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P46662

- MERL_MOUSE

UniProt

P46662 - MERL_MOUSE

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Protein

Merlin

Gene
Nf2, Nf-2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex By similarity. Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.1 Publication

GO - Molecular functioni

  1. protein binding Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. brain development Source: MGI
  3. cell-cell junction organization Source: MGI
  4. ectoderm development Source: MGI
  5. hippocampus development Source: MGI
  6. lens fiber cell differentiation Source: UniProtKB
  7. mesoderm formation Source: MGI
  8. negative regulation of cell-cell adhesion Source: Ensembl
  9. negative regulation of cell proliferation Source: MGI
  10. negative regulation of DNA replication Source: Ensembl
  11. negative regulation of MAPK cascade Source: MGI
  12. negative regulation of protein kinase activity Source: MGI
  13. negative regulation of tyrosine phosphorylation of Stat3 protein Source: Ensembl
  14. negative regulation of tyrosine phosphorylation of Stat5 protein Source: Ensembl
  15. odontogenesis of dentin-containing tooth Source: MGI
  16. positive regulation of cell differentiation Source: MGI
  17. positive regulation of stress fiber assembly Source: Ensembl
  18. regulation of cell proliferation Source: MGI
  19. regulation of hippo signaling Source: Ensembl
  20. regulation of neural precursor cell proliferation Source: MGI
  21. regulation of protein localization to nucleus Source: MGI
  22. regulation of protein stability Source: MGI
  23. Schwann cell proliferation Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Merlin
Alternative name(s):
Moesin-ezrin-radixin-like protein
Neurofibromin-2
Schwannomin
Gene namesi
Name:Nf2
Synonyms:Nf-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97307. Nf2.

Subcellular locationi

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection By similarity. Cytoplasmcytoskeleton By similarity. Nucleus By similarity
Note: Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with VPRBP in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions By similarity.

GO - Cellular componenti

  1. adherens junction Source: MGI
  2. apical part of cell Source: MGI
  3. cleavage furrow Source: MGI
  4. cortical actin cytoskeleton Source: MGI
  5. cytoplasm Source: MGI
  6. cytoskeleton Source: MGI
  7. early endosome Source: Ensembl
  8. extrinsic component of membrane Source: InterPro
  9. filopodium Source: MGI
  10. lamellipodium Source: MGI
  11. nucleolus Source: Ensembl
  12. nucleus Source: MGI
  13. perinuclear region of cytoplasm Source: Ensembl
  14. plasma membrane Source: UniProtKB-SubCell
  15. ruffle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are born with abnormally small lenses with serious structural defects. Failure of lens vesicle separation and the resulting changes in cell organization causes lenses to herniate, leading to expulsion of lens fiber cells through a perforation in the cornea. Developing lenses show loss of cell apical-basal polarity, failure of the lens vesicle to separate from the surface ectoderm, failure to properly exit the cell cycle during fiber cell differentiation and incomplete terminal differentiation of fiber cells.1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 596596MerlinPRO_0000219413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei518 – 5181Phosphoserine; by PAK By similarity

Post-translational modificationi

Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail By similarity.
Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP46662.
PaxDbiP46662.
PRIDEiP46662.

PTM databases

PhosphoSiteiP46662.

Expressioni

Gene expression databases

ArrayExpressiP46662.
BgeeiP46662.
CleanExiMM_NF2.
GenevestigatoriP46662.

Interactioni

Subunit structurei

Interacts with SLC9A3R1, HGS and AGAP2. Interacts with SGSM3. Interacts (via FERM domain) with MPP1 By similarity. Interacts with LAYN and WWC1. Interacts with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1 By similarity.1 Publication

Protein-protein interaction databases

BioGridi201737. 4 interactions.
IntActiP46662. 5 interactions.
MINTiMINT-242068.

