Q12929 (EPS8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epidermal growth factor receptor kinase substrate 8

Gene names

Name:

EPS8

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	822 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes. Ref.9 Ref.11
Subunit structure	Homodimer. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with MYO15A and DFNB31. Interacts with LANCL1 By similarity. Interacts with EGFR; mediates EPS8 phosphorylation By similarity. Interacts with BAIAP2. Interacts with SHB. Ref.6 Ref.8
Subcellular location	Cytoplasm › cell cortex By similarity. Cell projection › ruffle membrane By similarity. Cell projection › growth cone By similarity. Cell projection › stereocilium By similarity. Note: Localizes to the midzone of dividing cells By similarity.
Tissue specificity	Expressed in all tissues analyzed, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in all epithelial and fibroblastic lines examined and in some, but not all, hematopoietic cells.
Domain	The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. It mediates both barbed-end actin capping and actin bundling activities. The capping activity is mediated by an amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers, while the bundling activity is mediated by a compact 4 helix bundle, which contacts 3 actin subunits along the filament By similarity. The SH3 domain mediates interaction with SHB.
Post-translational modification	Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during G2 phase, leading to its transient degradation and subsequent cell shape changes required to allow mitotic progression. Reappears at the midzone of dividing cells By similarity. Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation By similarity. Phosphorylated by several receptor tyrosine kinases.
Involvement in disease	Defects in EPS8 are associated with some cancers, such as pancreatic, oral squamous cell carcinomas or pituitary cancers. Contributes to cell transformation in response to growth factor treatment and is overexpressed in a number of tumors, indicating that EPS8 levels must be tightly regulated.
Sequence similarities	Belongs to the EPS8 family. Contains 1 PH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	SH3 domain
Ligand	Actin-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rac protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB actin crosslink formation Inferred from sequence or structural similarity. Source: UniProtKB actin cytoskeleton reorganization Inferred from electronic annotation. Source: Compara actin filament bundle assembly Inferred from sequence or structural similarity. Source: UniProtKB actin polymerization-dependent cell motility Inferred from sequence or structural similarity. Source: UniProtKB adult locomotory behavior Inferred from electronic annotation. Source: Compara barbed-end actin filament capping Inferred from sequence or structural similarity. Source: UniProtKB behavioral response to ethanol Inferred from electronic annotation. Source: Compara cell proliferation Traceable author statement Ref.1. Source: ProtInc dendritic cell migration Inferred from sequence or structural similarity. Source: UniProtKB epidermal growth factor receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc exit from mitosis Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitotic prometaphase Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	N-methyl-D-aspartate selective glutamate receptor complex Inferred from electronic annotation. Source: Compara cell cortex Inferred from sequence or structural similarity. Source: UniProtKB growth cone Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from sequence or structural similarity. Source: UniProtKB stereocilium Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	Rac GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB SH3/SH2 adaptor activity Traceable author statement Ref.1. Source: ProtInc actin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALDH7A1	P49419	2	EBI-375576,EBI-726842
BAIAP2	Q9UQB8	4	EBI-375576,EBI-525456

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 822

822

Epidermal growth factor receptor kinase substrate 8

PRO_0000086994

Regions

Domain

69 – 129

61

PH; first part

Domain

381 – 414

34

PH; second part

Domain

531 – 590

60

SH3

Region

649 – 822

174

Effector region By similarity

Region

680 – 698

19

Amphipathic helix By similarity

Region

718 – 738

21

Helix bundle 1 By similarity

Region

752 – 757

6

Helix bundle 2 By similarity

Region

762 – 767

6

Helix bundle 3 By similarity

Region

766 – 785

20

Helix bundle 4 By similarity

Compositional bias

421 – 440

20

Pro-rich

Compositional bias

615 – 651

37

Pro-rich

Compositional bias

659 – 664

6

Poly-Ser

Amino acid modifications

Modified residue

476

1

Phosphoserine Ref.14

Modified residue

625

1

Phosphoserine; by MAPK By similarity

Modified residue

629

1

Phosphothreonine; by MAPK By similarity

Natural variations

Natural variant

761

1

D → E.
Corresponds to variant rs7137185 [ dbSNP | Ensembl ].

