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P31748

- AKT_MLVAT

UniProt

P31748 - AKT_MLVAT

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Protein

AKT kinase-transforming protein

Gene

V-AKT

Organism
AKT8 murine leukemia virus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei200 – 2001ATPPROSITE-ProRule annotation
Active sitei295 – 2951Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1859ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
AKT kinase-transforming protein (EC:2.7.11.1)
Gene namesi
Name:V-AKT
OrganismiAKT8 murine leukemia virus
Taxonomic identifieri11790 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

Pathology & Biotechi

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501AKT kinase-transforming proteinPRO_0000085614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei347 – 3471PhosphotyrosineBy similarity

Post-translational modificationi

Autophosphorylated on threonine and serine residues.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with mouse THEM4.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP31748.
SMRiP31748. Positions 24-142, 165-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 129104PHPROSITE-ProRule annotationAdd
BLAST
Domaini171 – 429259Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini430 – 50172AGC-kinase C-terminalAdd
BLAST

Domaini

The AGC-kinase C-terminal mediates interaction with THEM4.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31748-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
AREETLIIIP GLPLSLGATD TMNDVAIVKE GWLHKRGEYI KTWRPRYFLL
60 70 80 90 100
KNDGTFIGYK ERPQDVDQRE SPLNNFSVAQ CQLMKTERPR PNTFIIRCLQ
110 120 130 140 150
WTTVIERTFH VETPEEREEW ATAIQTVADG LKRQEEETMD FRSGSPSDNS
160 170 180 190 200
GAEEMEVSLA KPKHRVTMNE FEYLKLLGKG TFGKVILVKE KATGRYYAMK
210 220 230 240 250
ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT HDRLCFVMEY
260 270 280 290 300
ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN
310 320 330 340 350
LMLDKDGHIK ITDFGLCKEG IKDGATMKTF CGTPEYLAPE VLEDNDYGRA
360 370 380 390 400
VDWWGLGVVM YEMMCGRLPF YNQDHEKLFE LILMEEIRFP RTLGPEAKSL
410 420 430 440 450
LSGLLKKDPT QRLGGGSEDA KEIMQHRFFA NIVWQDVYEK KLSPPFKPQV
460 470 480 490 500
TSETDTRYFD EEFTAQMITI TPPDQDDSME CVDSERRPHF PQFSYSASGT

A
Length:501
Mass (Da):57,870
Last modified:July 1, 1993 - v1
Checksum:i5AEFDE58CD42F773
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80675 Genomic DNA. Translation: AAA42545.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80675 Genomic DNA. Translation: AAA42545.1 .

3D structure databases

ProteinModelPortali P31748.
SMRi P31748. Positions 24-142, 165-498.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P31748.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region."
    Bellacosa A., Testa J.R., Staal S.P., Tsichlis P.N.
    Science 254:274-277(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."
    Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.
    Science 294:374-380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THEM4.

Entry informationi

Entry nameiAKT_MLVAT
AccessioniPrimary (citable) accession number: P31748
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is synthesized as a Gag-Akt polyprotein.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3