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P10911 (MCF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene DBL
Alternative name(s):
Proto-oncogene MCF-2

Cleaved into the following 2 chains:

  1. MCF2-transforming protein
  2. DBL-transforming protein
Gene names
Name:MCF2
Synonyms:DBL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length925 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42.

Subunit structure

Interacts with an array of inositol phospholipids such as phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). May interact with CCPG1. Ref.13 Ref.14

Subcellular location

Cytoplasm Ref.13.

Isoform 1: Membrane.

Isoform 3: Membrane. Note: Colocalizes with CDC42 to plasma membrane. Ref.13

Tissue specificity

Isoform 1 is expressed only in brain. Isoform 3 is expressed in heart, kidney, spleen, liver and testis. Isoform 4 is expressed in brain, heart, kidney, testis, placenta, stomach and peripheral blood. The protein is detectable in brain, heart, kidney, intestine, muscle, lung and testis. Ref.3

Domain

The CRAL-TRIO domain is involved in interaction with inositol phospholipids. Ref.10 Ref.11 Ref.13

The DH domain is essential for transforming activity and directly catalyzes GDP-GTP exchange activity. It may interact with CCPG1. Ref.10 Ref.11 Ref.13

Post-translational modification

Phosphorylation by TNK2 enhances guanine nucleotide exchange factor (GEF) activity toward Rho family proteins.

Involvement in disease

MCF2 and DBL represent two activated versions of the same proto-oncogene.

Sequence similarities

Belongs to the MCF2 family.

Contains 1 CRAL-TRIO domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 spectrin repeat.

Sequence caution

The sequence AAA52172.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NME1P155314EBI-1914514,EBI-741141

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10911-1)

Also known as: Var.1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P10911-2)

Also known as: Var.2;

The sequence of this isoform differs from the canonical sequence as follows:
     842-860: KQQGAFISTEETELEHTST → DLCRRWLSYIDEATMSNGK
     861-925: Missing.
Isoform 3 (identifier: P10911-3)

Also known as: Var.3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MAEANPRRGKMRFRRNA → MQDIAFLSGG...SLKISLQKIS
Isoform 4 (identifier: P10911-4)

Also known as: Var.4;

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: Q → QVGVGYSFFQACKLFSK
Isoform 5 (identifier: P10911-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MAEANPRRGKMRFRRNA → MQDIAFLSGG...SLKISLQKIS
     454-454: Q → QVGVGYSFFQACKLFSK
Isoform 6 (identifier: P10911-6)

The sequence of this isoform differs from the canonical sequence as follows:
     58-96: Missing.
     842-860: KQQGAFISTEETELEHTST → DLCRRWLSYIDEATMSNGK
     861-925: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 925925Proto-oncogene DBL
PRO_0000030432
Chain398 – 925528MCF2-transforming protein
PRO_0000030433
Chain498 – 925428DBL-transforming protein
PRO_0000030434

Regions

Domain1 – 8888CRAL-TRIO
Repeat221 – 322102Spectrin
Domain495 – 675181DH
Domain687 – 809123PH

Natural variations

Alternative sequence1 – 1717MAEAN…FRRNA → MQDIAFLSGGRGKDNAWIIT FPENCNFRCIPEEVIAKVLT YLTSIARQNGSDSRFTIILD RRLDTWSSLKISLQKIS in isoform 3 and isoform 5.
VSP_008150
Alternative sequence58 – 9639Missing in isoform 6.
VSP_046118
Alternative sequence4541Q → QVGVGYSFFQACKLFSK in isoform 4 and isoform 5.
VSP_008153
Alternative sequence842 – 86019KQQGA…EHTST → DLCRRWLSYIDEATMSNGK in isoform 2 and isoform 6.
VSP_008151
Alternative sequence861 – 92565Missing in isoform 2 and isoform 6.
VSP_008152

Experimental info

Mutagenesis640 – 6467LLLKELL → IIIRDII: Transformation capability reduced; no stimulation of GDP dissociation.
Sequence conflict541L → P Ref.1
Sequence conflict541L → P Ref.3
Sequence conflict1781C → S in BAH12371. Ref.5
Sequence conflict3301L → F in BAH14787. Ref.5
Sequence conflict3581D → Y in BAH12371. Ref.5
Sequence conflict6341R → Q Ref.8
Sequence conflict6871N → I in BAH14787. Ref.5
Sequence conflict8861A → V Ref.9
Sequence conflict9001F → S in BAH13855. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Var.1) [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 96233C7AFC85D637

