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Protein

Receptor tyrosine-protein kinase erbB-2

Gene

Erbb2

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

Functioni

Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner (By similarity).By similarity
In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei755ATPPROSITE-ProRule annotation1
Active sitei847Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi728 – 736ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • glycoprotein binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein tyrosine kinase activity Source: RGD
  • receptor signaling protein tyrosine kinase activity Source: InterPro
  • RNA polymerase I core binding Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC
  • ubiquitin protein ligase binding Source: RGD

GO - Biological processi

  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to growth factor stimulus Source: UniProtKB
  • central nervous system development Source: RGD
  • estrous cycle Source: RGD
  • glial cell differentiation Source: RGD
  • liver development Source: RGD
  • mammary gland involution Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • peripheral nervous system development Source: RGD
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of MAPK cascade Source: RGD
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: RGD
  • positive regulation of protein targeting to membrane Source: UniProtKB
  • positive regulation of Ras protein signal transduction Source: RGD
  • positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
  • protein autophosphorylation Source: RGD
  • regulation of cell differentiation Source: RGD
  • regulation of cell proliferation Source: RGD
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of microtubule-based process Source: UniProtKB
  • response to axon injury Source: RGD
  • response to drug Source: RGD
  • response to progesterone Source: RGD
  • skeletal muscle tissue development Source: RGD
  • sympathetic nervous system development Source: RGD
  • tongue development Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor tyrosine-protein kinase erbB-2 (EC:2.7.10.1)
Alternative name(s):
Epidermal growth factor receptor-related protein
Proto-oncogene Neu
Proto-oncogene c-ErbB-2
p185erbB2
p185neu
CD_antigen: CD340
Gene namesi
Name:Erbb2
Synonyms:Neu
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2561. Erbb2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 654ExtracellularSequence analysisAdd BLAST632
Transmembranei655 – 677HelicalSequence analysisAdd BLAST23
Topological domaini678 – 1257CytoplasmicSequence analysisAdd BLAST580

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • basal plasma membrane Source: RGD
  • basolateral plasma membrane Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • lateral loop Source: RGD
  • membrane raft Source: RGD
  • microvillus Source: RGD
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: Reactome
  • postsynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL3848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001667123 – 1257Receptor tyrosine-protein kinase erbB-2Add BLAST1235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 53Combined sources
Glycosylationi68N-linked (GlcNAc...)Combined sources1
Disulfide bondi163 ↔ 193Combined sources
Glycosylationi188N-linked (GlcNAc...)Combined sources1
Disulfide bondi196 ↔ 205Combined sources
Disulfide bondi200 ↔ 213Combined sources
Disulfide bondi221 ↔ 228Combined sources
Disulfide bondi225 ↔ 236Combined sources
Disulfide bondi237 ↔ 245Combined sources
Disulfide bondi241 ↔ 253Combined sources
Disulfide bondi256 ↔ 265Combined sources
Glycosylationi260N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi269 ↔ 296Combined sources
Disulfide bondi300 ↔ 312Combined sources
Disulfide bondi316 ↔ 332Combined sources
Disulfide bondi335 ↔ 339Combined sources
Disulfide bondi343 ↔ 368Combined sources
Disulfide bondi476 ↔ 506Combined sources
Disulfide bondi513 ↔ 522Combined sources
Disulfide bondi517 ↔ 530Combined sources
Glycosylationi532N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi533 ↔ 542Combined sources
Disulfide bondi546 ↔ 562Combined sources
Disulfide bondi565 ↔ 578Combined sources
Disulfide bondi569 ↔ 586Combined sources
Glycosylationi573N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi589 ↔ 598Combined sources
Disulfide bondi602 ↔ 625Combined sources
Disulfide bondi628 ↔ 636By similarity
Glycosylationi631N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi632 ↔ 644By similarity
Modified residuei1056PhosphoserineCombined sources1
Modified residuei1080PhosphoserineCombined sources1
Modified residuei1085PhosphoserineCombined sources1
Modified residuei1109PhosphoserineBy similarity1
Modified residuei1114PhosphotyrosineBy similarity1
Modified residuei1141Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1168PhosphothreonineBy similarity1
Modified residuei1198PhosphotyrosineBy similarity1
Modified residuei1250Phosphotyrosine; by autocatalysisBy similarity1

Post-translational modificationi

Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligand-binding increases phosphorylation on tyrosine residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1250. Dephosphorylated by PTPN12.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP06494.
PRIDEiP06494.

PTM databases

iPTMnetiP06494.
PhosphoSitePlusiP06494.

