Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BPZ7

- SIN1_HUMAN

UniProt

Q9BPZ7 - SIN1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 kinase binding Source: ParkinsonsUK-UCL
  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
Complete GO annotation...

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_228016. VEGFR2 mediated vascular permeability.
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 vesicle Source: UniProtKB-KW
  2. cytosol Source: Reactome
  3. Golgi apparatus Source: UniProtKB
  4. nucleus Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9BPZ7.
ExpressionAtlasiQ9BPZ7. baseline and differential.
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. 22 interactions.
DIPiDIP-39480N.
IntActiQ9BPZ7. 17 interactions.
MINTiMINT-1454116.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000000642.
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

        10         20         30         40         50
MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS
60 70 80 90 100
GSEIQGSNGE TQGYVYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ
110 120 130 140 150
IKCKNIQWKE RNSKQSAQEL KSLFEKKSLK EKPPISGKQS ILSVRLEQCP
160 170 180 190 200
LQLNNPFNEY SKFDGKGHVG TTATKKIDVY LPLHSSQDRL LPMTVVTMAS
210 220 230 240 250
ARVQDLIGLI CWQYTSEGRE PKLNDNVSAY CLHIAEDDGE VDTDFPPLDS
260 270 280 290 300
NEPIHKFGFS TLALVEKYSS PGLTSKESLF VRINAAHGFS LIQVDNTKVT
310 320 330 340 350
MKEILLKAVK RRKGSQKVSG PQYRLEKQSE PNVAVDLDST LESQSAWEFC
360 370 380 390 400
LVRENSSRAD GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV
410 420 430 440 450
QLGISGDKVE IDPVTNQKAS TKFWIKQKPI SIDSDLLCAC DLAEEKSPSH
460 470 480 490 500
AIFKLTYLSN HDYKHLYFES DAATVNEIVL KVNYILESRA STARADYFAQ
510 520
KQRKLNRRTS FSFQKEKKSG QQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 22 interactions.
DIPi DIP-39480N.
IntActi Q9BPZ7. 17 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.
GeneTreei ENSGT00390000000642.
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_228016. VEGFR2 mediated vascular permeability.
REACT_75829. PIP3 activates AKT signaling.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9BPZ7.
ExpressionAtlasi Q9BPZ7. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 118 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