FASTA925107,673
        10         20         30         40         50         60 
MAEANPRRGK MRFRRNAASF PGNLHLVLVL RPTSFLQRTF TDIGFWFSQE DFMLKLPVVM 

        70         80         90        100        110        120 
LSSVSDLLTY IDDKQLTPEL GGTLQYCHSE WIIFRNAIEN FALTVKEMAQ MLQSFGTELA 

       130        140        150        160        170        180 
ETELPDDIPS IEEILAIRAE RYHLLKNDIT AVTKEGKILL TNLEVPDTEG AVSSRLECHR 

       190        200        210        220        230        240 
QISGDWQTIN KLLTQVHDME TAFDGFWEKH QLKMEQYLQL WKFEQDFQQL VTEVEFLLNQ 

       250        260        270        280        290        300 
QAELADVTGT IAQVKQKIKK LENLDENSQE LLSKAQFVIL HGHKLAANHH YALDLICQRC 

       310        320        330        340        350        360 
NELRYLSDIL VNEIKAKRIQ LSRTFKMHKL LQQARQCCDE GECLLANQEI DKFQSKEDAQ 

       370        380        390        400        410        420 
KALQDIENFL EMALPFINYE PETLQYEFDV ILSPELKVQM KTIQLKLENI RSIFENQQAG 

       430        440        450        460        470        480 
FRNLADKHVR PIQFVVPTPE NLVTSGTPFF SSKQGKKTWR QNQSNLKIEV VPDCQEKRSS 

       490        500        510        520        530        540 
GPSSSLDNGN SLDVLKNHVL NELIQTERVY VRELYTVLLG YRAEMDNPEM FDLMPPLLRN 

       550        560        570        580        590        600 
KKDILFGNMA EIYEFHNDIF LSSLENCAHA PERVGPCFLE RKDDFQMYAK YCQNKPRSET 

       610        620        630        640        650        660 
IWRKYSECAF FQECQRKLKH RLRLDSYLLK PVQRITKYQL LLKELLKYSK DCEGSALLKK 

       670        680        690        700        710        720 
ALDAMLDLLK SVNDSMHQIA INGYIGNLNE LGKMIMQGGF SVWIGHKKGA TKMKDLARFK 

       730        740        750        760        770        780 
PMQRHLFLYE KAIVFCKRRV ESGEGSDRYP SYSFKHCWKM DEVGITEYVK GDNRKFEIWY 

       790        800        810        820        830        840 
GEKEEVYIVQ ASNVDVKMTW LKEIRNILLK QQELLTVKKR KQQDQLTERD KFQISLQQND 

       850        860        870        880        890        900 
EKQQGAFIST EETELEHTST VVEVCEAIAS VQAEANTVWT EASQSAEISE EPAEWSSNYF 

       910        920 
YPTYDENEEE NRPLMRPVSE MALLY

« Hide

Isoform 2 (Var.2) [UniParc].

Checksum: CCD14CA833425027
Show »

FASTA860100,409
Isoform 3 (Var.3) [UniParc].

Checksum: 8D0C81505593C040
Show »

FASTA985114,376
Isoform 4 (Var.4) [UniParc].

Checksum: C5B1B4F9F368AC16
Show »

FASTA941109,436
Isoform 5 [UniParc].

Checksum: 8D7277D0703671B3
Show »

FASTA1,001116,139
Isoform 6 [UniParc].

Checksum: 4FAD1AAA126237A8
Show »

