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Protein

Afadin

Gene

Mllt4

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

Functioni

Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm.1 Publication

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • Ras GTPase binding Source: MGI

GO - Biological processi

  • adherens junction maintenance Source: MGI
  • brain morphogenesis Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cerebral cortex development Source: MGI
  • establishment of endothelial intestinal barrier Source: MGI
  • homeostasis of number of cells Source: MGI
  • neuroepithelial cell differentiation Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • radial glial cell differentiation Source: MGI
  • regulation of oligodendrocyte progenitor proliferation Source: MGI
  • signal transduction Source: InterPro
  • telencephalon development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Afadin
Alternative name(s):
Protein Af-6
Gene namesi
Name:Mllt4
Synonyms:Af6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1314653. Mllt4.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: MGI
  • apical part of cell Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Disruption phenotypei

Mice show developmental defects at stages during and after gastrulation, including disorganization of the ectoderm, impaired migration of the mesoderm and loss of somites and other structures derived from both the ectoderm and mesoderm. Cell-cell adherens juntions and tight junctions are improperly organized in the ectoderm-derived cells. No redundancy exists in the function of afadin during gastrulation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18201820AfadinPRO_0000215919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161PhosphoserineCombined sources
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei256 – 2561PhosphoserineBy similarity
Modified residuei391 – 3911PhosphoserineBy similarity
Modified residuei424 – 4241PhosphoserineBy similarity
Modified residuei512 – 5121PhosphoserineBy similarity
Modified residuei557 – 5571PhosphoserineCombined sources
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei655 – 6551PhosphoserineBy similarity
Modified residuei1083 – 10831PhosphoserineCombined sources
Modified residuei1107 – 11071PhosphoserineCombined sources
Modified residuei1126 – 11261PhosphoserineCombined sources
Modified residuei1140 – 11401PhosphoserineBy similarity
Modified residuei1143 – 11431PhosphoserineCombined sources
Modified residuei1172 – 11721PhosphoserineCombined sources
Modified residuei1173 – 11731PhosphoserineBy similarity
Modified residuei1182 – 11821PhosphoserineCombined sources
Modified residuei1199 – 11991PhosphoserineBy similarity
Modified residuei1232 – 12321PhosphothreonineBy similarity
Modified residuei1238 – 12381PhosphoserineBy similarity
Modified residuei1275 – 12751PhosphoserineBy similarity
Modified residuei1328 – 13281PhosphoserineBy similarity
Modified residuei1330 – 13301PhosphothreonineBy similarity
Modified residuei1499 – 14991PhosphoserineBy similarity
Modified residuei1510 – 15101PhosphoserineCombined sources
Modified residuei1694 – 16941PhosphoserineBy similarity
Modified residuei1719 – 17191PhosphoserineCombined sources
Modified residuei1770 – 17701PhosphoserineCombined sources
Modified residuei1795 – 17951PhosphoserineCombined sources
Modified residuei1803 – 18031N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QZQ1.
PaxDbiQ9QZQ1.
PeptideAtlasiQ9QZQ1.
PRIDEiQ9QZQ1.

PTM databases

iPTMnetiQ9QZQ1.
PhosphoSiteiQ9QZQ1.

Expressioni

Tissue specificityi

Isoform 1 is expressed only in a restricted set of epithelial structures during early embryogenesis.1 Publication

Developmental stagei

Highly expressed at restricted set of epithelial structures and highly concentrated at their junctional complex regions. At E6.5, localized at the most apical regions of cell-cell adhesion sites of the entire embryonic ectoderm; not detected in the extraembryonic regions. At E7.0, expressed in the primitive streak and the migrating paraxial mesoderm. At E7.5, highly expressed at the junctional complex regions in the primitive streak region (neuroepithelium) and the neural fold/grove region, but hardly detected in other areas of the ectoderm. By E8.5, highly expressed in the tail bud, somites and the paraxial mesoderm, concentrated at the junctional complex regions in neural tube, somites and pericardioperitoneal canal.1 Publication

Gene expression databases

BgeeiENSMUSG00000068036.
ExpressionAtlasiQ9QZQ1. baseline and differential.
GenevisibleiQ9QZQ1. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with F-actin, nectin and NECTIN3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR (By similarity).By similarity

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • Ras GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi201438. 5 interactions.
DIPiDIP-60737N.
IntActiQ9QZQ1. 3 interactions.
STRINGi10090.ENSMUSP00000118318.

