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P61981

- 1433G_HUMAN

UniProt

P61981 - 1433G_HUMAN

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Protein

14-3-3 protein gamma

Gene

YWHAG

Organism
Homo sapiens (Human)
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.1 Publication

Sites

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

GO - Molecular functioni

  1. insulin-like growth factor receptor binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. protein kinase C binding Source: UniProtKB
  4. protein kinase C inhibitor activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cellular response to insulin stimulus Source: Ensembl
  3. G2/M transition of mitotic cell cycle Source: Reactome
  4. intrinsic apoptotic signaling pathway Source: Reactome
  5. membrane organization Source: Reactome
  6. mitotic cell cycle Source: Reactome
  7. negative regulation of protein kinase activity Source: UniProtKB
  8. negative regulation of protein serine/threonine kinase activity Source: GOC
  9. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  10. protein targeting Source: Ensembl
  11. regulation of neuron differentiation Source: UniProtKB
  12. regulation of signal transduction Source: UniProtKB
  13. regulation of synaptic plasticity Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
SignaLinkiP61981.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein gamma
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name:
KCIP-1
Cleaved into the following chain:
Gene namesi
Name:YWHAG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:12852. YWHAG.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24724714-3-3 protein gammaPRO_0000367907Add
BLAST
Initiator methioninei1 – 11Removed; alternate5 Publications
Chaini2 – 24724614-3-3 protein gamma, N-terminally processedPRO_0000058606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial1 Publication
Modified residuei2 – 21N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed; partial4 Publications
Modified residuei2 – 21N-acetylvaline; partial4 Publications
Modified residuei145 – 1451Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by various PKC isozymes.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61981.
PaxDbiP61981.
PeptideAtlasiP61981.
PRIDEiP61981.

2D gel databases

REPRODUCTION-2DPAGEIPI00220642.

PTM databases

PhosphoSiteiP61981.

Expressioni

Tissue specificityi

Highly expressed in brain, skeletal muscle, and heart.1 Publication

Gene expression databases

BgeeiP61981.
CleanExiHS_YWHAG.
ExpressionAtlasiP61981. baseline and differential.
GenevestigatoriP61981.

Organism-specific databases

HPAiCAB013274.
CAB018389.
HPA026918.

Interactioni

Subunit structurei

Homodimer. Interacts with SAMSN1 (By similarity). Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with GAB2. Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53. Interacts with PKA-phosphorylated AANAT and SIRT2.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK1O147577EBI-359832,EBI-974488
CSNK1A1P678283EBI-359832,EBI-7540603From a different organism.
HDAC4P565243EBI-359832,EBI-308629
KANK1Q14678-23EBI-359832,EBI-6173812
LRRK2Q5S0074EBI-359832,EBI-5323863
MARK2Q7KZI72EBI-359832,EBI-516560
MARK3P274482EBI-359832,EBI-707595
MDM4O151517EBI-359832,EBI-398437
Rnd3P615882EBI-359832,EBI-6930266From a different organism.
TP53P046375EBI-359832,EBI-366083
YWHAEP622584EBI-359832,EBI-356498

Protein-protein interaction databases

BioGridi113364. 256 interactions.
IntActiP61981. 103 interactions.
MINTiMINT-248956.
STRINGi9606.ENSP00000306330.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Helixi20 – 3112Combined sources
Helixi39 – 7032Combined sources
Helixi79 – 10628Combined sources
Helixi108 – 1114Combined sources
Helixi117 – 13721Combined sources
Helixi140 – 16425Combined sources
Helixi170 – 18516Combined sources
Helixi190 – 20617Combined sources
Helixi207 – 2104Combined sources
Turni213 – 2153Combined sources
Helixi216 – 23318Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B05X-ray2.55A/B/C/D/E/F2-247[»]
3UZDX-ray1.86A1-247[»]
4E2EX-ray2.25A1-247[»]
4J6SX-ray3.08A/B/C/D1-247[»]
4O46X-ray2.90A/B/C/D/E/F1-247[»]
ProteinModelPortaliP61981.
SMRiP61981. Positions 1-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61981.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP61981.
KOiK16198.
OMAiCSETQHE.
OrthoDBiEOG7HHWT3.
PhylomeDBiP61981.
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.

P61981-1 [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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41R → P in AAD48408. (PubMed:10433554)Curated
Sequence conflicti19 – 191R → G in AAD48408. (PubMed:10433554)Curated
Sequence conflicti78 – 781Missing in AAD48408. (PubMed:10433554)Curated
Sequence conflicti89 – 891I → V in AAD48408. (PubMed:10433554)Curated
Sequence conflicti104 – 1041L → V in AAD48408. (PubMed:10433554)Curated
Sequence conflicti109 – 1091I → Y in AAD48408. (PubMed:10433554)Curated
Sequence conflicti119 – 1224SKVF → RKDL in AAD48408. (PubMed:10433554)Curated
Sequence conflicti144 – 1452AT → GD in AAD48408. (PubMed:10433554)Curated
Sequence conflicti157 – 1582AH → R in AAD48408. (PubMed:10433554)Curated
Sequence conflicti200 – 2023AFD → EFE in AAD48408. (PubMed:10433554)Curated
Sequence conflicti214 – 2141D → E in AAD48408. (PubMed:10433554)Curated
Sequence conflicti240 – 2401D → DH in AAD48408. (PubMed:10433554)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142498 mRNA. Translation: AAD48408.1.
AB024334 mRNA. Translation: BAA85184.1.
CR541904 mRNA. Translation: CAG46702.1.
CR541925 mRNA. Translation: CAG46723.1.
AC006388 Genomic DNA. No translation available.
BC020963 mRNA. Translation: AAH20963.1.
CCDSiCCDS5584.1.
RefSeqiNP_036611.2. NM_012479.3.
UniGeneiHs.744840.

