092.

    Interactioni

    Subunit structurei

    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.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKDCP785272EBI-749938,EBI-352053

    Protein-protein interaction databases

    BioGridi122551. 19 interactions.
    DIPiDIP-39480N.
    IntActiQ9BPZ7. 18 interactions.
    MINTiMINT-1454116.

    Structurei

    Secondary structure

    1
    522
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi372 – 3787
    Turni379 – 3813
    Beta strandi384 – 3929
    Turni393 – 3953
    Beta strandi396 – 4049
    Beta strandi406 – 4138
    Beta strandi430 – 4334
    Helixi434 – 4363
    Beta strandi437 – 4459
    Beta strandi447 – 4493
    Beta strandi451 – 4599
    Beta strandi462 – 4709
    Helixi472 – 48716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VOQX-ray2.00A/B372-493[»]
    ProteinModelPortaliQ9BPZ7.
    SMRiQ9BPZ7. Positions 371-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 267266Interaction with NBNAdd
    BLAST
    Regioni2 – 184183Interaction with MAP3K2Add
    BLAST
    Regioni468 – 52255Interaction with ATF2Add
    BLAST

    Sequence similaritiesi

    Belongs to the SIN1 family.Curated

    Phylogenomic databases

    eggNOGiNOG303753.
    HOVERGENiHBG023148.
    InParanoidiQ9BPZ7.
    OMAiLCACDLV.
    OrthoDBiEOG7GXPBF.
    PhylomeDBiQ9BPZ7.
    TreeFamiTF315174.

    Family and domain databases

    InterProiIPR008828. SIN1.
    [Graphical view]
    PANTHERiPTHR13335. PTHR13335. 1 hit.
    PfamiPF05422. SIN1. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BPZ7-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS    50
    GSEIQGSNGE TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ 100
    IKCKNIQWKE RNSKQSAQEL KSLFEKKSLK EKPPISGKQS ILSVRLEQCP 150
    LQLNNPFNEY SKFDGKGHVG TTATKKIDVY LPLHSSQDRL LPMTVVTMAS 200
    ARVQDLIGLI CWQYTSEGRE PKLNDNVSAY CLHIAEDDGE VDTDFPPLDS 250
    NEPIHKFGFS TLALVEKYSS PGLTSKESLF VRINAAHGFS LIQVDNTKVT 300
    MKEILLKAVK RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC 350
    LVRENSSRAD GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV 400
    QLGISGDKVE IDPVTNQKAS TKFWIKQKPI SIDSDLLCAC DLAEEKSPSH 450
    AIFKLTYLSN HDYKHLYFES DAATVNEIVL KVNYILESRA STARADYFAQ 500
    KQRKLNRRTS FSFQKEKKSG QQ 522
    Length:522
    Mass (Da):59,123
    Last modified:August 14, 2001 - v2
    Checksum:iE3B808C6E58F7C48
    GO
    Isoform 2 (identifier: Q9BPZ7-2) [UniParc]FASTAAdd to Basket

    Also known as: alpha, beta

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

    Show »
    Length:486
    Mass (Da):54,971
    Checksum:iC880D5047EEEC4A0
    GO
    Isoform 3 (identifier: Q9BPZ7-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:475
    Mass (Da):53,744
    Checksum:iAC1274FBE11ED04E
    GO
    Isoform 4 (identifier: Q9BPZ7-4) [UniParc]FASTAAdd to Basket

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

    Note: Not involved in a TORC2 complex.

    Show »
    Length:330
    Mass (Da):37,320
    Checksum:iE9ABF4B32E394142
    GO
    Isoform 5 (identifier: Q9BPZ7-5) [UniParc]FASTAAdd to Basket

    Also known as: alpha

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

    Show »
    Length:323
    Mass (Da):36,237
    Checksum:iFECEC53E16862340
    GO
    Isoform 6 (identifier: Q9BPZ7-6) [UniParc]FASTAAdd to Basket

