GenomeNet

Database: UniProt
Entry: Q9H329
LinkDB: Q9H329
Original site: Q9H329 
ID   E41LB_HUMAN             Reviewed;         900 AA.
AC   Q9H329; Q5T4G5; Q5T4G6; Q9H328; Q9P2V3;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   20-JAN-2016, entry version 121.
DE   RecName: Full=Band 4.1-like protein 4B;
DE   AltName: Full=FERM-containing protein CG1;
DE   AltName: Full=Protein EHM2;
GN   Name=EPB41L4B; Synonyms=EHM2, LULU2 {ECO:0000303|PubMed:22006950};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT THR-816.
RX   PubMed=10603000; DOI=10.1007/s003350010017;
RA   Chadwick B.P., Leyne M., Gill S., Liebert C.B., Mull J., Mezey E.,
RA   Robbins C.M., Pinkett H.W., Makalowska I., Maayan C., Blumenfeld A.,
RA   Axelrod F.B., Brownstein M., Gusella J.F., Slaugenhaupt S.A.;
RT   "Cloning, mapping, and expression of a novel brain-specific transcript
RT   in the familial dysautonomia candidate region on chromosome 9q31.";
RL   Mamm. Genome 11:81-83(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=10783258; DOI=10.1006/geno.2000.6154;
RA   Shimizu K., Nagamachi Y., Tani M., Kimura K., Shiroishi T., Wakana S.,
RA   Yokota J.;
RT   "Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, Ehm2, that
RT   is expressed in high-metastatic K1735 murine melanoma cells.";
RL   Genomics 65:113-120(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14521927; DOI=10.1016/j.bbrc.2003.08.147;
RA   Chauhan S., Pandey R., Way J.F., Sroka T.C., Demetriou M.C., Kunz S.,
RA   Cress A.E., Mount D.W., Miesfeld R.L.;
RT   "Androgen regulation of the human FERM domain encoding gene EHM2 in a
RT   cell model of steroid-induced differentiation.";
RL   Biochem. Biophys. Res. Commun. 310:421-432(2003).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22006950; DOI=10.1083/jcb.201104118;
RA   Nakajima H., Tanoue T.;
RT   "Lulu2 regulates the circumferential actomyosin tensile system in
RT   epithelial cells through p114RhoGEF.";
RL   J. Cell Biol. 195:245-261(2011).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23664528; DOI=10.1016/j.jdermsci.2013.04.008;
RA   Bosanquet D.C., Ye L., Harding K.G., Jiang W.G.;
RT   "Expressed in high metastatic cells (Ehm2) is a positive regulator of
RT   keratinocyte adhesion and motility: The implication for wound
RT   healing.";
RL   J. Dermatol. Sci. 71:115-121(2013).
CC   -!- FUNCTION: Up-regulates the activity of the Rho guanine nucleotide
CC       exchange factor ARHGEF18 (By similarity). Involved in the
CC       regulation of the circumferential actomyosin belt in epithelial
CC       cells (PubMed:22006950). Promotes cellular adhesion, migration and
CC       motility in vitro and may play a role in wound healing
CC       (PubMed:23664528). May have a role in mediating cytoskeletal
CC       changes associated with steroid-induced cell differentiation
CC       (PubMed:14521927). {ECO:0000250|UniProtKB:Q9JMC8,
CC       ECO:0000269|PubMed:14521927, ECO:0000269|PubMed:22006950,
CC       ECO:0000269|PubMed:23664528}.
CC   -!- SUBUNIT: Interacts (via FERM domain) with ARHGEF18 (via C-
CC       terminus); the interaction activates ARHGEF18.
CC       {ECO:0000250|UniProtKB:Q9JMC8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22006950}.
CC       Cell junction, tight junction {ECO:0000269|PubMed:22006950}.
CC       Note=Accumulates along apical cell-cell boundaries and is also
CC       detected in the cytoplasm in a punctate manner.
CC       {ECO:0000269|PubMed:22006950}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H329-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H329-2; Sequence=VSP_007202, VSP_007203;
CC   -!- TISSUE SPECIFICITY: Expressed at higher levels in acute wounds
CC       than chronic wounds with increased expression in healing wounds,
CC       especially at the leading wound edge (PubMed:23664528). Isoform 1
CC       is highly expressed in brain. Isoform 2 is highly expressed in
CC       testis with lower levels in prostate and breast (PubMed:14521927).
