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Protein

Tyrosine-protein kinase

Gene

Abl1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.UniRule annotationSAAS annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • delta-catenin binding Source: RGD
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  • protein kinase activity Source: RGD
  • protein kinase binding Source: RGD

GO - Biological processi

  • actin filament polymerization Source: RGD
  • associative learning Source: RGD
  • cellular response to oxidative stress Source: RGD
  • cellular response to transforming growth factor beta stimulus Source: RGD
  • glomerular visceral epithelial cell apoptotic process Source: RGD
  • learning or memory Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of dendrite development Source: RGD
  • positive regulation of extracellular matrix organization Source: RGD
  • positive regulation of fibroblast proliferation Source: RGD
  • positive regulation of hydrogen peroxide-mediated programmed cell death Source: RGD
  • positive regulation of neuron apoptotic process Source: RGD
  • positive regulation of neuron death Source: RGD
  • positive regulation of vasoconstriction Source: RGD
  • protein autophosphorylation Source: RGD
  • response to drug Source: RGD
  • response to endoplasmic reticulum stress Source: RGD
  • response to epinephrine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinaseUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-375170. CDO in myogenesis.
R-RNO-428890. Role of Abl in Robo-Slit signaling.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5685938. HDR through Single Strand Annealing (SSA).
R-RNO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinaseUniRule annotation (EC:2.7.10.2UniRule annotation)
Gene namesi
Name:Abl1Imported
Synonyms:LOC100909750Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1584969. Abl1.
6502032. LOC100909750.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • endoplasmic reticulum Source: RGD
  • growth cone Source: RGD
  • mitochondrion Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: RGD
  • ruffle Source: RGD
  • synapse Source: RGD
Complete GO annotation...

PTM / Processingi

Proteomic databases

PaxDbiE9PT20.

Expressioni

Gene expression databases

GenevisibleiE9PT20. RN.

Interactioni

GO - Molecular functioni

  • delta-catenin binding Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044534.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 14061SH3InterPro annotationAdd
BLAST
Domaini146 – 23691SH2InterPro annotationAdd
BLAST
Domaini261 – 512252Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.UniRule annotationSAAS annotation
Contains 1 SH2 domain.UniRule annotation
Contains 1 SH3 domain.UniRule annotation
Contains 1 protein kinase domain.UniRule annotation

Keywords - Domaini

SH3 domainUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
InParanoidiE9PT20.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG7GTT2V.
TreeFamiTF105081.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033221. ABL1.
IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF88. PTHR24418:SF88. 1 hit.
PfamiPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PT20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQQPGKVLG DQRRPSLPAL HFIKGAGKRD SSRHGGPHCN VFVEHEALQR
60 70 80 90 100
PVASDFEPQG LSEAARWNSK ENLLAGPSEN DPNLFVALYD FVASGDNTLS
110 120 130 140 150
ITKGEKLRVL GYNHNGEWCE AQTKNGQGWV PSNYITPVNS LEKHSWYHGP
160 170 180 190 200
VSRNAAEYLL SSGINGSFLV RESESSPGQR SISLRYEGRV YHYRINTASD
210 220 230 240 250
GKLYVSSESR FNTLAELVHH HSTVADGLIT TLHYPAPKRN KPTIYGVSPN
260 270 280 290 300
YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE
310 320 330 340 350
EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN
360 370 380 390 400
RQEVSAVVLL YMATQISSAM EYLEKKNFIH RDLAARNCLV GENHLVKVAD
410 420 430 440 450
FGLSRLMTGD TYTAHAGAKF PIKWTAPESL AYNKFSIKSD VWAFGVLLWE
460 470 480 490 500
IATYGMSPYP GIDLSQVYEL LEKDYRMERP EGCPEKVYEL MRACWQWNPS
510 520 530 540 550
DRPSFAEIHQ AFETMFQESS ISDEVEKELG KRGMRGAAGS TLQAPELPTK
560 570 580 590 600
TRTCRKTAEQ KDAPDALELL HTKGLGESDA LDSEPAVSPL LPRKERGPPD
610 620 630 640 650
GSLNEDERLL PKDKKTNLFS ALIKKKKKMA PTPPKRSSSF REMDGQSERR
660 670 680 690 700
GASEDDGREI SNGPPALTSD AVEPTKSPKA SNGAGVPNGA FREPGNSGFR
710 720 730 740 750
SPHVWKKSST LTSSRLAAAE EESGLSSSKR FLRSCSASCM PHGVRDTEWR
760 770 780 790 800
SVTLPRDLPS AGKQFDSSTF GGHKSEKPAL PRKRTSESRS EQVAKSTATP
810 820 830 840 850
PPRLVKKTEE AAEDVFKDTE SSPGSSPPSL TPKLLRRQVP ASPSSGPSHK
860 870 880 890 900
DEATKGNASG MGTPATAEPA APSNKAGLSK ASSEEPRARR HKHSSESPGR
910 920 930 940 950
DKGRLSKLKP APPPPPSSTG KAGKPAQSPS QDVAGEAGGA TKTKCTSLSV
960 970 980 990 1000
DAVNSDPTKA GQPGEGLRKS VPPSVPKPQS ATKPPGTPTS PVSTPSTAPA
1010 1020 1030 1040 1050
PSPLAGDQQP SSAAFIPLIS TRVSLRKTRQ PPERIASGTI TKGVVLDSTE
1060 1070 1080 1090 1100
ALCLAISRNS EQMASHSAVL EAGKNLYTFC VSYVDSIQQM RNKFAFREAI
1110 1120 1130 1140
NKLESNLREL QICPATASSG PAATQDFSKL LSSVKEISDI VRR
Length:1,143
Mass (Da):124,636
Last modified:April 5, 2011 - v1
Checksum:i72B4114809329E09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07072853 Genomic DNA. No translation available.
RefSeqiNP_001094320.1. NM_001100850.1.
XP_008773541.1. XM_008775319.1.
UniGeneiRn.3105.

Genome annotation databases

EnsembliENSRNOT00000042495; ENSRNOP00000044534; ENSRNOG00000047356.
GeneIDi100909750.
311860.
KEGGirno:311860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07072853 Genomic DNA. No translation available.
RefSeqiNP_001094320.1. NM_001100850.1.
XP_008773541.1. XM_008775319.1.
UniGeneiRn.3105.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044534.

Proteomic databases

PaxDbiE9PT20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000042495; ENSRNOP00000044534; ENSRNOG00000047356.
GeneIDi100909750.
311860.
KEGGirno:311860.

Organism-specific databases

CTDi25.
RGDi1584969. Abl1.
6502032. LOC100909750.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
InParanoidiE9PT20.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG7GTT2V.
TreeFamiTF105081.

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-375170. CDO in myogenesis.
R-RNO-428890. Role of Abl in Robo-Slit signaling.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5685938. HDR through Single Strand Annealing (SSA).
R-RNO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Gene expression databases

GenevisibleiE9PT20. RN.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033221. ABL1.
IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF88. PTHR24418:SF88. 1 hit.
PfamiPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiE9PT20_RAT
AccessioniPrimary (citable) accession number: E9PT20
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: June 8, 2016
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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

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 one 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.