    Also known as: gamma

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

    Show »
    Length:372
    Mass (Da):41,838
    Checksum:i228CE1A0DB9E2CD8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 8611WDFGIRRRSNT → ADPARSVEAAS in AAA36551. (PubMed:1849280)CuratedAdd
    BLAST
    Sequence conflicti178 – 1781D → N in AAT46480. (PubMed:15988011)Curated
    Sequence conflicti178 – 1781D → N in AAT46478. (PubMed:15988011)Curated
    Sequence conflicti178 – 1781D → N in AAT46479. (PubMed:15988011)Curated
    Sequence conflicti305 – 3051L → F in BAF82749. (PubMed:14702039)Curated
    Sequence conflicti478 – 4781I → T in CAH56311. (PubMed:17974005)Curated
    Sequence conflicti491 – 4911S → N in AAT46478. (PubMed:15988011)Curated
    Sequence conflicti491 – 4911S → N in AAT46479. (PubMed:15988011)Curated
    Sequence conflicti502 – 5021Q → K in AAA36551. (PubMed:1849280)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 192192Missing in isoform 4. 2 PublicationsVSP_033202Add
    BLAST
    Alternative sequencei321 – 438118Missing in isoform 5. 1 PublicationVSP_033203Add
    BLAST
    Alternative sequencei321 – 35636Missing in isoform 2. 4 PublicationsVSP_006098Add
    BLAST
    Alternative sequencei357 – 40347Missing in isoform 3. 1 PublicationVSP_033204Add
    BLAST
    Alternative sequencei357 – 37216SRADG…QIDIA → TLAASLHARFVRCKLA in isoform 6. 1 PublicationVSP_033205Add
    BLAST
    Alternative sequencei373 – 522150Missing in isoform 6. 1 PublicationVSP_033206Add
    BLAST
    Alternative sequencei442 – 52281Missing in isoform 5. 1 PublicationVSP_033207Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS35139.1. [Q9BPZ7-3]
    CCDS35140.1. [Q9BPZ7-1]
    CCDS35141.1. [Q9BPZ7-4]
    CCDS48020.1. [Q9BPZ7-5]
    CCDS6864.1. [Q9BPZ7-2]
    PIRiC38637.
    RefSeqiNP_001006618.1. NM_001006617.1. [Q9BPZ7-1]
    NP_001006619.1. NM_001006618.1. [Q9BPZ7-5]
    NP_001006620.1. NM_001006619.1. [Q9BPZ7-3]
    NP_001006621.1. NM_001006620.1. [Q9BPZ7-4]
    NP_001006622.1. NM_001006621.1. [Q9BPZ7-4]
    NP_077022.1. NM_024117.3. [Q9BPZ7-2]
    UniGeneiHs.495138.

    Genome annotation databases

    EnsembliENST00000265960; 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]
    GeneIDi79109.
    KEGGihsa:79109.
    UCSCiuc004bpv.3. human. [Q9BPZ7-1]
    uc004bpy.3. human. [Q9BPZ7-2]
    uc004bpz.3. human. [Q9BPZ7-3]
    uc004bqa.3. human. [Q9BPZ7-5]

    Polymorphism databases

    DMDMi15214282.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS35139.1. [Q9BPZ7-3 ]
    CCDS35140.1. [Q9BPZ7-1 ]
    CCDS35141.1. [Q9BPZ7-4 ]
    CCDS48020.1. [Q9BPZ7-5 ]
    CCDS6864.1. [Q9BPZ7-2 ]
    PIRi C38637.
    RefSeqi NP_001006618.1. NM_001006617.1. [Q9BPZ7-1 ]
    NP_001006619.1. NM_001006618.1. [Q9BPZ7-5 ]
    NP_001006620.1. NM_001006619.1. [Q9BPZ7-3 ]
    NP_001006621.1. NM_001006620.1. [Q9BPZ7-4 ]
    NP_001006622.1. NM_001006621.1. [Q9BPZ7-4 ]
    NP_077022.1. NM_024117.3. [Q9BPZ7-2 ]
    UniGenei Hs.495138.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VOQ X-ray 2.00 A/B 372-493 [» ]
    ProteinModelPortali Q9BPZ7.
    SMRi Q9BPZ7. Positions 371-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122551. 19 interactions.
    DIPi DIP-39480N.
    IntActi Q9BPZ7. 18 interactions.
    MINTi MINT-1454116.

    PTM databases

    PhosphoSitei Q9BPZ7.

    Polymorphism databases

    DMDMi 15214282.

    Proteomic databases

    MaxQBi Q9BPZ7.
    PaxDbi Q9BPZ7.
    PRIDEi Q9BPZ7.

    Protocols and materials databases

    DNASUi 79109.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265960 ; 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 ]
    GeneIDi 79109.
    KEGGi hsa:79109.
    UCSCi uc004bpv.3. human. [Q9BPZ7-1 ]
    uc004bpy.3. human. [Q9BPZ7-2 ]
    uc004bpz.3. human. [Q9BPZ7-3 ]
    uc004bqa.3. human. [Q9BPZ7-5 ]

    Organism-specific databases

    CTDi 79109.
    GeneCardsi GC09M128199.
    HGNCi HGNC:18752. MAPKAP1.
    HPAi HPA029091.
    HPA029092.
    MIMi 610558. gene.
    neXtProti NX_Q9BPZ7.
    PharmGKBi PA38674.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303753.
    HOVERGENi HBG023148.
    InParanoidi Q9BPZ7.
    OMAi LCACDLV.
    OrthoDBi EOG7GXPBF.
    PhylomeDBi Q9BPZ7.
    TreeFami TF315174.

    Enzyme and pathway databases

    Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_75829. PIP3 activates AKT signaling.

    Miscellaneous databases

    GeneWikii MAPKAP1.
    GenomeRNAii 79109.
    NextBioi 67979.
    PROi Q9BPZ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BPZ7.
    Bgeei Q9BPZ7.
    Genevestigatori Q9BPZ7.

    Family and domain databases

    InterProi IPR008828. SIN1.
    [Graphical view ]
    PANTHERi PTHR13335. PTHR13335. 1 hit.
    Pfami PF05422. SIN1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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.

    Entry informationi

    Entry nameiSIN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BPZ7
    Secondary accession number(s): A8K1Z5
    , B1AMA4, B7Z309, Q00426, Q5JSV5, Q5JSV6, Q5JSV9, Q658R0, Q699U1, Q699U2, Q699U3, Q699U4, Q6GVJ0, Q6GVJ1, Q6GVJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3