Interactioni

Subunit structurei

Homodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1198. Interacts with PRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr-1250) with MEMO1. Interacts with MUC1. Interacts (when phosphorylated on Tyr-1141) with GRB7 (via SH2 domain). Interacts (when phosphorylated on Tyr-1250) with ERBIN Interacts with SRC, KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA94, MYOC and ACTB (By similarity).By similarity

GO - Molecular functioni

  • Hsp90 protein binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • RNA polymerase I core binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: RGD

Protein-protein interaction databases

MINTiMINT-132326.
STRINGi10116.ENSRNOP00000040591.

Chemistry databases

BindingDBiP06494.

Structurei

Secondary structure

11257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 27Combined sources3
Helixi39 – 50Combined sources12
Beta strandi54 – 63Combined sources10
Helixi72 – 74Combined sources3
Beta strandi79 – 82Combined sources4
Beta strandi84 – 88Combined sources5
Turni109 – 111Combined sources3
Beta strandi112 – 117Combined sources6
Beta strandi153 – 158Combined sources6
Helixi170 – 173Combined sources4
Helixi176 – 178Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi201 – 203Combined sources3
Beta strandi205 – 209Combined sources5
Beta strandi228 – 232Combined sources5
Helixi233 – 235Combined sources3
Beta strandi241 – 243Combined sources3
Beta strandi245 – 249Combined sources5
Beta strandi252 – 261Combined sources10
Beta strandi264 – 268Combined sources5
Beta strandi272 – 274Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi295 – 299Combined sources5
Beta strandi310 – 315Combined sources6
Beta strandi320 – 324Combined sources5
Beta strandi330 – 334Combined sources5
Helixi349 – 351Combined sources3
Turni359 – 361Combined sources3
Helixi362 – 365Combined sources4
Beta strandi369 – 377Combined sources9
Helixi379 – 383Combined sources5
Turni386 – 389Combined sources4
Helixi395 – 401Combined sources7
Beta strandi406 – 409Combined sources4
Beta strandi411 – 414Combined sources4
Helixi424 – 426Combined sources3
Turni439 – 441Combined sources3
Beta strandi442 – 448Combined sources7
Beta strandi464 – 470Combined sources7
Helixi483 – 486Combined sources4
Beta strandi494 – 499Combined sources6
Turni507 – 510Combined sources4
Helixi518 – 520Combined sources3
Beta strandi522 – 526Combined sources5
Beta strandi530 – 538Combined sources9
Beta strandi541 – 544Combined sources4
Beta strandi547 – 553Combined sources7
Beta strandi558 – 561Combined sources4
Beta strandi573 – 575Combined sources3
Beta strandi577 – 582Combined sources6
Helixi583 – 585Combined sources3
Beta strandi586 – 594Combined sources9
Beta strandi597 – 601Combined sources5
Beta strandi604 – 606Combined sources3
Beta strandi615 – 619Combined sources5
Beta strandi623 – 627Combined sources5
Helixi650 – 669Combined sources20
Helixi670 – 674Combined sources5
Helixi675 – 679Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IIJNMR-A647-681[»]
1N8YX-ray2.40C23-631[»]
2J1Hmodel-A/B649-681[»]
ProteinModelPortaliP06494.
SMRiP06494.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06494.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini722 – 989Protein kinasePROSITE-ProRule annotationAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni678 – 691Required for interaction with KPNB1 and EEA1By similarityAdd BLAST14
Regioni1197 – 1199Interaction with PIK3C2BBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi678 – 691Nuclear localization signalBy similarityAdd BLAST14

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi159 – 369Cys-richAdd BLAST211
Compositional biasi473 – 646Cys-richAdd BLAST174

