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Q9QZQ1

- AFAD_MOUSE

UniProt

Q9QZQ1 - AFAD_MOUSE

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Protein
Afadin
Gene
Mllt4, Af6
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
  2. protein binding Source: MGI

GO - Biological processi

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

Keywords - Biological processi

Cell adhesion

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 junction Source: MGI
  4. cell-cell adherens junction Source: MGI
  5. cell-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 – 18201820Afadin
PRO_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 – 12321Phosphothreonine By similarity
Modified residuei1719 – 17191Phosphoserine By similarity
Modified residuei1795 – 17951Phosphoserine By 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

ArrayExpressiQ9QZQ1.
BgeeiQ9QZQ1.
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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
ProteinModelPortaliQ9QZQ1.
SMRiQ9QZQ1. Positions 42-135, 249-348, 381-502, 604-936, 1001-1096, 1507-1685.

Miscellaneous databases

EvolutionaryTraceiQ9QZQ1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 13395Ras-associating 1
Add
BLAST
Domaini246 – 348103Ras-associating 2
Add
BLAST
Domaini426 – 49267FHA
Add
BLAST
Domaini653 – 908256Dilute
Add
BLAST
Domaini1007 – 109387PDZ
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili146 – 18641 Reviewed prediction
Add
BLAST
Coiled coili1410 – 144637 Reviewed prediction
Add
BLAST
Coiled coili1523 – 156139 Reviewed prediction
Add
BLAST
Coiled coili1593 – 166573 Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 dilute domain.
Contains 1 FHA domain.
Contains 1 PDZ (DHR) domain.

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

MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK     50
AAGNFATKCI RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG 100
ERRLDIDEKP LVVQLNWNKD DREGRFVLKN ENDAIPAKKA QSNGPEKQEK 150
EGVIQNFKRT LSKKEKKEKK KKEKEALRQA SDKEERPSQG DDSENSRLAA 200
EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS DGRPDSGGTL 250
RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV 300
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY 350
IPKKMKKHVE GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY 400
YSYHTYEDGS DSRDKPKLYR LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC 450
DLTNMDGVVT VTPRSMDAET YVDGQRISET TMLQSGMRLQ FGTSHVFKFV 500
DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV HSGTALPASR 550
STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI 600
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH 650
RPDISPTERT HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN 700
FIKQDRDLSR ITLDAQDVLA HLVQMAFKYL VHCLQSELNN YMPAFLDDPE 750
ENSLQRPKID DVLHTLTGAM SLLRRCRVNA ALTIQLFSQL FHFINMWLFN 800
RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD CHLSRIVQAT 850
TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE 900
NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN 950
GLQEFLDPLC QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP 1000
LRKEPEIITV TLKKQNGMGL SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG 1050
RLAAGDQLLS VDGRSLVGLS QERAAELMTR TSSVVTLEVA KQGAIYHGLA 1100
TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS PESPQMPWTE 1150
YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV 1200
STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP 1250
NYEEKPHVHT ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC 1300
DSDMWINQSS SVESSTSSQE HLNHSSKSVT PASTLTKSGP GRWKTPAAVL 1350
PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD GIPMDLPLPP PPANQAGPQS 1400
AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL GQMRSQTLNP 1450
ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK 1500
EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE 1550
ESDRLRKLML EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR 1600
ARMQDEERRR QQQLEEMRKR EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ 1650
EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG LSRPPLPRDY EPPSLSSAPC 1700
APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP AGPNSYSGSA 1750
GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV 1800
SDKVKASRKL TELENELNTK 1820
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):

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei393 – 40715Missing in isoform 1.
VSP_026731Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231N → Y in AAD54283. 1 Publication
Sequence conflicti101 – 1011E → EE in AK016557. 1 Publication
Sequence conflicti694 – 6941N → D in AK016557. 1 Publication
Sequence conflicti897 – 9004DLIE → PEMR in AK016557. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 42-135, 249-348, 381-502, 604-936, 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.

Miscellaneous databases

ChiTaRSi MLLT4. mouse.
EvolutionaryTracei Q9QZQ1.
NextBioi 291962.
PROi Q9QZQ1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9QZQ1.
Bgeei Q9QZQ1.
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: July 9, 2014
This is version 112 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

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