CC       {ECO:0000269|PubMed:14521927, ECO:0000269|PubMed:23664528}.
CC   -!- INDUCTION: By the androgen dihydrotestosterone (DHT).
CC       {ECO:0000269|PubMed:14521927}.
CC   -!- PTM: May be negatively regulated by phosphorylation.
CC       {ECO:0000250|UniProtKB:Q9JMC8}.
CC   -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00084}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG43366.1; Type=Frameshift; Positions=19, 35, 870; Evidence={ECO:0000305};
CC       Sequence=AAG43368.1; Type=Frameshift; Positions=19, 35; Evidence={ECO:0000305};
DR   EMBL; AF153416; AAG43366.1; ALT_FRAME; mRNA.
DR   EMBL; AF153418; AAG43368.1; ALT_FRAME; mRNA.
DR   EMBL; AB032179; BAA96079.2; -; mRNA.
DR   EMBL; AL359963; CAH71092.1; -; Genomic_DNA.
DR   EMBL; AL358815; CAH71092.1; JOINED; Genomic_DNA.
DR   EMBL; AL359963; CAH71093.1; -; Genomic_DNA.
DR   EMBL; AL358815; CAH71093.1; JOINED; Genomic_DNA.
DR   EMBL; AL358815; CAI15130.1; -; Genomic_DNA.
DR   EMBL; AL359963; CAI15130.1; JOINED; Genomic_DNA.
DR   EMBL; AL358815; CAI15129.1; -; Genomic_DNA.
DR   EMBL; AL359963; CAI15129.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS43859.1; -. [Q9H329-1]
DR   CCDS; CCDS43860.1; -. [Q9H329-2]
DR   RefSeq; NP_060894.2; NM_018424.3. [Q9H329-2]
DR   RefSeq; NP_061987.3; NM_019114.4. [Q9H329-1]
DR   UniGene; Hs.591901; -.
DR   ProteinModelPortal; Q9H329; -.
DR   SMR; Q9H329; 84-367.
DR   BioGrid; 120044; 4.
DR   IntAct; Q9H329; 12.
DR   STRING; 9606.ENSP00000363694; -.
DR   iPTMnet; Q9H329; -.
DR   PhosphoSite; Q9H329; -.
DR   BioMuta; EPB41L4B; -.
DR   DMDM; 209572611; -.
DR   MaxQB; Q9H329; -.
DR   PaxDb; Q9H329; -.
DR   PRIDE; Q9H329; -.
DR   Ensembl; ENST00000374557; ENSP00000363685; ENSG00000095203. [Q9H329-2]
DR   Ensembl; ENST00000374566; ENSP00000363694; ENSG00000095203. [Q9H329-1]
DR   GeneID; 54566; -.
DR   KEGG; hsa:54566; -.
DR   UCSC; uc004bdz.1; human. [Q9H329-1]
DR   UCSC; uc004bea.3; human. [Q9H329-2]
DR   CTD; 54566; -.
DR   GeneCards; EPB41L4B; -.
DR   HGNC; HGNC:19818; EPB41L4B.
DR   HPA; HPA042862; -.
DR   MIM; 610340; gene.
DR   neXtProt; NX_Q9H329; -.
DR   PharmGKB; PA134986250; -.
DR   eggNOG; ENOG410IQ5Y; Eukaryota.
DR   eggNOG; ENOG410YG1S; LUCA.
DR   GeneTree; ENSGT00760000118823; -.
DR   HOGENOM; HOG000231632; -.
DR   HOVERGEN; HBG051434; -.
DR   InParanoid; Q9H329; -.
DR   OMA; DPNVRSP; -.
DR   OrthoDB; EOG73FQM2; -.
DR   PhylomeDB; Q9H329; -.
DR   TreeFam; TF319780; -.
DR   ChiTaRS; EPB41L4B; human.
DR   GenomeRNAi; 54566; -.
DR   NextBio; 57050; -.
DR   PRO; PR:Q9H329; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; Q9H329; -.
