ECT2

Functionⁱ

Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.16 Publications

Activity regulationⁱ

Autoinhibited by the C-terminal PH domain which folds back and binds to the surface of the DH domain, blocking binding of RHOA to the catalytic center of the DH domain (PubMed:31888991). The 2nd BRCT domain is also involved in inhibition, probably by helping to impede RHOA binding (PubMed:31888991). Allosterically activated by binding of activated GTP-bound RHOA to the PH domain which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the catalytic center (PubMed:31888991). Binding of phosphorylated RACGAP1 to the N-terminal BRCT domain-containing region also releases autoinhibition (PubMed:25068414).2 Publications

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Guanine-nucleotide releasing factor
Biological process	Cell cycle, Cell division, Differentiation, Neurogenesis, Protein transport, Transport

Enzyme and pathway databases

PathwayCommonsⁱ	Q9H8V3
Reactomeⁱ	R-HSA-193648, NRAGE signals death through JNK R-HSA-194840, Rho GTPase cycle R-HSA-416482, G alpha (12/13) signalling events
SignaLinkⁱ	Q9H8V3
SIGNORⁱ	Q9H8V3

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein ECT2 Alternative name(s): Epithelial cell-transforming sequence 2 oncogene
Gene namesⁱ	Name:ECT2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000114346.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3155, ECT2
MIMⁱ	600586, gene
neXtProtⁱ	NX_Q9H8V3

Keywords - Cellular componentⁱ

Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Tight junction

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	184	T → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 2 Publications	1
Mutagenesisⁱ	226	K → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 2 Publications	1
Mutagenesisⁱ	336	W → R: Inhibits homodimerization. Increases binding with RhoA and GEF activity. 1 Publication	1
Mutagenesisⁱ	338	W → A: 2-fold increase in GEF activity. 1 Publication	1
Mutagenesisⁱ	359	T → A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity. 1 Publication	1
Mutagenesisⁱ	373	T → A: Does not inhibit its Rho exchange activity. Increases interaction with RACGAP1. Does not inhibit anchorage-independent growth and invasion in cancer cells. 2 Publications	1
Mutagenesisⁱ	373	T → D: Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity. 2 Publications	1
Mutagenesisⁱ	379 – 381	KRR → AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication	3
Mutagenesisⁱ	402 – 404	RKR → AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication	3
Mutagenesisⁱ	444	T → A: Diminishes its phosphorylation status. Reduces its interaction with PLK1 and Rho exchange activity. Does not change its subcellular localization. Does not inhibit anchorage-independent growth and invasion in cancer cells. 1 Publication	1
Mutagenesisⁱ	444	T → D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity. 1 Publication	1
Mutagenesisⁱ	488	R → C: Partially releases inhibition. 1 Publication	1
Mutagenesisⁱ	570	R → D: 2-fold increase in GEF activity. 1 Publication	1
Mutagenesisⁱ	573	A → D: 2-fold increase in GEF activity. 1 Publication	1
Mutagenesisⁱ	586	R → Q: Complete loss of GEF activity and failure to support cytokinesis. 1 Publication	1
Mutagenesisⁱ	596 – 599	PVQR → AAAA: Inhibits activation of the transforming activity. 1 Publication	4
Mutagenesisⁱ	601	P → S: Complete loss of GEF activity and failure to support cytokinesis. 1 Publication	1
Mutagenesisⁱ	652	F → A: No effect on GEF activity but severely decreases ECT2 activation by RHOA. Localizes correctly but fails to rescue the cytokinesis defect caused by knockdown of endogenous ECT2 in contrast to the wild-type protein which rescues this defect. 1 Publication	1
Mutagenesisⁱ	656	Y → A: No effect on GEF activity but severely decreases ECT2 activation by RHOA. Fails to rescue the cytokinesis defect caused by knockdown of endogenous ECT2 in contrast to the wild-type protein which rescues this defect. 1 Publication	1
Mutagenesisⁱ	670	R → Q: Marked increase in GEF activity and rescues the cytokinesis defect caused by depletion of endogenous ECT2. When expressed in a cancer cell line, causes faster cell proliferation than the wild-type protein. 1 Publication	1
Mutagenesisⁱ	734	P → D: More than 10-fold increase in GEF activity. Overexpression causes noticeable changes in interphase cell morphology such as cell rounding and formation of stress fibers, suggesting ectopic RhoA activation. 1 Publication	1
Mutagenesisⁱ	796	C → K: More than 10-fold increase in GEF activity. Overexpression causes noticeable changes in interphase cell morphology such as cell rounding and formation of stress fibers, suggesting ectopic RHOA activation. 1 Publication	1
Mutagenesisⁱ	846	T → A: Diminishes its phosphorylation status. 1 Publication	1

