| UniProt ID | ERBB3_HUMAN | |
|---|---|---|
| UniProt AC | P21860 | |
| Protein Name | Receptor tyrosine-protein kinase erbB-3 | |
| Gene Name | ERBB3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1342 | |
| Subcellular Localization |
Isoform 1: Cell membrane Single-pass type I membrane protein. Isoform 2: Secreted. |
|
| Protein Description | Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. [PubMed: 20682778 May also be activated by CSPG5] | |
| Protein Sequence | MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 15 | Phosphorylation | QVLGLLFSLARGSEV HHHHHHHHHHCCCCC | 22.53 | 22964224 | |
| 123 | Phosphorylation | AIFVMLNYNTNSSHA EEEEEEECCCCCHHH | 21.28 | 30619164 | |
| 125 | Phosphorylation | FVMLNYNTNSSHALR EEEEECCCCCHHHHH | 26.56 | 30619164 | |
| 126 | N-linked_Glycosylation | VMLNYNTNSSHALRQ EEEECCCCCHHHHHH | 37.57 | UniProtKB CARBOHYD | |
| 144 | Phosphorylation | TQLTEILSGGVYIEK HHHHHHHHCCEEEEE | 38.88 | 22468782 | |
| 169 (in isoform 2) | Phosphorylation | - | 41.75 | - | |
| 174 (in isoform 2) | Phosphorylation | - | 4.65 | - | |
| 250 | N-linked_Glycosylation | CFACRHFNDSGACVP CEECCCCCCCCCCCC | 36.09 | 12154198 | |
| 334 | Phosphorylation | CPKACEGTGSGSRFQ CCHHCCCCCCCCCEE | 13.09 | 30576142 | |
| 336 | Phosphorylation | KACEGTGSGSRFQTV HHCCCCCCCCCEEEC | 33.17 | 30576142 | |
| 353 | N-linked_Glycosylation | SNIDGFVNCTKILGN CCCCCEEEHHHHHCC | 26.02 | 12154198 | |
| 408 | N-linked_Glycosylation | SWPPHMHNFSVFSNL CCCCCCCCEECEECC | 24.26 | 12154198 | |
| 414 | N-linked_Glycosylation | HNFSVFSNLTTIGGR CCEECEECCEEECCH | 29.91 | 12154198 | |
| 437 | N-linked_Glycosylation | LLIMKNLNVTSLGFR EEEEECCCCCEECCC | 44.40 | 12154198 | |
| 469 | N-linked_Glycosylation | LCYHHSLNWTKVLRG EEEECCCCCEECCCC | 47.59 | 12154198 | |
| 522 | N-linked_Glycosylation | GQCLSCRNYSRGGVC CCCCCCCCCCCCCEE | 43.38 | 12154198 | |
| 566 | N-linked_Glycosylation | MEGTATCNGSGSDTC CCCCEECCCCCCCCC | 43.22 | 12154198 | |
| 616 | N-linked_Glycosylation | ECRPCHENCTQGCKG CCCCCCCCCCCCCCC | 15.52 | UniProtKB CARBOHYD | |
| 640 | Phosphorylation | TLVLIGKTHLTMALT EEEEECCHHHHHHHH | 19.53 | - | |
| 647 | Phosphorylation | THLTMALTVIAGLVV HHHHHHHHHHHHHHH | 10.59 | 24043423 | |
| 662 | Phosphorylation | IFMMLGGTFLYWRGR HHHHHCCCHHHHCCH | 14.52 | 24043423 | |
| 665 | Phosphorylation | MLGGTFLYWRGRRIQ HHCCCHHHHCCHHHH | 6.72 | 24043423 | |
| 680 | Phosphorylation | NKRAMRRYLERGESI CHHHHHHHHHCCCCC | 11.53 | 27987026 | |
