Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9QZQ1

- AFAD_MOUSE

UniProt

Q9QZQ1 - AFAD_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Afadin

Gene

Mllt4

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. cell adhesion molecule binding Source: BHF-UCL

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_230395. 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
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1314653. Mllt4.

Subcellular locationi

Cell junctionadherens junction
Note: Not found at cell-matrix AJs.

GO - Cellular componenti

  1. adherens junction Source: MGI
  2. apical part of cell Source: MGI
  3. cell-cell adherens junction Source: MGI
  4. cell-cell junction Source: MGI
  5. cell junction Source: MGI
  6. cytoplasm Source: MGI
  7. nucleus Source: Ensembl
  8. plasma membrane Source: Ensembl
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 – 2161Phosphoserine1 Publication
Modified residuei557 – 5571Phosphoserine1 Publication
Modified residuei1107 – 11071Phosphoserine1 Publication
Modified residuei1182 – 11821Phosphoserine1 Publication
Modified residuei1232 – 12321PhosphothreonineBy similarity
Modified residuei1719 – 17191PhosphoserineBy similarity
Modified residuei1795 – 17951PhosphoserineBy similarity
Modified residuei1803 – 18031N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QZQ1.
PaxDbiQ9QZQ1.
PRIDEiQ9QZQ1.

PTM databases

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

BgeeiQ9QZQ1.
ExpressionAtlasiQ9QZQ1. baseline and differential.
GenevestigatoriQ9QZQ1.

Interactioni

Subunit structurei

Homodimer. Interacts with F-actin, nectin and PVRL3/nectin-3. 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

Protein-protein interaction databases

BioGridi201438. 5 interactions.
DIPiDIP-60737N.
IntActiQ9QZQ1. 2 interactions.

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, 605-936, 1001-1096, 1507-1685.
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

eggNOGiNOG291597.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000008041.
HOVERGENiHBG050463.
InParanoidiQ9QZQ1.
KOiK05702.
OrthoDBiEOG7G4QDD.
PhylomeDBiQ9QZQ1.
TreeFamiTF350731.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. Ras-assoc.
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]
SMARTiSM00240. 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. Align

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.
CCDSi CCDS49955.1. [Q9QZQ1-3 ]
RefSeqi NP_034936.1. NM_010806.1. [Q9QZQ1-3 ]
UniGenei Mm.59167.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WLN NMR - A 381-502 [» ]
1WXA NMR - A 246-348 [» ]
3AXA X-ray 2.78 A/B 1003-1095 [» ]
ProteinModelPortali Q9QZQ1.
SMRi Q9QZQ1. Positions 249-348, 381-502, 605-936, 1001-1096, 1507-1685.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201438. 5 interactions.
DIPi DIP-60737N.
IntActi Q9QZQ1. 2 interactions.

PTM databases

PhosphoSitei Q9QZQ1.

Proteomic databases

MaxQBi Q9QZQ1.
PaxDbi Q9QZQ1.
PRIDEi Q9QZQ1.

Protocols and materials databases

DNASUi 17356.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000139666 ; ENSMUSP00000118318 ; ENSMUSG00000068036 . [Q9QZQ1-3 ]
ENSMUST00000150848 ; ENSMUSP00000122447 ; ENSMUSG00000068036 . [Q9QZQ1-2 ]
GeneIDi 17356.
KEGGi mmu:17356.
UCSCi uc008amr.1. mouse. [Q9QZQ1-3 ]

Organism-specific databases

CTDi 4301.
MGIi MGI:1314653. Mllt4.

Phylogenomic databases

eggNOGi NOG291597.
GeneTreei ENSGT00390000010033.
HOGENOMi HOG000008041.
HOVERGENi HBG050463.
InParanoidi Q9QZQ1.
KOi K05702.
OrthoDBi EOG7G4QDD.
PhylomeDBi Q9QZQ1.
TreeFami TF350731.

Enzyme and pathway databases

Reactomei REACT_230395. Adherens junctions interactions.

Miscellaneous databases

ChiTaRSi Mllt4. mouse.
EvolutionaryTracei Q9QZQ1.
NextBioi 291962.
PROi Q9QZQ1.
SOURCEi Search...

Gene expression databases

Bgeei Q9QZQ1.
ExpressionAtlasi Q9QZQ1. baseline and differential.
Genevestigatori Q9QZQ1.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProi IPR018444. Dil_domain.
IPR002710. Dilute.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. Ras-assoc.
IPR008984. SMAD_FHA_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view ]
SMARTi SM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEi PS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "Afadin: a key molecule essential for structural organization of cell-cell junctions of polarized epithelia during embryogenesis."
    Ikeda W., Nakanishi H., Miyoshi J., Mandai K., Ishizaki H., Tanaka M., Togawa A., Takahashi K., Nishioka H., Yoshida H., Mizoguchi A., Nishikawa S., Takai Y.
    J. Cell Biol. 146:1117-1132(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-320 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: C57BL/6.
  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] OF 36-900 (ISOFORM 3).
    Tissue: Leukemia.
  4. "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities."
    Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., Takai Y.
    J. Biol. Chem. 275:10291-10299(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PVRL3.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "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-1803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Solution structure of the FHA domain and RAS-binding domain in mouse AF-6 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 246-487.

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: November 26, 2014
This is version 115 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