DR   CleanEx; HS_EPB41L4B; -.
DR   Genevisible; Q9H329; HS.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR   GO; GO:0031032; P:actomyosin structure organization; IDA:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IDA:UniProtKB.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR030698; Band4.1-like4B.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_dom-like.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   PANTHER; PTHR23280:SF18; PTHR23280:SF18; 2.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF50729; SSF50729; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell junction; Complete proteome; Cytoplasm;
KW   Phosphoprotein; Polymorphism; Reference proteome; Tight junction.
FT   CHAIN         1    900       Band 4.1-like protein 4B.
FT                                /FTId=PRO_0000219404.
FT   DOMAIN       85    369       FERM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00084}.
FT   COMPBIAS    504    517       His-rich.
FT   VAR_SEQ     470    518       SYPLPSPVLSSSDRLPFGIEENGGTPFLTAASGRHHHQHQH
FT                                QHQHQHHS -> RPSFQDDRSHWKASASGDDSHFDYVHDQN
FT                                QKNLGGMQSMMYRDKLMTAL (in isoform 2).
FT                                {ECO:0000303|PubMed:10603000,
FT                                ECO:0000303|PubMed:10783258}.
FT                                /FTId=VSP_007202.
FT   VAR_SEQ     519    900       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10603000,
FT                                ECO:0000303|PubMed:10783258}.
FT                                /FTId=VSP_007203.
FT   VARIANT     816    816       N -> T (in dbSNP:rs3750450).
FT                                {ECO:0000269|PubMed:10603000}.
FT                                /FTId=VAR_048356.
FT   CONFLICT     73     73       V -> M (in Ref. 2; BAA96079).
FT                                {ECO:0000305}.
FT   CONFLICT    899    899       E -> R (in Ref. 1; AAG43366).
FT                                {ECO:0000305}.
SQ   SEQUENCE   900 AA;  99712 MW;  9A4BD658DBE65BDE CRC64;
     MLRFLRRTFG RRSMQRYARG AAGRGAAGLG DERDGGPRGG PAAAASSSAL PAAPGGSVFP
     AGGGPLLTGG AAVHISAAGA AKATLYCRVF LLDGTEVSVD LPKHAKGQDL FDQIVYHLDL
     VETDYFGLQF LDSAQVAHWL DHAKPIKKQM KIGPAYALHF RVKYYSSEPN NLREEFTRYL
     FVLQLRHDIL SGKLKCPYET AVELAALCLQ AELGECELPE HTPELVSEFR FIPNQTEAME
     FDIFQRWKEC RGKSPAQAEL SYLNKAKWLE MYGVDMHVVR GRDGCEYSLG LTPTGILIFE
     GANKIGLFFW PKITKMDFKK SKLTLVVVED DDQGREQEHT FVFRLDSART CKHLWKCAVE
     HHAFFRLRTP GNSKSNRSDF IRLGSRFRFS GRTEYQATHG SRLRRTSTFE RKPSKRYPSR
     RHSTFKASNP VIAAQLCSKT NPEVHNYQPQ YHPNIHPSQP RWHPHSPNVS YPLPSPVLSS
     SDRLPFGIEE NGGTPFLTAA SGRHHHQHQH QHQHQHHSNY SLSLTLENKE GPLRSPNSSS
     KSLTKLSPGT PALFSEAAAH LKKLELETVK AAGPWPPLHI NINKAEEKKV SEKTLQTPLL
     PSPVADHVKC NILKAQLENA SRVNIQGGKE ESPFVNINKK SSLQDASVRS PIPIRVETAQ
     PAVEKPEIKP PRVRKLTRQY SFDEDDLPPD LAEAVGVTTS TTTNTTTAAT QVSVPLPSPK
     VQNVSSPHKS EGKGLLSPGA KSPSDRGGAF TLEPGDLLMD FTEATPLAEP ASNPHCAHSR
     CSPPLSLPMK EETTGVCMYP PIKTRLIKTF PVDTMNPFPD TFTTGPQFTA DFRDSKLQCC
     PGPTSPLIPA ATLRPLTETV STVQTIYTTR KPVSLAASAE TLRQELEREK MMKRLLMTEL
//
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