| 686 | Phosphorylation | RYLERGESIEPLDPS HHHHCCCCCCCCCHH | 34.77 | 29255136 | |
| 693 | Phosphorylation | SIEPLDPSEKANKVL CCCCCCHHHHHHHHH | 51.93 | 20639409 | |
| 695 | Ubiquitination | EPLDPSEKANKVLAR CCCCHHHHHHHHHHH | 62.69 | 33845483 | |
| 698 | Ubiquitination | DPSEKANKVLARIFK CHHHHHHHHHHHHHH | 43.41 | 30230243 | |
| 717 | Phosphorylation | RKLKVLGSGVFGTVH HHHEEECCCCCCEEE | 27.85 | 26657352 | |
| 722 | Phosphorylation | LGSGVFGTVHKGVWI ECCCCCCEEECCEEC | 14.15 | 28857561 | |
| 736 | Ubiquitination | IPEGESIKIPVCIKV CCCCCCEEECEEEEE | 50.68 | 33845483 | |
| 736 | Methylation | IPEGESIKIPVCIKV CCCCCCEEECEEEEE | 50.68 | 23644510 | |
| 844 | Phosphorylation | ARNVLLKSPSQVQVA HHHCHHCCCCCEEEE | 29.74 | 26657352 | |
| 846 | Phosphorylation | NVLLKSPSQVQVADF HCHHCCCCCEEEECC | 50.50 | 28857561 | |
| 864 | Ubiquitination | DLLPPDDKQLLYSEA CCCCCCCHHHHHHCC | 50.67 | 29901268 | |
| 868 | Phosphorylation | PDDKQLLYSEAKTPI CCCHHHHHHCCCCCC | 17.04 | - | |
| 869 | Phosphorylation | DDKQLLYSEAKTPIK CCHHHHHHCCCCCCE | 30.92 | - | |
| 873 | Phosphorylation | LLYSEAKTPIKWMAL HHHHCCCCCCEEEEE | 36.98 | 12824184 | |
| 926 | Ubiquitination | EVPDLLEKGERLAQP HCHHHHHHCCHHCCC | 67.07 | 29901268 | |
| 982 | Phosphorylation | YLVIKRESGPGIAPG EEEEEECCCCCCCCC | 55.08 | 30266825 | |
| 996 | Phosphorylation | GPEPHGLTNKKLEEV CCCCCCCCCCCCEEE | 49.97 | 25850435 | |
| 1024 | Phosphorylation | AEEDNLATTTLGSAL CCCCCCCCCCHHHHH | 24.39 | 26552605 | |
| 1025 | Phosphorylation | EEDNLATTTLGSALS CCCCCCCCCHHHHHC | 17.89 | 26552605 | |
| 1026 | Phosphorylation | EDNLATTTLGSALSL CCCCCCCCHHHHHCC | 25.43 | 26552605 | |
| 1029 | Phosphorylation | LATTTLGSALSLPVG CCCCCHHHHHCCCCC | 29.20 | 26552605 | |
| 1032 | Phosphorylation | TTLGSALSLPVGTLN CCHHHHHCCCCCCCC | 30.28 | 26552605 | |
| 1037 | Phosphorylation | ALSLPVGTLNRPRGS HHCCCCCCCCCCCCC | 22.54 | 26552605 | |
| 1044 | Phosphorylation | TLNRPRGSQSLLSPS CCCCCCCCCCCCCCC | 20.20 | 26356563 | |
| 1046 | Phosphorylation | NRPRGSQSLLSPSSG CCCCCCCCCCCCCCC | 32.73 | 26356563 | |
| 1049 | Phosphorylation | RGSQSLLSPSSGYMP CCCCCCCCCCCCCCC | 28.20 | 22210691 | |
| 1051 | Phosphorylation | SQSLLSPSSGYMPMN CCCCCCCCCCCCCCC | 32.78 | 26356563 | |
| 1052 | Phosphorylation | QSLLSPSSGYMPMNQ CCCCCCCCCCCCCCC | 37.01 | 26356563 | |
| 1054 | Phosphorylation | LLSPSSGYMPMNQGN CCCCCCCCCCCCCCC | 10.45 | 16729043 | |