Structurei

Secondary structure

1
1820
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi249 – 2524Combined sources
Turni255 – 2573Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi264 – 2674Combined sources
Helixi274 – 28512Combined sources
Beta strandi288 – 2903Combined sources
Turni292 – 2943Combined sources
Beta strandi295 – 3017Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi315 – 3173Combined sources
Helixi325 – 3306Combined sources
Helixi334 – 3363Combined sources
Beta strandi339 – 3457Combined sources
Helixi381 – 3833Combined sources
Beta strandi386 – 3905Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi423 – 4275Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi450 – 4578Combined sources
Beta strandi459 – 4646Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi470 – 4745Combined sources
Beta strandi481 – 4833Combined sources
Beta strandi488 – 4914Combined sources
Turni492 – 4943Combined sources
Beta strandi495 – 5006Combined sources
Beta strandi1007 – 10137Combined sources
Beta strandi1015 – 10173Combined sources
Beta strandi1019 – 10268Combined sources
Beta strandi1031 – 104111Combined sources
Helixi1045 – 10495Combined sources
Beta strandi1057 – 10615Combined sources
Helixi1071 – 10799Combined sources
Beta strandi1083 – 10908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
ProteinModelPortaliQ9QZQ1.
SMRiQ9QZQ1. Positions 249-348, 381-502, 1001-1096.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZQ1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 13395Ras-associating 1PROSITE-ProRule annotationAdd
BLAST
Domaini246 – 348103Ras-associating 2PROSITE-ProRule annotationAdd
BLAST
Domaini426 – 49267FHAAdd
BLAST
Domaini653 – 908256DilutePROSITE-ProRule annotationAdd
BLAST
Domaini1007 – 109387PDZPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili146 – 18641Sequence analysisAdd
BLAST
Coiled coili1410 – 144637Sequence analysisAdd
BLAST
Coiled coili1523 – 156139Sequence analysisAdd
BLAST
Coiled coili1593 – 166573Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi163 – 17513Glu/Lys-richAdd
BLAST
Compositional biasi1346 – 139247Pro-richAdd
BLAST
Compositional biasi1676 – 170631Pro-richAdd
BLAST
Compositional biasi1733 – 17364Poly-Glu

Sequence similaritiesi

Contains 1 dilute domain.PROSITE-ProRule annotation
Contains 1 FHA domain.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 2 Ras-associating domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1892. Eukaryota.
ENOG410XR0S. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000008041.
HOVERGENiHBG050463.
InParanoidiQ9QZQ1.
KOiK05702.
PhylomeDBiQ9QZQ1.
TreeFamiTF350731.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. RA_dom.
IPR008984. SMAD_FHA_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
SMARTiSM01132. DIL. 1 hit.
SM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9QZQ1-3) [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

        10         20         30         40         50
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK
60 70 80 90 100
AAGNFATKCI RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG
110 120 130 140 150
ERRLDIDEKP LVVQLNWNKD DREGRFVLKN ENDAIPAKKA QSNGPEKQEK
160 170 180 190 200
EGVIQNFKRT LSKKEKKEKK KKEKEALRQA SDKEERPSQG DDSENSRLAA
210 220 230 240 250
EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS DGRPDSGGTL
260 270 280 290 300
RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV
310 320 330 340 350
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY
360 370 380 390 400
IPKKMKKHVE GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY
410 420 430 440 450
YSYHTYEDGS DSRDKPKLYR LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC
460 470 480 490 500
DLTNMDGVVT VTPRSMDAET YVDGQRISET TMLQSGMRLQ FGTSHVFKFV
510 520 530 540 550
DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV HSGTALPASR
560 570 580 590 600
STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI
610 620 630 640 650
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH
660 670 680 690 700
RPDISPTERT HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN
710 720 730 740 750
FIKQDRDLSR ITLDAQDVLA HLVQMAFKYL VHCLQSELNN YMPAFLDDPE
760 770 780 790 800
ENSLQRPKID DVLHTLTGAM SLLRRCRVNA ALTIQLFSQL FHFINMWLFN
810 820 830 840 850
RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD CHLSRIVQAT
860 870 880 890 900
TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
910 920 930 940 950
NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN
960 970 980 990 1000
GLQEFLDPLC QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP
1010 1020 1030 1040 1050
LRKEPEIITV TLKKQNGMGL SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG
1060 1070 1080 1090 1100
RLAAGDQLLS VDGRSLVGLS QERAAELMTR TSSVVTLEVA KQGAIYHGLA
1110 1120 1130 1140 1150
TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS PESPQMPWTE
1160 1170 1180 1190 1200
YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV
1210 1220 1230 1240 1250
STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP
1260 1270 1280 1290 1300
NYEEKPHVHT ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC
1310 1320 1330 1340 1350
DSDMWINQSS SVESSTSSQE HLNHSSKSVT PASTLTKSGP GRWKTPAAVL
1360 1370 1380 1390 1400
PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD GIPMDLPLPP PPANQAGPQS
1410 1420 1430 1440 1450
AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL GQMRSQTLNP
1460 1470 1480 1490 1500
ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK
1510 1520 1530 1540 1550
EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE
1560 1570 1580 1590 1600
ESDRLRKLML EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR
1610 1620 1630 1640 1650
ARMQDEERRR QQQLEEMRKR EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ
1660 1670 1680 1690 1700
EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG LSRPPLPRDY EPPSLSSAPC
1710 1720 1730 1740 1750
APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP AGPNSYSGSA
1760 1770 1780 1790 1800
GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV
1810 1820
SDKVKASRKL TELENELNTK
Length:1,820
Mass (Da):206,499
Last modified:July 10, 2007 - v3
Checksum:i9FA4F378D840D8B1
GO
Isoform 1 (identifier: Q9QZQ1-2) [UniParc]FASTAAdd to basket
Also known as: l-afadin

