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Protein

Moesin

Gene

Msn

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

Functioni

Probably involved in connections of major cytoskeletal structures to the plasma membrane.

Enzyme regulationi

A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Moesin
Alternative name(s):
Membrane-organizing extension spike protein
Gene namesi
Name:Msn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:97167. Msn.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Apical cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
  • Cell projectionmicrovillus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

  • Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity).By similarity

GO - Cellular componenti

  • apical part of cell Source: MGI
  • apical plasma membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • blood microparticle Source: MGI
  • cell periphery Source: MGI
  • cytoplasm Source: MGI
  • cytoskeleton Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • extrinsic component of membrane Source: InterPro
  • filopodium Source: MGI
  • focal adhesion Source: MGI
  • microvillus Source: MGI
  • microvillus membrane Source: UniProtKB-SubCell
  • myelin sheath Source: UniProtKB
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • uropod Source: MGI
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi558 – 5581T → A: Diminishes the number of microvilli-like structures. 1 Publication
Mutagenesisi558 – 5581T → D: No effect on microvilli-like structures. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 577576MoesinPRO_0000219417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei83 – 831N6-succinyllysineBy similarity
Modified residuei116 – 1161Phosphotyrosine1 Publication
Modified residuei117 – 1171S-nitrosocysteineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei146 – 1461PhosphotyrosineBy similarity
Modified residuei165 – 1651N6-acetyllysine1 Publication
Modified residuei558 – 5581Phosphothreonine; by ROCK2 and STK102 Publications

Post-translational modificationi

Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization (By similarity). Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding.By similarity2 Publications
S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP26041.
PaxDbiP26041.
PRIDEiP26041.

PTM databases

PhosphoSiteiP26041.

Expressioni

Gene expression databases

BgeeiP26041.
CleanExiMM_MSN.
ExpressionAtlasiP26041. baseline and differential.
GenevisibleiP26041. MM.

Interactioni

Subunit structurei

Binds SLC9A3R1 (By similarity). In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts with PPP1R16B (By similarity). Interacts with PDZD8 (By similarity). Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG (By similarity).By similarity

Protein-protein interaction databases

BioGridi201534. 2 interactions.
IntActiP26041. 5 interactions.
MINTiMINT-4996580.
STRINGi10090.ENSMUSP00000113071.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Beta strandi15 – 206Combined sources
Helixi26 – 3712Combined sources
Helixi42 – 443Combined sources
Beta strandi45 – 517Combined sources
Beta strandi56 – 583Combined sources
Helixi65 – 673Combined sources
Beta strandi74 – 8411Combined sources
Helixi89 – 924Combined sources
Helixi96 – 11116Combined sources
Helixi119 – 13416Combined sources
Turni139 – 1413Combined sources
Turni144 – 1496Combined sources
Helixi155 – 1606Combined sources
Helixi165 – 17814Combined sources
Turni179 – 1813Combined sources
Helixi184 – 19512Combined sources
Turni199 – 2024Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2443Combined sources
Beta strandi245 – 2517Combined sources
Beta strandi254 – 2618Combined sources
Beta strandi267 – 2704Combined sources
Helixi274 – 29421Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YL8X-ray1.50A1-297[»]
ProteinModelPortaliP26041.
SMRiP26041. Positions 3-577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 295294FERMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi115 – 1206[IL]-x-C-x-x-[DE] motifBy similarity

Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236035.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26041.
KOiK05763.
OMAiHKKMERA.
OrthoDBiEOG7BGHK6.
PhylomeDBiP26041.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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]

Sequencei

Sequence statusi: Complete.