| 1065 | Phosphorylation | NQGNLGESCQESAVS CCCCCCHHHHHHHCC | 21.21 | 22210691 | |
| 1069 | Phosphorylation | LGESCQESAVSGSSE CCHHHHHHHCCCCCC | 14.21 | 22210691 | |
| 1083 | Phosphorylation | ERCPRPVSLHPMPRG CCCCCCCCCCCCCCC | 24.52 | 24719451 | |
| 1094 | Phosphorylation | MPRGCLASESSEGHV CCCCCCCCCCCCCCC | 25.68 | 29255136 | |
| 1096 | Phosphorylation | RGCLASESSEGHVTG CCCCCCCCCCCCCCC | 31.06 | 29255136 | |
| 1097 | Phosphorylation | GCLASESSEGHVTGS CCCCCCCCCCCCCCC | 43.47 | 29255136 | |
| 1102 | Phosphorylation | ESSEGHVTGSEAELQ CCCCCCCCCCHHHHH | 29.34 | 28857561 | |
| 1104 | Phosphorylation | SEGHVTGSEAELQEK CCCCCCCCHHHHHHH | 25.03 | 25849741 | |
| 1113 | Phosphorylation | AELQEKVSMCRSRSR HHHHHHHHHHHCCCC | 24.19 | 24719451 | |
| 1117 | Phosphorylation | EKVSMCRSRSRSRSP HHHHHHHCCCCCCCC | 29.67 | 30631047 | |
| 1119 | Phosphorylation | VSMCRSRSRSRSPRP HHHHHCCCCCCCCCC | 35.54 | 22468782 | |
| 1121 | Phosphorylation | MCRSRSRSRSPRPRG HHHCCCCCCCCCCCC | 38.05 | 17081983 | |
| 1123 | Phosphorylation | RSRSRSRSPRPRGDS HCCCCCCCCCCCCCC | 26.89 | 20068231 | |
| 1130 | Phosphorylation | SPRPRGDSAYHSQRH CCCCCCCCHHHHHCC | 33.29 | 24719451 | |
| 1132 | Phosphorylation | RPRGDSAYHSQRHSL CCCCCCHHHHHCCCC | 13.12 | 27251275 | |
| 1134 | Phosphorylation | RGDSAYHSQRHSLLT CCCCHHHHHCCCCCC | 19.08 | 33259812 | |
| 1138 | Phosphorylation | AYHSQRHSLLTPVTP HHHHHCCCCCCCCCC | 27.54 | 29802988 | |
| 1141 | Phosphorylation | SQRHSLLTPVTPLSP HHCCCCCCCCCCCCC | 22.47 | 26356563 | |
| 1144 | Phosphorylation | HSLLTPVTPLSPPGL CCCCCCCCCCCCCCC | 21.51 | 28348404 | |
| 1147 | Phosphorylation | LTPVTPLSPPGLEEE CCCCCCCCCCCCCCC | 30.19 | 26356563 | |
| 1159 | Phosphorylation | EEEDVNGYVMPDTHL CCCCCCCEECCCCCC | 6.59 | 27259358 | |
| 1164 | Phosphorylation | NGYVMPDTHLKGTPS CCEECCCCCCCCCCC | 24.20 | 26356563 | |
| 1169 | Phosphorylation | PDTHLKGTPSSREGT CCCCCCCCCCCCCCC | 20.57 | 23879269 | |
| 1176 | Phosphorylation | TPSSREGTLSSVGLS CCCCCCCCCCCCCHH | 20.79 | 23879269 | |
| 1183 | Phosphorylation | TLSSVGLSSVLGTEE CCCCCCHHHCCCCCC | 16.69 | 23879269 | |
| 1184 | Phosphorylation | LSSVGLSSVLGTEEE CCCCCHHHCCCCCCC | 26.80 | 23879269 | |
| 1188 | Phosphorylation | GLSSVLGTEEEDEDE CHHHCCCCCCCCCHH | 35.74 | 28348404 | |
| 1197 | Phosphorylation | EEDEDEEYEYMNRRR CCCCHHHHHHHHHHH | 15.43 | 16729043 | |
| 1199 | Phosphorylation | DEDEEYEYMNRRRRH CCHHHHHHHHHHHCC | 9.97 | 16729043 | |
| 1207 | Phosphorylation | MNRRRRHSPPHPPRP HHHHHCCCCCCCCCC | 38.01 | 23312004 | |