Structurei

Secondary structure

1
596
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 277
Beta strandi32 – 387
Helixi43 – 5412
Helixi59 – 613
Beta strandi62 – 687
Beta strandi71 – 744
Beta strandi77 – 804
Helixi81 – 833
Beta strandi89 – 10012
Helixi105 – 1084
Helixi112 – 12716
Helixi135 – 15016
Turni155 – 1573
Turni160 – 1656
Helixi171 – 1766
Helixi181 – 19212
Helixi193 – 1953
Helixi200 – 21112
Turni215 – 2184
Beta strandi220 – 2267
Beta strandi231 – 2366
Beta strandi238 – 2458
Beta strandi248 – 2514
Beta strandi253 – 2575
Helixi258 – 2603
Beta strandi261 – 2677
Beta strandi270 – 2778
Turni278 – 2803
Beta strandi283 – 2864
Helixi290 – 30920
Helixi316 – 33722

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISNX-ray2.90A18-340[»]
3WA0X-ray2.31A/B/C/D/E/F19-314[»]
4P7IX-ray2.60A/B1-313[»]
ProteinModelPortaliP46662.
SMRiP46662. Positions 18-382.

Miscellaneous databases

EvolutionaryTraceiP46662.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 311290FERMAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi327 – 465139Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 FERM domain.

Phylogenomic databases

eggNOGiNOG328202.
GeneTreeiENSGT00650000092953.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP46662.
KOiK16684.
OMAiITNEMER.
OrthoDBiEOG7BGHK6.
PhylomeDBiP46662.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin_like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_like_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P46662-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV    50
CRTLGLRETW FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF 100
YPENAEEELV QEITQHLFFL QVKKQILDEK VYCPPEASVL LASYAVQAKY 150
GDYDPSVHKR GFLAQEELLP KRVINLYQMT PEMWEERITA WYAEHRGRAR 200
DEAEMEYLKI AQDLEMYGVN YFTIRNKKGT ELLLGVDALG LHIYDPENRL 250
TPKISFPWNE IRNISYSDKE FTIKPLDKKI DVFKFNSSKL RVNKLILQLC 300
IGNHDLFMRR RKADSLEVQQ MKAQAREEKA RKQMERQRLA REKQMREEAE 350
RTRDELERRL LQMKEEATMA NEALMRSEET ADLLAEKAQI TEEEAKLLAQ 400
KAAEAEQEMQ RIKATAIRTE EEKRLMEQKV LEAEVLALKM AEESERRAKE 450
ADQLKQDLQE AREAERRAKQ KLLEIATKPT YPPMNPIPPP LPPDIPSFDI 500
IADSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN ELKTEIEALK 550
LKERETALDV LHSESSDRGG PSSKHNTIKK LTLQSAKSRV AFFEEL 596
Length:596
Mass (Da):69,776
Last modified:June 27, 2003 - v2
Checksum:i8D06F557E3435851
GO
Isoform 2 (identifier: P46662-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     581-596: LTLQSAKSRVAFFEEL → PQAQGRRPICI

Show »
Length:591
Mass (Da):69,176
Checksum:i20B97F99EBF87184
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei581 – 59616LTLQS…FFEEL → PQAQGRRPICI in isoform 2. VSP_000493Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti475 – 4751I → T in AAA39808. 1 Publication
Sequence conflicti554 – 5541R → A in AAA39807. 1 Publication
Sequence conflicti554 – 5541R → A in AAA63648. 1 Publication
Sequence conflicti570 – 5701G → A in AAA39808. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74671 mRNA. Translation: CAA52737.1.
L27105 mRNA. Translation: AAA39807.1.
L27090 mRNA. Translation: AAA63648.1.
L28176 mRNA. Translation: AAA39808.1.
AK045998 mRNA. Translation: BAC32567.1.
X75759 mRNA. Translation: CAA53386.1.
CCDSiCCDS24391.1. [P46662-1]
CCDS56757.1. [P46662-2]
PIRiI48683.
I54368.
I68664.
RefSeqiNP_001239179.1. NM_001252250.1. [P46662-2]
NP_001239180.1. NM_001252251.1. [P46662-2]
NP_001239181.1. NM_001252252.1.
NP_001239182.1. NM_001252253.1.
NP_035028.2. NM_010898.4. [P46662-1]
XP_006514633.1. XM_006514570.1. [P46662-2]
UniGeneiMm.297109.

