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Protein
Submitted name:

RAC-beta serine/threonine-protein kinase

Gene

AKT2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Submitted name:
RAC-beta serine/threonine-protein kinaseImported
Gene namesi
Name:AKT2Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:392. AKT2.

Expressioni

Gene expression databases

BgeeiC9JIF6.
ExpressionAtlasiC9JIF6. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000375892.

Structurei

3D structure databases

ProteinModelPortaliC9JIF6.
SMRiC9JIF6. Positions 1-67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00770000120449.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

C9JIF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP
60
PLNNFSVAEC QLMKTER
Length:67
Mass (Da):7,930
Last modified:November 3, 2009 - v1
Checksum:iD876277012D0B316
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei67 – 671Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC118344 Genomic DNA. No translation available.
KC877734 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000427375; ENSP00000403890; ENSG00000105221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC118344 Genomic DNA. No translation available.
KC877734 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliC9JIF6.
SMRiC9JIF6. Positions 1-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000375892.

Chemistry

BindingDBiC9JIF6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000427375; ENSP00000403890; ENSG00000105221.

Organism-specific databases

HGNCiHGNC:392. AKT2.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00770000120449.

Miscellaneous databases

ChiTaRSiAKT2. human.
NextBioi35486613.

Gene expression databases

BgeeiC9JIF6.
ExpressionAtlasiC9JIF6. baseline and differential.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  3. "Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiC9JIF6_HUMAN
AccessioniPrimary (citable) accession number: C9JIF6
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: June 24, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.