Keywords - Diseaseⁱ

Oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1894
Open Targets More...OpenTargetsⁱ	ENSG00000114346
PharmGKBⁱ	PA27600

Miscellaneous databases

Pharosⁱ	Q9H8V3, Tbio

Pharosⁱ

Q9H8V3, Tbio

Polymorphism and mutation databases

BioMutaⁱ	ECT2
DMDMⁱ	357529579

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000080938	2 – 914	Protein ECT2Add BLAST		913

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources	1
Modified residueⁱ	359	Phosphothreonine; by PKC/PRKCICombined sources1 Publication	1
Modified residueⁱ	367	PhosphoserineCombined sources	1
Modified residueⁱ	370	PhosphoserineCombined sources	1
Modified residueⁱ	373	Phosphothreonine; by CDK1Combined sources1 Publication	1
Modified residueⁱ	376	PhosphoserineCombined sources	1
Modified residueⁱ	444	Phosphothreonine; by CDK11 Publication	1
Cross-linkⁱ	611	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	716	PhosphoserineCombined sources	1
Modified residueⁱ	842	PhosphoserineCombined sources	1
Modified residueⁱ	846	Phosphothreonine; by CDK1Combined sources	1
Modified residueⁱ	861	PhosphoserineCombined sources	1
Modified residueⁱ	866	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells.4 Publications

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9H8V3
jPOSTⁱ	Q9H8V3
MassIVEⁱ	Q9H8V3
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9H8V3
PaxDbⁱ	Q9H8V3
PeptideAtlas More...PeptideAtlasⁱ	Q9H8V3
PRIDEⁱ	Q9H8V3
ProteomicsDBⁱ	81243 [Q9H8V3-1] 81244 [Q9H8V3-2] 81245 [Q9H8V3-3]

PTM databases

iPTMnetⁱ	Q9H8V3
MetOSiteⁱ	Q9H8V3
PhosphoSitePlusⁱ	Q9H8V3

Expressionⁱ

Tissue specificityⁱ

Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma.1 Publication

Inductionⁱ

Up-regulated by calcium in cells forming cell-cell contact sites. Up-regulated by DNA damaging agents like H₂O₂ or ionizing radiation (IR).2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000114346, Expressed in secondary oocyte and 206 other tissues
ExpressionAtlasⁱ	Q9H8V3, baseline and differential
Genevisibleⁱ	Q9H8V3, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000114346, Tissue enhanced (lymphoid)

HPAⁱ

ENSG00000114346, Tissue enhanced (lymphoid)

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:15545273, PubMed:14645260, PubMed:16170345). Homooligomer (PubMed:15545273).

Found in the centralspindlin complex (PubMed:16236794).

Interacts with NR1I3 (By similarity).

Interacts (Thr-359 phosphorylated form) with PARD6A; the interaction is observed in cancer cells (PubMed:15254234, PubMed:19617897).

Interacts (Thr-359 phosphorylated form) with PRKCI; the interaction is observed in cancer cells (PubMed:19617897).

Interacts with PKP4; the interaction is observed at the midbody (PubMed:22814378).

Interacts with RACGAP1/CYK4; the interaction is direct, occurs in a microtubule-dependent manner, occurs at anaphase and during cytokinesis, is inhibited in metaphase by phosphorylation of ECT2 on Thr-373 and is stimulated in early anaphase by dephosphorylation of ECT2 probably on Thr-373 through CDK1 activity (PubMed:16103226, PubMed:16129829, PubMed:16236794, PubMed:19468300, PubMed:19468302, PubMed:25068414).

Interacts with PLK1; the interaction is stimulated upon its phosphorylation on Thr-444 (PubMed:16247472).

Interacts with RHOA; the interaction results in allosteric activation of ECT2 (PubMed:31888991).

Interacts with KIF23, PARD3, PARD6B and PRKCQ (PubMed:15254234, PubMed:16236794).