| 1215 | Phosphorylation | PPHPPRPSSLEELGY CCCCCCCCHHHHHCC | 49.16 | 24275569 | |
| 1222 | Phosphorylation | SSLEELGYEYMDVGS CHHHHHCCCEEECCC | 19.26 | 16729043 | |
| 1260 | Phosphorylation | GTTPDEDYEYMNRQR CCCCCHHHHHHHCCC | 13.60 | 16729043 | |
| 1262 | Phosphorylation | TPDEDYEYMNRQRDG CCCHHHHHHHCCCCC | 8.08 | 16729043 | |
| 1276 | Phosphorylation | GGGPGGDYAAMGACP CCCCCCCCCCCCCCC | 10.27 | 16729043 | |
| 1285 | Phosphorylation | AMGACPASEQGYEEM CCCCCCHHHHHHHHH | 18.65 | 19060867 | |
| 1289 | Phosphorylation | CPASEQGYEEMRAFQ CCHHHHHHHHHHHHC | 14.38 | 16729043 | |
| 1307 | Phosphorylation | HQAPHVHYARLKTLR CCCCCHHHHHHHHHH | 7.73 | 28152594 | |
| 1312 | Phosphorylation | VHYARLKTLRSLEAT HHHHHHHHHHHHHCC | 31.81 | 28857561 | |
| 1315 | Phosphorylation | ARLKTLRSLEATDSA HHHHHHHHHHCCCCC | 33.40 | 21945579 | |
| 1319 | Phosphorylation | TLRSLEATDSAFDNP HHHHHHCCCCCCCCC | 22.55 | 21945579 | |
| 1321 | Phosphorylation | RSLEATDSAFDNPDY HHHHCCCCCCCCCCH | 26.87 | 21945579 | |
| 1328 | Phosphorylation | SAFDNPDYWHSRLFP CCCCCCCHHHHHHCC | 13.28 | 16729043 | |
| 1331 | Phosphorylation | DNPDYWHSRLFPKAN CCCCHHHHHHCCHHH | 19.28 | 21945579 | |
| 1336 | Ubiquitination | WHSRLFPKANAQRT- HHHHHCCHHHCCCC- | 47.11 | 29901268 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:24662824 |
| - | K | Ubiquitination | E3 ubiquitin ligase | RNF41 | Q9H4P4 | PMID:12411582 |
| - | K | Ubiquitination | E3 ubiquitin ligase | PRKN | O60260 | PMID:15632191 |
| - | K | Ubiquitination | E3 ubiquitin ligase | ITCH | Q96J02 | PMID:27203743 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERBB3_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ERBB3_HUMAN !! | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Structure of the extracellular region of HER3 reveals an interdomaintether."; Cho H.S., Leahy D.J.; Science 297:1330-1333(2002). Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-640, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-250; ASN-353; ASN-408; ASN-414; ASN-437; ASN-469;ASN-522 AND ASN-566. | |
| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, AND MASSSPECTROMETRY. | |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-680, AND MASSSPECTROMETRY. | |
| "An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1328, AND MASSSPECTROMETRY. | |
| "Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1328, AND MASSSPECTROMETRY. | |