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

P26041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ
60 70 80 90 100
DTKAFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR
110 120 130 140 150
LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD
160 170 180 190 200
KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM
210 220 230 240 250
YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF
260 270 280 290 300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
310 320 330 340 350
EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK
360 370 380 390 400
LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK
410 420 430 440 450
EALLQASRDQ KKTQEQLASE MAELTARISQ LEMARKKKES EAVEWQQKAQ
460 470 480 490 500
MVQEDLEKTR AELKTAMSTP HVAEPAENEH DEQDENGAEA SAELRADAMA
510 520 530 540 550
KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR
560 570
LGRDKYKTLR QIRQGNTKQR IDEFESM
Length:577
Mass (Da):67,767
Last modified:January 23, 2007 - v3
Checksum:i4E9B5521313EF5B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3322EL → DV in AAA39728 (PubMed:1573844).Curated
Sequence conflicti371 – 3722RA → SP in AAA39728 (PubMed:1573844).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S47577 mRNA. Translation: AAA11762.1.
AK031171 mRNA. Translation: BAC27288.1.
AK088336 mRNA. Translation: BAC40290.1.
AK133819 mRNA. Translation: BAE21861.1.
AK145746 mRNA. Translation: BAE26623.1.
AK150869 mRNA. Translation: BAE29920.1.
AK153210 mRNA. Translation: BAE31809.1.
AL805963 Genomic DNA. Translation: CAM27501.1.
BC047366 mRNA. Translation: AAH47366.1.
M86390 mRNA. Translation: AAA39728.1.
CCDSiCCDS53139.1.
RefSeqiNP_034963.2. NM_010833.2.
UniGeneiMm.138876.

Genome annotation databases

EnsembliENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207.
GeneIDi17698.
KEGGimmu:17698.
UCSCiuc009tug.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S47577 mRNA. Translation: AAA11762.1.
AK031171 mRNA. Translation: BAC27288.1.
AK088336 mRNA. Translation: BAC40290.1.
AK133819 mRNA. Translation: BAE21861.1.
AK145746 mRNA. Translation: BAE26623.1.
AK150869 mRNA. Translation: BAE29920.1.
AK153210 mRNA. Translation: BAE31809.1.
AL805963 Genomic DNA. Translation: CAM27501.1.
BC047366 mRNA. Translation: AAH47366.1.
M86390 mRNA. Translation: AAA39728.1.
CCDSiCCDS53139.1.
RefSeqiNP_034963.2. NM_010833.2.
UniGeneiMm.138876.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YL8X-ray1.50A1-297[»]
ProteinModelPortaliP26041.
SMRiP26041. Positions 3-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201534. 2 interactions.
IntActiP26041. 5 interactions.
MINTiMINT-4996580.
STRINGi10090.ENSMUSP00000113071.

PTM databases

PhosphoSiteiP26041.

Proteomic databases

MaxQBiP26041.
PaxDbiP26041.
PRIDEiP26041.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207.
GeneIDi17698.
KEGGimmu:17698.
UCSCiuc009tug.1. mouse.

Organism-specific databases

CTDi4478.
MGIiMGI:97167. Msn.

Phylogenomic databases

eggNOGiNOG236035.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26041.
KOiK05763.
OMAiHKKMERA.
OrthoDBiEOG7BGHK6.
PhylomeDBiP26041.
TreeFamiTF313935.

Miscellaneous databases

ChiTaRSiMsn. mouse.
NextBioi292286.
PROiP26041.
SOURCEiSearch...

Gene expression databases

BgeeiP26041.
CleanExiMM_MSN.
ExpressionAtlasiP26041. baseline and differential.
GenevisibleiP26041. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites."
    Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S.
    J. Cell Sci. 103:131-143(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Forelimb and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Moesin, a new cytoskeletal protein and constituent of filopodia: its role in cellular functions."
    Furthmayr H., Lankes W.T., Amieva M.R.
    Kidney Int. 41:665-670(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-577.
  6. "Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures."
    Oshiro N., Fukata Y., Kaibuchi K.
    J. Biol. Chem. 273:34663-34666(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-558, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-558.
  7. "Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association."
    Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S.
    J. Cell Biol. 140:647-657(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-558, ENZYME REGULATION.
  8. "Negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly."
    Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H., Miyazaki M., Nakajima N., Okada M., Saito T.
    J. Immunol. 168:541-544(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SLC9A3R1 AND PAG1.
  9. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiMOES_MOUSE
AccessioniPrimary (citable) accession number: P26041
Secondary accession number(s): B1AX70, Q3UL28, Q8BSN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 137 of the entry and version 3 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.