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P61982

- 1433G_MOUSE

UniProt

P61982 - 1433G_MOUSE

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Protein

14-3-3 protein gamma

Gene

Ywhag

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interaction with phosphoserine on interacting proteinBy similarity
Sitei132 – 1321Interaction with phosphoserine on interacting proteinBy similarity

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. insulin-like growth factor receptor binding Source: UniProtKB
  3. poly(A) RNA binding Source: Ensembl
  4. protein domain specific binding Source: MGI
  5. protein kinase C binding Source: UniProtKB

GO - Biological processi

  1. cellular response to insulin stimulus Source: Ensembl
  2. protein targeting Source: MGI
  3. regulation of neuron differentiation Source: UniProtKB
  4. regulation of synaptic plasticity Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein gamma
Cleaved into the following chain:
Gene namesi
Name:Ywhag
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:108109. Ywhag.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24724714-3-3 protein gammaPRO_0000367908Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 24724614-3-3 protein gamma, N-terminally processedPRO_0000058607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in 14-3-3 protein gamma, N-terminally processedBy similarity
Modified residuei145 – 1451PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated by various PKC isozymes.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61982.
PaxDbiP61982.
PRIDEiP61982.

2D gel databases

REPRODUCTION-2DPAGEP61982.
UCD-2DPAGEP61982.

PTM databases

PhosphoSiteiP61982.

Expressioni

Gene expression databases

BgeeiP61982.
ExpressionAtlasiP61982. baseline and differential.
GenevestigatoriP61982.

Interactioni

Subunit structurei

Homodimer. Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53. Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with GAB2. Interacts with PKA-phosphorylated AANAT and SIRT2 (By similarity). Interacts with SAMSN1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnma1Q084604EBI-359843,EBI-1633915
Lrrk2Q5S0067EBI-359843,EBI-2693710

Protein-protein interaction databases

BioGridi204620. 16 interactions.
IntActiP61982. 17 interactions.
MINTiMINT-1869483.

Structurei

3D structure databases

ProteinModelPortaliP61982.
SMRiP61982. Positions 1-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOVERGENiHBG050423.
InParanoidiP61982.
KOiK16198.
OMAiCSETQHE.
OrthoDBiEOG7HHWT3.
PhylomeDBiP61982.
TreeFamiTF102003.

Family and domain databases

Gene3Di1.20.190.20. 1 hit.
InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61982-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK
60 70 80 90 100
NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV
110 120 130 140 150
LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS
160 170 180 190 200
EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA
210 220 230 240
FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN
Length:247
Mass (Da):28,303
Last modified:January 23, 2007 - v2
Checksum:iB0D16C6DE1F4455D
GO

Sequence cautioni

The sequence BAE28625.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501S → F in AAC14345. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF058799 mRNA. Translation: AAC14345.1.
CT010208 mRNA. Translation: CAJ18416.1.
AK088847 mRNA. Translation: BAC40609.1.
AK148618 mRNA. Translation: BAE28625.1. Different initiation.
AK153307 mRNA. Translation: BAE31888.1.
AK164356 mRNA. Translation: BAE37756.1.
BC008129 mRNA. Translation: AAH08129.1.
CCDSiCCDS19748.1.
RefSeqiNP_061359.2. NM_018871.3.
UniGeneiMm.233813.

Genome annotation databases

EnsembliENSMUST00000055808; ENSMUSP00000051223; ENSMUSG00000051391.
GeneIDi22628.
KEGGimmu:22628.
UCSCiuc008zzf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF058799 mRNA. Translation: AAC14345.1 .
CT010208 mRNA. Translation: CAJ18416.1 .
AK088847 mRNA. Translation: BAC40609.1 .
AK148618 mRNA. Translation: BAE28625.1 . Different initiation.
AK153307 mRNA. Translation: BAE31888.1 .
AK164356 mRNA. Translation: BAE37756.1 .
BC008129 mRNA. Translation: AAH08129.1 .
CCDSi CCDS19748.1.
RefSeqi NP_061359.2. NM_018871.3.
UniGenei Mm.233813.

3D structure databases

ProteinModelPortali P61982.
SMRi P61982. Positions 1-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204620. 16 interactions.
IntActi P61982. 17 interactions.
MINTi MINT-1869483.

Chemistry

BindingDBi P61982.

PTM databases

PhosphoSitei P61982.

2D gel databases

REPRODUCTION-2DPAGE P61982.
UCD-2DPAGE P61982.

Proteomic databases

MaxQBi P61982.
PaxDbi P61982.
PRIDEi P61982.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055808 ; ENSMUSP00000051223 ; ENSMUSG00000051391 .
GeneIDi 22628.
KEGGi mmu:22628.
UCSCi uc008zzf.2. mouse.

Organism-specific databases

CTDi 7532.
MGIi MGI:108109. Ywhag.

Phylogenomic databases

eggNOGi COG5040.
GeneTreei ENSGT00760000119116.
HOVERGENi HBG050423.
InParanoidi P61982.
KOi K16198.
OMAi CSETQHE.
OrthoDBi EOG7HHWT3.
PhylomeDBi P61982.
TreeFami TF102003.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.

Miscellaneous databases

ChiTaRSi Ywhag. mouse.
NextBioi 302991.
PROi P61982.
SOURCEi Search...

Gene expression databases

Bgeei P61982.
ExpressionAtlasi P61982. baseline and differential.
Genevestigatori P61982.

Family and domain databases

Gene3Di 1.20.190.20. 1 hit.
InterProi IPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view ]
PANTHERi PTHR18860. PTHR18860. 1 hit.
Pfami PF00244. 14-3-3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000868. 14-3-3. 1 hit.
PRINTSi PR00305. 1433ZETA.
SMARTi SM00101. 14_3_3. 1 hit.
[Graphical view ]
SUPFAMi SSF48445. SSF48445. 1 hit.
PROSITEi PS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Karpitskiy V.V., Shaw A.S.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Kang S.U., Klug S., Friebe K., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-50; 43-56; 62-69; 78-83; 92-120 AND 133-247, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: INTERACTION WITH SAMSN1.

Entry informationi

Entry namei1433G_MOUSE
AccessioniPrimary (citable) accession number: P61982
Secondary accession number(s): O70457
, P35214, Q3UFD6, Q4FK44, Q9UDP2, Q9UN99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3