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP06494.
PhylomeDBiP06494.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR032778. GF_recep_IV.
IPR009030. Growth_fac_rcpt_.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF14843. GF_recep_IV. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06494-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELAAWCRWG FLLALLPPGI AGTQVCTGTD MKLRLPASPE THLDMLRHLY
60 70 80 90 100
QGCQVVQGNL ELTYVPANAS LSFLQDIQEV QGYMLIAHNQ VKRVPLQRLR
110 120 130 140 150
IVRGTQLFED KYALAVLDNR DPQDNVAAST PGRTPEGLRE LQLRSLTEIL
160 170 180 190 200
KGGVLIRGNP QLCYQDMVLW KDVFRKNNQL APVDIDTNRS RACPPCAPAC
210 220 230 240 250
KDNHCWGESP EDCQILTGTI CTSGCARCKG RLPTDCCHEQ CAAGCTGPKH
260 270 280 290 300
SDCLACLHFN HSGICELHCP ALVTYNTDTF ESMHNPEGRY TFGASCVTTC
310 320 330 340 350
PYNYLSTEVG SCTLVCPPNN QEVTAEDGTQ RCEKCSKPCA RVCYGLGMEH
360 370 380 390 400
LRGARAITSD NVQEFDGCKK IFGSLAFLPE SFDGDPSSGI APLRPEQLQV
410 420 430 440 450
FETLEEITGY LYISAWPDSL RDLSVFQNLR IIRGRILHDG AYSLTLQGLG
460 470 480 490 500
IHSLGLRSLR ELGSGLALIH RNAHLCFVHT VPWDQLFRNP HQALLHSGNR
510 520 530 540 550
PEEDLCVSSG LVCNSLCAHG HCWGPGPTQC VNCSHFLRGQ ECVEECRVWK
560 570 580 590 600
GLPREYVSDK RCLPCHPECQ PQNSSETCFG SEADQCAACA HYKDSSSCVA
610 620 630 640 650
RCPSGVKPDL SYMPIWKYPD EEGICQPCPI NCTHSCVDLD ERGCPAEQRA
660 670 680 690 700
SPVTFIIATV VGVLLFLILV VVVGILIKRR RQKIRKYTMR RLLQETELVE
710 720 730 740 750
PLTPSGAMPN QAQMRILKET ELRKVKVLGS GAFGTVYKGI WIPDGENVKI
760 770 780 790 800
PVAIKVLREN TSPKANKEIL DEAYVMAGVG SPYVSRLLGI CLTSTVQLVT
810 820 830 840 850
QLMPYGCLLD HVREHRGRLG SQDLLNWCVQ IAKGMSYLED VRLVHRDLAA
860 870 880 890 900
RNVLVKSPNH VKITDFGLAR LLDIDETEYH ADGGKVPIKW MALESILRRR
910 920 930 940 950
FTHQSDVWSY GVTVWELMTF GAKPYDGIPA REIPDLLEKG ERLPQPPICT
960 970 980 990 1000
IDVYMIMVKC WMIDSECRPR FRELVSEFSR MARDPQRFVV IQNEDLGPSS
1010 1020 1030 1040 1050
PMDSTFYRSL LEDDDMGDLV DAEEYLVPQQ GFFSPDPTPG TGSTAHRRHR
1060 1070 1080 1090 1100
SSSTRSGGGE LTLGLEPSEE GPPRSPLAPS EGAGSDVFDG DLAMGVTKGL
1110 1120 1130 1140 1150
QSLSPHDLSP LQRYSEDPTL PLPPETDGYV APLACSPQPE YVNQSEVQPQ
1160 1170 1180 1190 1200
PPLTPEGPLP PVRPAGATLE RPKTLSPGKN GVVKDVFAFG GAVENPEYLV
1210 1220 1230 1240 1250
PREGTASPPH PSPAFSPAFD NLYYWDQNSS EQGPPPSNFE GTPTAENPEY

LGLDVPV
Length:1,257
Mass (Da):138,832
Last modified:December 15, 1998 - v3
Checksum:i6129264583011402
GO

Sequence cautioni

The sequence AAH61863 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA27059 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145S → G in AAH61863 (PubMed:15489334).Curated1
Sequence conflicti505 – 509LCVSS → CGLE in AAH61863 (PubMed:15489334).Curated5

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti661V → E in oncogenic NEU. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03362 mRNA. Translation: CAA27059.1. Different initiation.
BC061863 mRNA. Translation: AAH61863.1. Different initiation.
PIRiA24562. TVRTNU.
UniGeneiRn.93966.

Genome annotation databases

UCSCiRGD:2561. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03362 mRNA. Translation: CAA27059.1. Different initiation.
BC061863 mRNA. Translation: AAH61863.1. Different initiation.
PIRiA24562. TVRTNU.
UniGeneiRn.93966.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IIJNMR-A647-681[»]
1N8YX-ray2.40C23-631[»]
2J1Hmodel-A/B649-681[»]
ProteinModelPortaliP06494.
SMRiP06494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-132326.
STRINGi10116.ENSRNOP00000040591.

Chemistry databases

BindingDBiP06494.
ChEMBLiCHEMBL3848.

PTM databases

iPTMnetiP06494.
PhosphoSitePlusiP06494.

Proteomic databases

PaxDbiP06494.
PRIDEiP06494.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2561. rat.

Organism-specific databases

RGDi2561. Erbb2.

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP06494.
PhylomeDBiP06494.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

EvolutionaryTraceiP06494.
PROiP06494.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR032778. GF_recep_IV.
IPR009030. Growth_fac_rcpt_.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF14843. GF_recep_IV. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERBB2_RAT
AccessioniPrimary (citable) accession number: P06494
Secondary accession number(s): Q6P732
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: December 15, 1998
Last modified: November 2, 2016
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.