VAR_050971

Natural variant

806

1

A → S.
Corresponds to variant rs1802658 [ dbSNP | Ensembl ].

VAR_050972

Experimental info

Sequence conflict

73

1

F → S in BAF84466. Ref.2

Sequence conflict

128

1

F → S in BAF84466. Ref.2

Sequence conflict

194

1

R → G in BAF84466. Ref.2

Sequence conflict

205

1

A → S in BAF85620. Ref.2

Sequence conflict

497

1

I → V in BAF85620. Ref.2

Sequence conflict

631

1

A → V in AAH30010. Ref.5

Sequence conflict

705

1

A → T in BAF85620. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

822

Helix Strand Turn

Details...

Helix

729 – 737

9

Helix

741 – 746

6

Beta strand

748 – 750

3

Helix

752 – 757

6

Helix

760 – 766

7

Helix

770 – 784

15

Sequences

	Sequence		Length	Mass (Da)
	Q12929 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: AC5EB1D28B784B3B	FASTA	822	91,882
	10 20 30 40 50 60 MNGHISNHPS SFGMYPSQMN GYGSSPTFSQ TDREHGSKTS AKALYEQRKN YARDSVSSVS 70 80 90 100 110 120 DISQYRVEHL TTFVLDRKDA MITVDDGIRK LKLLDAKGKV WTQDMILQVD DRAVSLIDLE 130 140 150 160 170 180 SKNELENFPL NTIQHCQAVM HSCSYDSVLA LVCKEPTQNK PDLHLFQCDE VKANLISEDI 190 200 210 220 230 240 ESAISDSKGG KQKRRPDALR MISNADPSIP PPPRAPAPAP PGTVTQVDVR SRVAAWSAWA 250 260 270 280 290 300 ADQGDFEKPR QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR 310 320 330 340 350 360 KKNKKGKRKG PGEGVLTLRA KPPPPDEFLD CFQKFKHGFN LLAKLKSHIQ NPSAADLVHF 370 380 390 400 410 420 LFTPLNMVVQ ATGGPELASS VLSPLLNKDT IDFLNYTVNG DERQLWMSLG GTWMKARAEW 430 440 450 460 470 480 PKEQFIPPYV PRFRNGWEPP MLNFMGATME QDLYQLAESV ANVAEHQRKQ EIKRLSTEHS 490 500 510 520 530 540 SVSEYHPADG YAFSSNIYTR GSHLDQGEAA VAFKPTSNRH IDRNYEPLKT QPKKYAKSKY 550 560 570 580 590 600 DFVARNNSEL SVLKDDILEI LDDRKQWWKV RNASGDSGFV PNNILDIVRP PESGLGRADP 610 620 630 640 650 660 PYTHTIQKQR MEYGPRPADT PPAPSPPPTP APVPVPLPPS TPAPVPVSKV PANITRQNSS 670 680 690 700 710 720 SSDSGGSIVR DSQRHKQLPV DRRKSQMEEV QDELIHRLTI GRSAAQKKFH VPRQNVPVIN 730 740 750 760 770 780 ITYDSTPEDV KTWLQSKGFN PVTVNSLGVL NGAQLFSLNK DELRTVCPEG ARVYSQITVQ 790 800 810 820 KAALEDSSGS SELQEIMRRR QEKISAAASD SGVESFDEGS SH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolutionary conservation of the EPS8 gene and its mapping to human chromosome 12q23-q24." Wong W.T., Carlomagno F., Druck T., Barletta C., Croce C.M., Huebner K., Kraus M.H., di Fiore P.P. Oncogene 9:3057-3061(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and Trachea.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins." Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P., Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M. Oncogene 10:1475-1483(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHB.
[7]	"Overexpression of p97Eps8 leads to cellular transformation: implication of pleckstrin homology domain in p97Eps8-mediated ERK activation." Maa M.C., Hsieh C.Y., Leu T.H. Oncogene 20:106-112(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[8]	"IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness." Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H. Cancer Res. 64:5237-5244(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAIAP2.
[9]	"Eps8 controls actin-based motility by capping the barbed ends of actin filaments." Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E., Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G. Nat. Cell Biol. 6:1180-1188(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex." Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E., Steffen A., Berhoerster K., Kreienkamp H.J., Milanesi F., Di Fiore P.P., Ciliberto A., Stradal T.E., Scita G. Nat. Cell Biol. 8:1337-1347(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Eps8 is increased in pancreatic cancer and required for dynamic actin-based cell protrusions and intercellular cytoskeletal organization." Welsch T., Endlich K., Giese T., Buchler M.W., Schmidt J. Cancer Lett. 255:205-218(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[13]	"Eps8 decreases chemosensitivity and affects survival of cervical cancer patients." Chen Y.J., Shen M.R., Chen Y.J., Maa M.C., Leu T.H. Mol. Cancer Ther. 7:1376-1385(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Role for EPS8 in squamous carcinogenesis." Wang H., Patel V., Miyazaki H., Gutkind J.S., Yeudall W.A. Carcinogenesis 30:165-174(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[16]	"Epidermal growth factor receptor pathway substrate 8 is overexpressed in human pituitary tumors: role in proliferation and survival." Xu M., Shorts-Cary L., Knox A.J., Kleinsmidt-DeMasters B., Lillehei K., Wierman M.E. Endocrinology 150:2064-2071(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[17]	"Upregulation of Eps8 in oral squamous cell carcinoma promotes cell migration and invasion through integrin-dependent Rac1 activation." Yap L.F., Jenei V., Robinson C.M., Moutasim K., Benn T.M., Threadgold S.P., Lopes V., Wei W., Thomas G.J., Paterson I.C. Oncogene 28:2524-2534(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[18]	"Solution structure of the C-terminal SAM-domain of epidermal growth receptor pathway substrate 8." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 699-788.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U12535 mRNA. Translation: AAA62280.1.
AK291777 mRNA. Translation: BAF84466.1.
AK292931 mRNA. Translation: BAF85620.1.
AC092753 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96354.1.
BC030010 mRNA. Translation: AAH30010.1.

IPI

IPI00290337.

PIR

I38728.

RefSeq

NP_004438.3. NM_004447.5.

UniGene

Hs.591160.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E8M	NMR	-	A	699-784	[»]

ProteinModelPortal

Q12929.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32859N.

IntAct

Q12929. 35 interactions.

MINT

MINT-5004506.

STRING

9606.ENSP00000281172.

PTM databases

PhosphoSite

Q12929.

Polymorphism databases

DMDM

2833239.

Proteomic databases

PaxDb

Q12929.

PRIDE

Q12929.

Protocols and materials databases

DNASU

2059.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000281172; ENSP00000281172; ENSG00000151491.
ENST00000543523; ENSP00000441867; ENSG00000151491.
ENST00000543612; ENSP00000442388; ENSG00000151491.

GeneID

2059.

KEGG

hsa:2059.

UCSC

uc001rdb.3. human.

Organism-specific databases

CTD

2059.

GeneCards

GC12M015673.

HGNC

HGNC:3420. EPS8.

HPA

HPA003897.

MIM

600206. gene.

neXtProt

NX_Q12929.

PharmGKB

PA27839.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG263108.

HOGENOM

HOG000060324.

HOVERGEN

HBG003090.

InParanoid

Q12929.

OMA

PEDVKTW.

OrthoDB

EOG42V8FP.

Gene expression databases

ArrayExpress

Q12929.

Bgee

Q12929.

CleanEx

HS_EPS8.

Genevestigator

Q12929.

GermOnline

ENSG00000151491. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTyr_interaction_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50003. PH_DOMAIN. False negative.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

EPS8. human.

EvolutionaryTrace

Q12929.

GenomeRNAi

2059.

NextBio

35464377.

SOURCE

Search...

Entry information

Entry name

EPS8_HUMAN

Accession

Primary (citable) accession number: Q12929
Secondary accession number(s): A6NMC3 , A8K6W2, A8KA66, Q8N6J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.