FASTA82195,940

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the human dbl proto-oncogene: evidence that its overexpression is sufficient to transform NIH/3T3 cells."
Ron D., Tronick S.R., Aaronson S.A., Eva A.
EMBO J. 7:2465-2473(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]Ron D.
Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Alternative splicing variants of the human DBL (MCF-2) proto-oncogene."
Komai K., Okayama R., Kitagawa M., Yagi H., Chihara K., Shiozawa S.
Biochem. Biophys. Res. Commun. 299:455-458(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, CHARACTERIZATION.
[4]Rhodes S., Huckle E.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"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. expand/collapse author list , 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] (ISOFORMS 5 AND 6).
Tissue: Testis and Thalamus.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The predicted DBL oncogene product defines a distinct class of transforming proteins."
Eva A., Vecchio G., Rao C.D., Tronick S.R., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 85:2061-2065(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 498-925 (ISOFORM 1).
[9]"Activation of a mcf.2 oncogene by deletion of amino-terminal coding sequences."
Noguchi T., Galland F., Batoz M., Mattei M.-G., Birnbaum D.
Oncogene 3:709-715(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 398-925 (ISOFORM 1).
[10]"A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr."
Ron D., Zannini M., Lewis M., Wickner R.B., Hunt L.T., Graziani G., Tronick S.R., Aaronson S.A., Eva A.
New Biol. 3:372-379(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN DBL-HOMOLOGY, MUTAGENESIS.
[11]"Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product."
Hart M.J., Eva A., Zangrilli D., Aaronson S.A., Evans T., Cerione R.A., Zheng Y.
J. Biol. Chem. 269:62-65(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF DBL DOMAIN.
[12]"Activation of the guanine nucleotide exchange factor Dbl following ACK1-dependent tyrosine phosphorylation."
Kato J., Kaziro Y., Satoh T.
Biochem. Biophys. Res. Commun. 268:141-147(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY TNK2.
[13]"Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites."
Ueda S., Kataoka T., Satoh T.
Cell. Signal. 16:899-906(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN CRAL-TRIO, INTERACTION WITH INOSITOL PHOSPHOLIPIDS.
[14]"Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INTERACTION WITH CCPG1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X12556 mRNA. Translation: CAA31069.1.
AB085901 mRNA. Translation: BAC41200.1.
AB085902 mRNA. Translation: BAC41201.1.
AL117234 mRNA. Translation: CAB55301.1.
AK296488 mRNA. Translation: BAH12371.1.
AK302957 mRNA. Translation: BAH13855.1.
AK316416 mRNA. Translation: BAH14787.1.
AL033403 Genomic DNA. Translation: CAA21955.1.
AL033403 Genomic DNA. Translation: CAI42107.1.
AL033403 Genomic DNA. Translation: CAI42108.1.
AL161777 Genomic DNA. No translation available.
CH471150 Genomic DNA. Translation: EAW88427.1.
CH471150 Genomic DNA. Translation: EAW88430.1.
J03639 mRNA. Translation: AAA52172.1. Different initiation.
X13230 mRNA. Translation: CAA31617.1. Sequence problems.
IPIIPI00339309.
IPI00339310.
IPI00339311.
IPI00339312.
IPI00641162.
IPI00955487.
IPI00981456.
PIRTVHUBD. A28051.
TVHUDB. A30040.
S10138.
RefSeqNP_001093325.1. NM_001099855.1.
NP_001165347.1. NM_001171876.1.
NP_001165348.1. NM_001171877.1.
NP_001165349.1. NM_001171878.1.
NP_001165350.1. NM_001171879.1.
NP_005360.3. NM_005369.4.
UniGeneHs.387262.

3D structure databases

ProteinModelPortalP10911.
ModBaseSearch...

Protein-protein interaction databases

IntActP10911. 1 interaction.
STRING9606.ENSP00000397055.

PTM databases

PhosphoSiteP10911.

Polymorphism databases

DMDM92087039.

Proteomic databases

PaxDbP10911.
PRIDEP10911.

Protocols and materials databases

DNASU4168.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338585; ENSP00000342204; ENSG00000101977.
ENST00000370573; ENSP00000359605; ENSG00000101977.
ENST00000370576; ENSP00000359608; ENSG00000101977.
ENST00000414978; ENSP00000397055; ENSG00000101977.
ENST00000519895; ENSP00000430276; ENSG00000101977.
ENST00000520602; ENSP00000427745; ENSG00000101977.
ENST00000536274; ENSP00000438155; ENSG00000101977.
GeneID4168.
KEGGhsa:4168.
UCSCuc004fau.3. human.
uc004fav.3. human.
uc004faw.2. human.
uc010nsh.2. human.

Organism-specific databases

CTD4168.
GeneCardsGC0XM138663.
HGNCHGNC:6940. MCF2.
HPACAB010423.
MIM311030. gene.
neXtProtNX_P10911.
PharmGKBPA30684.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315020.
HOVERGENHBG062385.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP10911.
BgeeP10911.
CleanExHS_MCF2.
GenevestigatorP10911.
GermOnlineENSG00000101977. Homo sapiens.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PfamPF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00150. SPEC. 1 hit.
[Graphical view]
SUPFAMSSF48065. DH-domain. 1 hit.
PROSITEPS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMCF2. human.
GenomeRNAi4168.
NextBio16414.
SOURCESearch...

Entry information

Entry nameMCF2_HUMAN
AccessionPrimary (citable) accession number: P10911
Secondary accession number(s): B7Z3Y5 expand/collapse secondary AC list , B7Z869, B7ZAV1, E9PH77, F5H091, P14919, Q5JYJ2, Q5JYJ3, Q5JYJ4, Q8IUF3, Q8IUF4, Q9UJB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 7, 2006
Last modified: May 1, 2013
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

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Human chromosome X: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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