By similarity14 Publications

Binary interactionsⁱ

Hide details

Q9H8V3

With	#Exp.	IntAct
CDH1 [P12830]	3	EBI-1054039,EBI-727477
CTNNA1 [P35221]	3	EBI-1054039,EBI-701918
KIF23 [Q02241]	2	EBI-1054039,EBI-306852
NCK1 [P16333]	3	EBI-1054039,EBI-389883
PLK4 [O00444]	3	EBI-1054039,EBI-746202
RACGAP1 [Q9H0H5]	15	EBI-1054039,EBI-717233

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	108223, 161 interactors
CORUMⁱ	Q9H8V3
Database of interacting proteins More...DIPⁱ	DIP-47496N
IntActⁱ	Q9H8V3, 23 interactors
Molecular INTeraction database More...MINTⁱ	Q9H8V3
STRINGⁱ	9606.ENSP00000376457

Miscellaneous databases

RNActⁱ	Q9H8V3, protein

RNActⁱ

Q9H8V3, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	51 – 56	Combined sources	6
Helixⁱ	57 – 59	Combined sources	3
Helixⁱ	63 – 70	Combined sources	8
Beta strandⁱ	107 – 112	Combined sources	6
Helixⁱ	115 – 119	Combined sources	5
Beta strandⁱ	124 – 129	Combined sources	6
Helixⁱ	136 – 143	Combined sources	8
Beta strandⁱ	147 – 149	Combined sources	3
Helixⁱ	151 – 159	Combined sources	9
Turnⁱ	173 – 178	Combined sources	6
Beta strandⁱ	180 – 184	Combined sources	5
Helixⁱ	189 – 201	Combined sources	13
Beta strandⁱ	215 – 224	Combined sources	10
Helixⁱ	225 – 233	Combined sources	9
Helixⁱ	241 – 249	Combined sources	9
Helixⁱ	260 – 263	Combined sources	4
Helixⁱ	264 – 266	Combined sources	3
Turnⁱ	270 – 273	Combined sources	4
Beta strandⁱ	278 – 280	Combined sources	3
Helixⁱ	283 – 295	Combined sources	13
Beta strandⁱ	309 – 313	Combined sources	5
Turnⁱ	315 – 317	Combined sources	3
Beta strandⁱ	318 – 320	Combined sources	3
Beta strandⁱ	330 – 333	Combined sources	4
Helixⁱ	334 – 343	Combined sources	10
Helixⁱ	349 – 351	Combined sources	3
Helixⁱ	453 – 477	Combined sources	25
Helixⁱ	479 – 483	Combined sources	5
Helixⁱ	495 – 502	Combined sources	8
Helixⁱ	505 – 522	Combined sources	18
Helixⁱ	532 – 552	Combined sources	21
Helixⁱ	554 – 567	Combined sources	14
Helixⁱ	569 – 579	Combined sources	11
Helixⁱ	582 – 584	Combined sources	3
Helixⁱ	589 – 611	Combined sources	23
Helixⁱ	622 – 634	Combined sources	13
Helixⁱ	635 – 637	Combined sources	3
Helixⁱ	642 – 657	Combined sources	16
Helixⁱ	664 – 667	Combined sources	4
Beta strandⁱ	672 – 687	Combined sources	16
Beta strandⁱ	691 – 697	Combined sources	7
Beta strandⁱ	700 – 706	Combined sources	7
Beta strandⁱ	726 – 734	Combined sources	9
Helixⁱ	735 – 737	Combined sources	3
Beta strandⁱ	738 – 744	Combined sources	7
Beta strandⁱ	748 – 758	Combined sources	11
Turnⁱ	761 – 763	Combined sources	3
Beta strandⁱ	767 – 773	Combined sources	7
Helixⁱ	780 – 795	Combined sources	16
Beta strandⁱ	803 – 807	Combined sources	5

Show more details

3D structure databases

SMRⁱ	Q9H8V3
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9H8V3

EvolutionaryTraceⁱ

Q9H8V3

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	171 – 260	BRCT 1PROSITE-ProRule annotationAdd BLAST	90
Domainⁱ	266 – 354	BRCT 2PROSITE-ProRule annotationAdd BLAST	89
Domainⁱ	452 – 641	DHPROSITE-ProRule annotationAdd BLAST	190
Domainⁱ	675 – 794	PHAdd BLAST	120

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	378 – 382	Nuclear localization signal		5
Motifⁱ	401 – 405	Nuclear localization signal		5

Domainⁱ

The BRCT domains 1 and 2 are required for intramolecular interaction, but not for intermolecular oligomerization (PubMed:15545273). The BRCT domains negatively inhibit its GEF activity in interphase cells (PubMed:15545273, PubMed:31888991). The same BRCT domains may act as a positive regulatory motif for the completion of cytokinesis after the breakdown of nuclear membrane during mitosis (PubMed:15545273).2 Publications