Genome annotation databases

EnsembliENST00000307630; ENSP00000306330; ENSG00000170027.
GeneIDi7532.
KEGGihsa:7532.
UCSCiuc011kgj.1. human.

Polymorphism databases

DMDMi48428721.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142498 mRNA. Translation: AAD48408.1 .
AB024334 mRNA. Translation: BAA85184.1 .
CR541904 mRNA. Translation: CAG46702.1 .
CR541925 mRNA. Translation: CAG46723.1 .
AC006388 Genomic DNA. No translation available.
BC020963 mRNA. Translation: AAH20963.1 .
CCDSi CCDS5584.1.
RefSeqi NP_036611.2. NM_012479.3.
UniGenei Hs.744840.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B05 X-ray 2.55 A/B/C/D/E/F 2-247 [» ]
3UZD X-ray 1.86 A 1-247 [» ]
4E2E X-ray 2.25 A 1-247 [» ]
4J6S X-ray 3.08 A/B/C/D 1-247 [» ]
4O46 X-ray 2.90 A/B/C/D/E/F 1-247 [» ]
ProteinModelPortali P61981.
SMRi P61981. Positions 1-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113364. 256 interactions.
IntActi P61981. 103 interactions.
MINTi MINT-248956.
STRINGi 9606.ENSP00000306330.

Chemistry

BindingDBi P61981.
ChEMBLi CHEMBL1293296.

PTM databases

PhosphoSitei P61981.

Polymorphism databases

DMDMi 48428721.

2D gel databases

REPRODUCTION-2DPAGE IPI00220642.

Proteomic databases

MaxQBi P61981.
PaxDbi P61981.
PeptideAtlasi P61981.
PRIDEi P61981.

Protocols and materials databases

DNASUi 7532.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307630 ; ENSP00000306330 ; ENSG00000170027 .
GeneIDi 7532.
KEGGi hsa:7532.
UCSCi uc011kgj.1. human.

Organism-specific databases

CTDi 7532.
GeneCardsi GC07M075956.
HGNCi HGNC:12852. YWHAG.
HPAi CAB013274.
CAB018389.
HPA026918.
MIMi 605356. gene.
neXtProti NX_P61981.
PharmGKBi PA37441.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5040.
GeneTreei ENSGT00760000119116.
HOGENOMi HOG000240379.
HOVERGENi HBG050423.
InParanoidi P61981.
KOi K16198.
OMAi CSETQHE.
OrthoDBi EOG7HHWT3.
PhylomeDBi P61981.
TreeFami TF102003.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
SignaLinki P61981.

Miscellaneous databases

ChiTaRSi YWHAG. human.
EvolutionaryTracei P61981.
GeneWikii YWHAG.
GenomeRNAii 7532.
NextBioi 29467.
PROi P61981.
SOURCEi Search...

Gene expression databases

Bgeei P61981.
CleanExi HS_YWHAG.
ExpressionAtlasi P61981. baseline and differential.
Genevestigatori P61981.

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. "14-3-3gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells."
    Autieri M.V., Carbone C.J.
    DNA Cell Biol. 18:555-564(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, INTERACTION WITH RAF1.
    Tissue: Vascular smooth muscle.
  2. "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma gene (YWHAG) to 7q11.23."
    Horie M., Suzuki M., Takahashi E., Tanigami A.
    Genomics 60:241-243(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Endometrial tumor.
  6. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, PHOSPHORYLATION AT THR-145, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Hepatoma.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Platelet.
  8. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis."
    Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AANAT.
  11. Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
    Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.
    Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRTC2.
  13. "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."
    Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.
    J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSH1.
  14. "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage."
    Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.
    Nat. Cell Biol. 7:278-285(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation."
    Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.
    EMBO J. 25:1207-1218(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TP53 ACTIVATION, INTERACTION WITH MDM4.
  16. "Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53."
    Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y., Lee K.Y.
    Biochem. Biophys. Res. Commun. 368:690-695(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRT2.
  17. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
    Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
    EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAB2.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

Entry informationi

Entry namei1433G_HUMAN
AccessioniPrimary (citable) accession number: P61981
Secondary accession number(s): O70457
, P35214, Q6FH52, Q9UDP2, Q9UN99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 125 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 7
    Human chromosome 7: 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