The sequence of this isoform differs from the canonical sequence as follows:
     393-407: Missing.

Show »
Length:1,805
Mass (Da):204,553
Checksum:i5987A16BA9F28C2E
GO
Isoform 2 (identifier: Q9QZQ1-1)
Also known as: s-afadin
Sequence is not available
Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231N → Y in AAD54283 (PubMed:10477764).Curated
Sequence conflicti101 – 1011E → EE in AK016557 (PubMed:16141072).Curated
Sequence conflicti694 – 6941N → D in AK016557 (PubMed:16141072).Curated
Sequence conflicti897 – 9004DLIE → PEMR in AK016557 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei393 – 40715Missing in isoform 1. 1 PublicationVSP_026731Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC155253 Genomic DNA. No translation available.
CAAA01106165 Genomic DNA. No translation available.
CAAA01134612 Genomic DNA. No translation available.
CAAA01201738 Genomic DNA. No translation available.
CAAA01218165 Genomic DNA. No translation available.
AF172447 mRNA. Translation: AAD54283.1.
AK016557 mRNA. No translation available.
CCDSiCCDS49955.1. [Q9QZQ1-3]
RefSeqiNP_034936.1. NM_010806.1. [Q9QZQ1-3]
UniGeneiMm.59167.

Genome annotation databases

EnsembliENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
GeneIDi17356.
KEGGimmu:17356.
UCSCiuc008amr.1. mouse. [Q9QZQ1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC155253 Genomic DNA. No translation available.
CAAA01106165 Genomic DNA. No translation available.
CAAA01134612 Genomic DNA. No translation available.
CAAA01201738 Genomic DNA. No translation available.
CAAA01218165 Genomic DNA. No translation available.
AF172447 mRNA. Translation: AAD54283.1.
AK016557 mRNA. No translation available.
CCDSiCCDS49955.1. [Q9QZQ1-3]
RefSeqiNP_034936.1. NM_010806.1. [Q9QZQ1-3]
UniGeneiMm.59167.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
ProteinModelPortaliQ9QZQ1.
SMRiQ9QZQ1. Positions 249-348, 381-502, 1001-1096.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201438. 5 interactions.
DIPiDIP-60737N.
IntActiQ9QZQ1. 3 interactions.
STRINGi10090.ENSMUSP00000118318.

PTM databases

iPTMnetiQ9QZQ1.
PhosphoSiteiQ9QZQ1.

Proteomic databases

MaxQBiQ9QZQ1.
PaxDbiQ9QZQ1.
PeptideAtlasiQ9QZQ1.
PRIDEiQ9QZQ1.

Protocols and materials databases

DNASUi17356.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
GeneIDi17356.
KEGGimmu:17356.
UCSCiuc008amr.1. mouse. [Q9QZQ1-3]

Organism-specific databases

CTDi4301.
MGIiMGI:1314653. Mllt4.

Phylogenomic databases

eggNOGiKOG1892. Eukaryota.
ENOG410XR0S. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000008041.
HOVERGENiHBG050463.
InParanoidiQ9QZQ1.
KOiK05702.
PhylomeDBiQ9QZQ1.
TreeFamiTF350731.

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.

Miscellaneous databases

ChiTaRSiMllt4. mouse.
EvolutionaryTraceiQ9QZQ1.
PROiQ9QZQ1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000068036.
ExpressionAtlasiQ9QZQ1. baseline and differential.
GenevisibleiQ9QZQ1. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. RA_dom.
IPR008984. SMAD_FHA_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
SMARTiSM01132. DIL. 1 hit.
SM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAFAD_MOUSE
AccessioniPrimary (citable) accession number: Q9QZQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 10, 2007
Last modified: September 7, 2016
This is version 132 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

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 one 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.