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG3524, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000156299
HOGENOMⁱ	CLU_008187_0_0_1
InParanoidⁱ	Q9H8V3
KEGG Orthology (KO) More...KOⁱ	K20704
OMAⁱ	CKAKESN
Database of Orthologous Groups More...OrthoDBⁱ	557169at2759
TreeFamⁱ	TF101161

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00160, RhoGEF, 1 hit
Gene3Dⁱ	1.20.900.10, 1 hit 2.30.29.30, 1 hit 3.40.50.10190, 3 hits
InterProⁱ	View protein in InterPro IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR035899, DBL_dom_sf IPR000219, DH-domain IPR026817, Ect2 IPR001331, GDS_CDC24_CS IPR011993, PH-like_dom_sf
PANTHERⁱ	PTHR16777, PTHR16777, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00533, BRCT, 1 hit PF12738, PTCB-BRCT, 1 hit PF00621, RhoGEF, 1 hit
SMARTⁱ	View protein in SMART SM00292, BRCT, 2 hits SM00325, RhoGEF, 1 hit
SUPFAMⁱ	SSF48065, SSF48065, 1 hit SSF52113, SSF52113, 2 hits
PROSITEⁱ	View protein in PROSITE PS50172, BRCT, 2 hits PS00741, DH_1, 1 hit PS50010, DH_2, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 8 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9H8V3-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE 
        60         70         80         90        100
TRVILVQEAG KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN 
       110        120        130        140        150
MDIKVGFVKM ESVEEFEGLD SPEFENVFVV TDFQDSVFND LYKADCRVIG 
       160        170        180        190        200
PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV LCFTGFRKKE ELVRLVTLVH 
       210        220        230        240        250
HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP EWIYKAWERR 
       260        270        280        290        300
NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 
       310        320        330        340        350
LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET 
       360        370        380        390        400
MYLYEKANTP ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP 
       410        420        430        440        450
PRKRPSAEHS LSIGSLLDIS NTPESSINYG DTPKSCTKSS KSSTPVPSKQ 
       460        470        480        490        500
SARWQVAKEL YQTESNYVNI LATIIQLFQV PLEEEGQRGG PILAPEEIKT 
       510        520        530        540        550
IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS KDLVKTYPPF 
       560        570        580        590        600
VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 
       610        620        630        640        650
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ 
       660        670        680        690        700
IFDVVYEVDG CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC 
       710        720        730        740        750
LEIARKRHKV IGTFRSPHGQ TRPPASLKHI HLMPLSQIKK VLDIRETEDC 
       760        770        780        790        800
HNAFALLVRP PTEQANVLLS FQMTSDELPK ENWLKMLCRH VANTICKADA 
       810        820        830        840        850
ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA FSFSKTPKRA 
       860        870        880        890        900
LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAGIPSP SLVSLPSFFE 
       910 
RRSHTLSRST THLI

Length:914

Mass (Da):103,505

Last modified:November 16, 2011 - v4

Checksum:ⁱF40FC4F982FB8C78

GO

Isoform 2 (identifier: Q9H8V3-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
44-44: Missing.
71-101: Missing.

« Hide

        10         20         30         40         50
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEMPQIET 
        60         70         80         90        100
RVILVQEAGK QEELIKALKD IKVGFVKMES VEEFEGLDSP EFENVFVVTD 
       110        120        130        140        150
FQDSVFNDLY KADCRVIGPP VVLNCSQKGE PLPFSCRPLY CTSMMNLVLC 
       160        170        180        190        200
FTGFRKKEEL VRLVTLVHHM GGVIRKDFNS KVTHLVANCT QGEKFRVAVS 
       210        220        230        240        250
LGTPIMKPEW IYKAWERRNE QDFYAAVDDF RNEFKVPPFQ DCILSFLGFS 
       260        270        280        290        300
DEEKTNMEEM TEMQGGKYLP LGDERCTHLV VEENIVKDLP FEPSKKLYVV 
       310        320        330        340        350
KQEWFWGSIQ MDARAGETMY LYEKANTPEL KKSVSMLSLN TPNSNRKRRR 
       360        370        380        390        400
LKETLAQLSR ETDVSPFPPR KRPSAEHSLS IGSLLDISNT PESSINYGDT 
       410        420        430        440        450
PKSCTKSSKS STPVPSKQSA RWQVAKELYQ TESNYVNILA TIIQLFQVPL 
       460        470        480        490        500
EEEGQRGGPI LAPEEIKTIF GSIPDIFDVH TKIKDDLEDL IVNWDESKSI 
       510        520        530        540        550
GDIFLKYSKD LVKTYPPFVN FFEMSKETII KCEKQKPRFH AFLKINQAKP 
       560        570        580        590        600
ECGRQSLVEL LIRPVQRLPS VALLLNDLKK HTADENPDKS TLEKAIGSLK 
       610        620        630        640        650
EVMTHINEDK RKTEAQKQIF DVVYEVDGCP ANLLSSHRSL VQRVETISLG 
       660        670        680        690        700
EHPCDRGEQV TLFLFNDCLE IARKRHKVIG TFRSPHGQTR PPASLKHIHL 
       710        720        730        740        750
MPLSQIKKVL DIRETEDCHN AFALLVRPPT EQANVLLSFQ MTSDELPKEN 
       760        770        780        790        800
WLKMLCRHVA NTICKADAEN LIYTADPESF EVNTKDMDST LSRASRAIKK 
       810        820        830        840        850
TSKKVTRAFS FSKTPKRALR RALMTSHGSV EGRSPSSNDK HVMSRLSSTS 
       860        870        880 
SLAGIPSPSL VSLPSFFERR SHTLSRSTTH LI

Show »

Length:882

Mass (Da):99,921

Checksum:ⁱAAD4483A503D086C

GO

Isoform 3 (identifier: Q9H8V3-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
886-914: GIPSPSLVSLPSFFERRSHTLSRSTTHLI → ITHSVSTSNV...SKSSLTFVKN

« Hide

        10         20         30         40         50
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE 
        60         70         80         90        100
TRVILVQEAG KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN 
       110        120        130        140        150
MDIKVGFVKM ESVEEFEGLD SPEFENVFVV TDFQDSVFND LYKADCRVIG 
       160        170        180        190        200
PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV LCFTGFRKKE ELVRLVTLVH 
       210        220        230        240        250
HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP EWIYKAWERR 
       260        270        280        290        300
NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 
       310        320        330        340        350
LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET 
       360        370        380        390        400
MYLYEKANTP ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP 
       410        420        430        440        450
PRKRPSAEHS LSIGSLLDIS NTPESSINYG DTPKSCTKSS KSSTPVPSKQ 
       460        470        480        490        500
SARWQVAKEL YQTESNYVNI LATIIQLFQV PLEEEGQRGG PILAPEEIKT 
       510        520        530        540        550
IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS KDLVKTYPPF 
       560        570        580        590        600
VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 
       610        620        630        640        650
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ 
       660        670        680        690        700
IFDVVYEVDG CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC 
       710        720        730        740        750
LEIARKRHKV IGTFRSPHGQ TRPPASLKHI HLMPLSQIKK VLDIRETEDC 
       760        770        780        790        800
HNAFALLVRP PTEQANVLLS FQMTSDELPK ENWLKMLCRH VANTICKADA 
       810        820        830        840        850
ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA FSFSKTPKRA 
       860        870        880        890        900
LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAITHSV STSNVIGFTK 
       910        920        930        940        950
HVYVQRLNST GGRSQYSWFQ SVRHSAFRAS FSEILEGNTD FSNFKKVLSK 

SSLTFVKN

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.Curated

Show »

Length:958

Mass (Da):108,529

Checksum:ⁱF505EBBF2E1BBE23

GO

Isoform 4 (identifier: Q9H8V3-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
71-101: Missing.

« Hide

        10         20         30         40         50
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE 
        60         70         80         90        100
TRVILVQEAG KQEELIKALK DIKVGFVKME SVEEFEGLDS PEFENVFVVT 
       110        120        130        140        150
DFQDSVFNDL YKADCRVIGP PVVLNCSQKG EPLPFSCRPL YCTSMMNLVL 
       160        170        180        190        200
CFTGFRKKEE LVRLVTLVHH MGGVIRKDFN SKVTHLVANC TQGEKFRVAV 
       210        220        230        240        250
SLGTPIMKPE WIYKAWERRN EQDFYAAVDD FRNEFKVPPF QDCILSFLGF 
       260        270        280        290        300
SDEEKTNMEE MTEMQGGKYL PLGDERCTHL VVEENIVKDL PFEPSKKLYV 
       310        320        330        340        350
VKQEWFWGSI QMDARAGETM YLYEKANTPE LKKSVSMLSL NTPNSNRKRR 
       360        370        380        390        400
RLKETLAQLS RETDVSPFPP RKRPSAEHSL SIGSLLDISN TPESSINYGD 
       410        420        430        440        450
TPKSCTKSSK SSTPVPSKQS ARWQVAKELY QTESNYVNIL ATIIQLFQVP 
       460        470        480        490        500
LEEEGQRGGP ILAPEEIKTI FGSIPDIFDV HTKIKDDLED LIVNWDESKS 
       510        520        530        540        550
IGDIFLKYSK DLVKTYPPFV NFFEMSKETI IKCEKQKPRF HAFLKINQAK 
       560        570        580        590        600
PECGRQSLVE LLIRPVQRLP SVALLLNDLK KHTADENPDK STLEKAIGSL 
       610        620        630        640        650
KEVMTHINED KRKTEAQKQI FDVVYEVDGC PANLLSSHRS LVQRVETISL 
       660        670        680        690        700
GEHPCDRGEQ VTLFLFNDCL EIARKRHKVI GTFRSPHGQT RPPASLKHIH 
       710        720        730        740        750
LMPLSQIKKV LDIRETEDCH NAFALLVRPP TEQANVLLSF QMTSDELPKE 
       760        770        780        790        800
NWLKMLCRHV ANTICKADAE NLIYTADPES FEVNTKDMDS TLSRASRAIK 
       810        820        830        840        850
KTSKKVTRAF SFSKTPKRAL RRALMTSHGS VEGRSPSSND KHVMSRLSST 
       860        870        880 
SSLAGIPSPS LVSLPSFFER RSHTLSRSTT HLI

Show »

Length:883

Mass (Da):100,051

Checksum:ⁱBAEFC693495C50E1

GO

Computationally mapped potential isoform sequencesⁱ

There are 8 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H7C3G1	H7C3G1_HUMAN	Protein ECT2 Protein ECT2	ECT2	209	Annotation score:
C9JDB4	C9JDB4_HUMAN	Protein ECT2 Protein ECT2	ECT2	204	Annotation score:
C9J0L6	C9J0L6_HUMAN	Protein ECT2 Protein ECT2	ECT2	106	Annotation score:
H7C103	H7C103_HUMAN	Protein ECT2 Protein ECT2	ECT2	298	Annotation score:
C9J1C4	C9J1C4_HUMAN	Protein ECT2 Protein ECT2	ECT2	159	Annotation score:
C9JTI2	C9JTI2_HUMAN	Protein ECT2 Protein ECT2	ECT2	150	Annotation score:
C9JDV9	C9JDV9_HUMAN	Protein ECT2 Protein ECT2	ECT2	110	Annotation score:
C9JB41	C9JB41_HUMAN	Protein ECT2 Protein ECT2	ECT2	18	Annotation score:

Sequence cautionⁱ

The sequence BAA91624 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	66	I → T in BAB14498 (PubMed:16641997).Curated	1
Sequence conflictⁱ	276	L → F in BAB14498 (PubMed:16641997).Curated	1
Sequence conflictⁱ	393	E → D in BAB14498 (PubMed:16641997).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_047064	15	S → T. Corresponds to variant dbSNP:rs34703432Ensembl.		1
Natural variantⁱVAR_035975	833	T → P in a breast cancer sample; somatic mutation. 1 Publication		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_041976	44	Missing in isoform 2. 4 Publications	1
Alternative sequenceⁱVSP_041977	71 – 101	Missing in isoform 2 and isoform 4. 4 PublicationsAdd BLAST	31
Alternative sequenceⁱVSP_041978	886 – 914	GIPSP…TTHLI → ITHSVSTSNVIGFTKHVYVQ RLNSTGGRSQYSWFQSVRHS AFRASFSEILEGNTDFSNFK KVLSKSSLTFVKN in isoform 3. 1 PublicationAdd BLAST	29

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY376439 mRNA Translation: AAQ83675.1 DQ847274 mRNA Translation: ABH10140.1 AK001323 mRNA Translation: BAA91624.1 Different initiation. AK023267 mRNA Translation: BAB14498.1 AK314581 mRNA Translation: BAG37157.1 AC108667 Genomic DNA No translation available. BC112086 mRNA Translation: AAI12087.1 AL137710 mRNA Translation: CAB70886.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3220.1 [Q9H8V3-4] CCDS58860.1 [Q9H8V3-1] CCDS87168.1 [Q9H8V3-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001245244.1, NM_001258315.1 [Q9H8V3-1] NP_001245245.1, NM_001258316.1 [Q9H8V3-4] NP_060568.3, NM_018098.5 [Q9H8V3-4] XP_011510816.1, XM_011512514.2 [Q9H8V3-3]

Genome annotation databases

Ensemblⁱ	ENST00000232458; ENSP00000232458; ENSG00000114346 [Q9H8V3-4] ENST00000392692; ENSP00000376457; ENSG00000114346 [Q9H8V3-1] ENST00000417960; ENSP00000415876; ENSG00000114346 [Q9H8V3-2] ENST00000441497; ENSP00000412259; ENSG00000114346 [Q9H8V3-4] ENST00000540509; ENSP00000443160; ENSG00000114346 [Q9H8V3-4]
GeneIDⁱ	1894
KEGGⁱ	hsa:1894
UCSC genome browser More...UCSCⁱ	uc003fih.4, human [Q9H8V3-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9H8V3	ECT2 protein		HUMAN		182	UniRef100_Q9H8V3
Uncharacterized protein		RHIRO		182
cDNA FLJ14807 fis, clone NT2RP4001760, weakly similar to PUTATIVE RHO/RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR		HUMAN		359
Q9H8V3-3	Protein ECT2 (Fragment)		HUMAN		110	UniRef100_Q9H8V3-3
Protein ECT2 (Fragment)		HUMAN		150

Protein	Similar proteins		Species	Score	Length	Source
Q9H8V3	ECT2 protein		HUMAN		182	UniRef90_Q9H8V3
Uncharacterized protein		RHIRO		182
Epithelial cell transforming 2		HORSE		1042
protein ECT2 isoform X1		TURTR		973
protein ECT2 isoform X1		NEOAA		973
+286

Protein	Similar proteins		Species	Score	Length	Source
Q9H8V3	ECT2 protein		HUMAN		182	UniRef50_Q9H8V3
Uncharacterized protein		RHIRO		182
Epithelial cell transforming 2		HORSE		1042
protein ECT2 isoform X1		TURTR		973
protein ECT2 isoform X1		NEOAA		973
+529

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY376439 mRNA Translation: AAQ83675.1 DQ847274 mRNA Translation: ABH10140.1 AK001323 mRNA Translation: BAA91624.1 Different initiation. AK023267 mRNA Translation: BAB14498.1 AK314581 mRNA Translation: BAG37157.1 AC108667 Genomic DNA No translation available. BC112086 mRNA Translation: AAI12087.1 AL137710 mRNA Translation: CAB70886.1
CCDSⁱ	CCDS3220.1 [Q9H8V3-4] CCDS58860.1 [Q9H8V3-1] CCDS87168.1 [Q9H8V3-2]
RefSeqⁱ	NP_001245244.1, NM_001258315.1 [Q9H8V3-1] NP_001245245.1, NM_001258316.1 [Q9H8V3-4] NP_060568.3, NM_018098.5 [Q9H8V3-4] XP_011510816.1, XM_011512514.2 [Q9H8V3-3]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3L46	X-ray	1.48	A/B	268-361	[»]
	4N40	X-ray	3.11	A	45-356	[»]
	6L30	X-ray	2.80	A	173-865	[»]
SMRⁱ	Q9H8V3
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	108223, 161 interactors
CORUMⁱ	Q9H8V3
DIPⁱ	DIP-47496N
IntActⁱ	Q9H8V3, 23 interactors
MINTⁱ	Q9H8V3
STRINGⁱ	9606.ENSP00000376457

PTM databases

iPTMnetⁱ	Q9H8V3
MetOSiteⁱ	Q9H8V3
PhosphoSitePlusⁱ	Q9H8V3

Polymorphism and mutation databases

BioMutaⁱ	ECT2
DMDMⁱ	357529579

Proteomic databases

EPDⁱ	Q9H8V3
jPOSTⁱ	Q9H8V3
MassIVEⁱ	Q9H8V3
MaxQBⁱ	Q9H8V3
PaxDbⁱ	Q9H8V3
PeptideAtlasⁱ	Q9H8V3
PRIDEⁱ	Q9H8V3
ProteomicsDBⁱ	81243 [Q9H8V3-1] 81244 [Q9H8V3-2] 81245 [Q9H8V3-3]

Protocols and materials databases

Antibodypediaⁱ	33733, 365 antibodies

Antibodypediaⁱ

33733, 365 antibodies

Genome annotation databases

Ensemblⁱ	ENST00000232458; ENSP00000232458; ENSG00000114346 [Q9H8V3-4] ENST00000392692; ENSP00000376457; ENSG00000114346 [Q9H8V3-1] ENST00000417960; ENSP00000415876; ENSG00000114346 [Q9H8V3-2] ENST00000441497; ENSP00000412259; ENSG00000114346 [Q9H8V3-4] ENST00000540509; ENSP00000443160; ENSG00000114346 [Q9H8V3-4]
GeneIDⁱ	1894
KEGGⁱ	hsa:1894
UCSCⁱ	uc003fih.4, human [Q9H8V3-1]

Organism-specific databases

CTDⁱ	1894
DisGeNETⁱ	1894
EuPathDBⁱ	HostDB:ENSG00000114346.13
GeneCardsⁱ	ECT2
HGNCⁱ	HGNC:3155, ECT2
HPAⁱ	ENSG00000114346, Tissue enhanced (lymphoid)
MIMⁱ	600586, gene
neXtProtⁱ	NX_Q9H8V3
OpenTargetsⁱ	ENSG00000114346
PharmGKBⁱ	PA27600
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3524, Eukaryota
GeneTreeⁱ	ENSGT00940000156299
HOGENOMⁱ	CLU_008187_0_0_1
InParanoidⁱ	Q9H8V3
KOⁱ	K20704
OMAⁱ	CKAKESN
OrthoDBⁱ	557169at2759
TreeFamⁱ	TF101161

Enzyme and pathway databases

PathwayCommonsⁱ	Q9H8V3
Reactomeⁱ	R-HSA-193648, NRAGE signals death through JNK R-HSA-194840, Rho GTPase cycle R-HSA-416482, G alpha (12/13) signalling events
SignaLinkⁱ	Q9H8V3
SIGNORⁱ	Q9H8V3

Miscellaneous databases

BioGRID-ORCSⁱ	1894, 610 hits in 881 CRISPR screens
ChiTaRSⁱ	ECT2, human
EvolutionaryTraceⁱ	Q9H8V3
GeneWikiⁱ	ECT2
GenomeRNAiⁱ	1894
Pharosⁱ	Q9H8V3, Tbio
Protein Ontology More...PROⁱ	PR:Q9H8V3
RNActⁱ	Q9H8V3, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000114346, Expressed in secondary oocyte and 206 other tissues
ExpressionAtlasⁱ	Q9H8V3, baseline and differential
Genevisibleⁱ	Q9H8V3, HS

Family and domain databases

CDDⁱ	cd00160, RhoGEF, 1 hit
Gene3Dⁱ	1.20.900.10, 1 hit 2.30.29.30, 1 hit 3.40.50.10190, 3 hits
InterProⁱ	View protein in InterPro IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR035899, DBL_dom_sf IPR000219, DH-domain IPR026817, Ect2 IPR001331, GDS_CDC24_CS IPR011993, PH-like_dom_sf
PANTHERⁱ	PTHR16777, PTHR16777, 1 hit
Pfamⁱ	View protein in Pfam PF00533, BRCT, 1 hit PF12738, PTCB-BRCT, 1 hit PF00621, RhoGEF, 1 hit
SMARTⁱ	View protein in SMART SM00292, BRCT, 2 hits SM00325, RhoGEF, 1 hit
SUPFAMⁱ	SSF48065, SSF48065, 1 hit SSF52113, SSF52113, 2 hits
PROSITEⁱ	View protein in PROSITE PS50172, BRCT, 2 hits PS00741, DH_1, 1 hit PS50010, DH_2, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ECT2_HUMAN
Accessionⁱ	Q9H8V3Primary (citable) accession number: Q9H8V3 Secondary accession number(s): Q0MT80 , Q2M269, Q6U836, Q9NSV8, Q9NVW9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
	Last sequence update:	November 16, 2011
	Last modified:	August 12, 2020
	This is version 171 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM

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UniProtKB - Q9H8V3 (ECT2_HUMAN)

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Protein ECT2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Keywords - Diseasei

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<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

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<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Q9H8V3

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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Keywords - Domaini

Phylogenomic databases

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<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

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Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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Sequence databases

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Protein-protein interaction databases

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Protocols and materials databases

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Miscellaneous databases

Gene expression databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