Genome annotation databases

EnsembliENSMUST00000053079; ENSMUSP00000055033; ENSMUSG00000009073. [P46662-2]
ENSMUST00000056290; ENSMUSP00000055061; ENSMUSG00000009073. [P46662-2]
ENSMUST00000109910; ENSMUSP00000105536; ENSMUSG00000009073. [P46662-1]
GeneIDi18016.
KEGGimmu:18016.
UCSCiuc007hvf.2. mouse. [P46662-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74671 mRNA. Translation: CAA52737.1 .
L27105 mRNA. Translation: AAA39807.1 .
L27090 mRNA. Translation: AAA63648.1 .
L28176 mRNA. Translation: AAA39808.1 .
AK045998 mRNA. Translation: BAC32567.1 .
X75759 mRNA. Translation: CAA53386.1 .
CCDSi CCDS24391.1. [P46662-1 ]
CCDS56757.1. [P46662-2 ]
PIRi I48683.
I54368.
I68664.
RefSeqi NP_001239179.1. NM_001252250.1. [P46662-2 ]
NP_001239180.1. NM_001252251.1. [P46662-2 ]
NP_001239181.1. NM_001252252.1.
NP_001239182.1. NM_001252253.1.
NP_035028.2. NM_010898.4. [P46662-1 ]
XP_006514633.1. XM_006514570.1. [P46662-2 ]
UniGenei Mm.297109.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ISN X-ray 2.90 A 18-340 [» ]
3WA0 X-ray 2.31 A/B/C/D/E/F 19-314 [» ]
4P7I X-ray 2.60 A/B 1-313 [» ]
ProteinModelPortali P46662.
SMRi P46662. Positions 18-382.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201737. 4 interactions.
IntActi P46662. 5 interactions.
MINTi MINT-242068.

PTM databases

PhosphoSitei P46662.

Proteomic databases

MaxQBi P46662.
PaxDbi P46662.
PRIDEi P46662.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000053079 ; ENSMUSP00000055033 ; ENSMUSG00000009073 . [P46662-2 ]
ENSMUST00000056290 ; ENSMUSP00000055061 ; ENSMUSG00000009073 . [P46662-2 ]
ENSMUST00000109910 ; ENSMUSP00000105536 ; ENSMUSG00000009073 . [P46662-1 ]
GeneIDi 18016.
KEGGi mmu:18016.
UCSCi uc007hvf.2. mouse. [P46662-1 ]

Organism-specific databases

CTDi 4771.
MGIi MGI:97307. Nf2.

Phylogenomic databases

eggNOGi NOG328202.
GeneTreei ENSGT00650000092953.
HOGENOMi HOG000007113.
HOVERGENi HBG002185.
InParanoidi P46662.
KOi K16684.
OMAi ITNEMER.
OrthoDBi EOG7BGHK6.
PhylomeDBi P46662.
TreeFami TF313935.

Miscellaneous databases

ChiTaRSi NF2. mouse.
EvolutionaryTracei P46662.
NextBioi 293053.
PROi P46662.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46662.
Bgeei P46662.
CleanExi MM_NF2.
Genevestigatori P46662.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin_like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_like_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF002305. ERM. 1 hit.
PRINTSi PR00935. BAND41.
PR00661. ERMFAMILY.
SMARTi SM00295. B41. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The murine NF2 homologue encodes a highly conserved merlin protein with alternative forms."
    Haase V.H., Trofatter J.A., Maccollin M., Tarttelin E., Gusella J.F., Ramesh V.
    Hum. Mol. Genet. 3:407-411(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Alternative transcripts in the mouse neurofibromatosis type 2 (NF2) gene are conserved and code for schwannomins with distinct C-terminal domains."
    Huynh D.P., Nechiporuk T., Pulst S.M.
    Hum. Mol. Genet. 3:1075-1079(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "The mouse neurofibromatosis type 2 gene maps to chromosome 11."
    Claudio J.O., Marineau C., Rouleau G.A.
    Genomics 21:437-439(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 400-596.
    Tissue: Brain.
  5. "Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin."
    Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T., Hynes R.O.
    Exp. Cell Res. 308:177-187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAYN.
  6. "The tumor suppressor merlin is required for cell cycle exit, terminal differentiation, and cell polarity in the developing murine lens."
    Wiley L.A., Dattilo L.K., Kang K.B., Giovannini M., Beebe D.C.
    Invest. Ophthalmol. Vis. Sci. 51:3611-3618(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMERL_MOUSE
AccessioniPrimary (citable) accession number: P46662
Secondary accession number(s): Q8BR03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 27, 2003
Last modified: September 3, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi