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P55196 (AFAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Afadin
Alternative name(s):
ALL1-fused gene from chromosome 6 protein
Short name=Protein AF-6
Gene names
Name:MLLT4
Synonyms:AF6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1824 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer. Interacts with F-actin, nectin and PVRL3/nectin-3. Essential for the association of nectin and E-cadherin. Isoform 1/s-afadindoes not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1 and RIT2 By similarity. Interacts with NRXN1 and BCR. Ref.7

Subcellular location

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

Domain

The PDZ/DHR domain interacts with the C-terminus of nectin and the Pro-rich C-terminus domain interacts with F-actin.

Involvement in disease

A chromosomal aberration involving MLLT4 is associated with acute leukemias. Translocation t(6;11)(q27;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Sequence similarities

Contains 1 dilute domain.

Contains 1 FHA domain.

Contains 1 PDZ (DHR) domain.

Contains 2 Ras-associating domains.

Sequence caution

The sequence CAB82312.1 differs from that shown. Reason: Frameshift at positions 1509, 1512 and 1701.

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: P55196-4)

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.
Isoform 1 (identifier: P55196-2)

Also known as: s-afadin;

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: Missing.
     393-407: Missing.
     1605-1628: LQDEERRRQQQLEEMRKREAEDRA → VKGGVLWLCPSVVPILASACFPWG
     1629-1824: Missing.
Note: May be due to intron retention.
Isoform 2 (identifier: P55196-1)

Also known as: l-afadin;

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: Missing.
     393-407: Missing.
     1048-1048: Missing.
     1747-1824: PNSYPGSTGA...TELENELNTK → QDKYSSTRKS...KRVTNQLSLS
Note: May be due to intron retention.
Isoform 3 (identifier: P55196-3)

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: Missing.
     393-407: Missing.
     1048-1048: Missing.
     1683-1746: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: P55196-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1605-1606: Missing.
     1650-1653: RRQE → VMVL
     1654-1824: Missing.
Isoform 5 (identifier: P55196-5)

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: Missing.
     1604-1604: R → RTAMPAISVLDL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18241824Afadin
PRO_0000215918

Regions

Domain39 – 13395Ras-associating 1
Domain246 – 348103Ras-associating 2
Domain426 – 49267FHA
Domain668 – 908241Dilute
Domain1007 – 109387PDZ
Coiled coil146 – 18540 Potential
Coiled coil1408 – 144841 Potential
Coiled coil1523 – 1667145 Potential
Compositional bias163 – 17513Glu/Lys-rich
Compositional bias1346 – 139247Pro-rich
Compositional bias1578 – 158811Asp/Glu-rich (acidic)
Compositional bias1678 – 170831Pro-rich

Sites

Site261Breakpoint for translocation to form KMT2A/MLL1-MLLT4

Amino acid modifications

Modified residue2161Phosphoserine Ref.12
Modified residue5571Phosphoserine By similarity
Modified residue11071Phosphoserine Ref.12
Modified residue11821Phosphoserine Ref.9 Ref.10 Ref.12 Ref.14
Modified residue12321Phosphothreonine Ref.12
Modified residue17211Phosphoserine Ref.12 Ref.14 Ref.15
Modified residue17791Phosphoserine Ref.12 Ref.15
Modified residue17991Phosphoserine Ref.12 Ref.15
Modified residue18071N6-acetyllysine By similarity

Natural variations

Alternative sequence1391Missing in isoform 1, isoform 2, isoform 3 and isoform 5.
VSP_038707
Alternative sequence393 – 40715Missing in isoform 1, isoform 2 and isoform 3.
VSP_038708
Alternative sequence10481Missing in isoform 2 and isoform 3.
VSP_038709
Alternative sequence16041R → RTAMPAISVLDL in isoform 5.
VSP_019257
Alternative sequence1605 – 162824LQDEE…AEDRA → VKGGVLWLCPSVVPILASAC FPWG in isoform 1.
VSP_000217
Alternative sequence1605 – 16062Missing in isoform 6.
VSP_041197
Alternative sequence1629 – 1824196Missing in isoform 1.
VSP_000218
Alternative sequence1650 – 16534RRQE → VMVL in isoform 6.
VSP_041198
Alternative sequence1654 – 1824171Missing in isoform 6.
VSP_041199
Alternative sequence1683 – 174664Missing in isoform 3.
VSP_038710
Alternative sequence1747 – 182478PNSYP…ELNTK → QDKYSSTRKSHGDLLPAPLK PRPPPCQPRPASDGVFLSNS FQPPSAKANSTAHKKGQPLP PPKKSSSYHPSHCKGRGKRV TNQLSLS in isoform 2.
VSP_038711

Experimental info

Sequence conflict3741G → V in AAC50059. Ref.1
Sequence conflict14251R → P in AAC50059. Ref.1
Isoform 1:
Sequence conflict1031 – 10322DV → D in AAC50059. Ref.1
Sequence conflict1031 – 10322DV → D in BAA32485. Ref.2

Secondary structure

.................... 1824
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified February 9, 2010. Version 3.
Checksum: 51486232F183A3BA

FASTA1,824206,804
        10         20         30         40         50         60 
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI 

        70         80         90        100        110        120 
RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG ERRLDIDEKP LVVQLNWNKD 

       130        140        150        160        170        180 
DREGRFVLKN ENDAIPPKKA QSNGPEKQEK EGVIQNFKRT LSKKEKKEKK KREKEALRQA 

       190        200        210        220        230        240 
SDKDDRPFQG EDVENSRLAA EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS 

       250        260        270        280        290        300 
DGRPDSGGTL RIYADSLKPN IPYKTILLST TDPADFAVAE ALEKYGLEKE NPKDYCIARV 

       310        320        330        340        350        360 
MLPPGAQHSD EKGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDH IPKKTKKHLE 

       370        380        390        400        410        420 
GKTPKGKERA DGSGYGSTLP PEKLPYLVEL SPGRRNHFAY YNYHTYEDGS DSRDKPKLYR 

       430        440        450        460        470        480 
LQLSVTEVGT EKLDDNSIQL FGPGIQPHHC DLTNMDGVVT VTPRSMDAET YVEGQRISET 

       490        500        510        520        530        540 
TMLQSGMKVQ FGASHVFKFV DPSQDHALAK RSVDGGLMVK GPRHKPGIVQ ETTFDLGGDI 

       550        560        570        580        590        600 
HSGTALPTSK STTRLDSDRV SSASSTAERG MVKPMIRVEQ QPDYRRQESR TQDASGPELI 

       610        620        630        640        650        660 
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSNQY RPDISPTERT 

       670        680        690        700        710        720 
HKVIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN FIKQDRDLSR ITLDAQDVLA 

       730        740        750        760        770        780 
HLVQMAFKYL VHCLQSELNN YMPAFLDDPE ENSLQRPKID DVLHTLTGAM SLLRRCRVNA 

       790        800        810        820        830        840 
ALTIQLFSQL FHFINMWLFN RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD 

       850        860        870        880        890        900 
CHLSRIVQAT TLLTMDKYAP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE 

       910        920        930        940        950        960 
NVVTVAENTA DELARSDGRE VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN GLQEFLDPLC 

       970        980        990       1000       1010       1020 
QRGFCRLIPH TRSPGTWTIY FEGADYESHL LRENTELAQP LRKEPEIITV TLKKQNGMGL 

      1030       1040       1050       1060       1070       1080 
SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS QERAAELMTR 

      1090       1100       1110       1120       1130       1140 
TSSVVTLEVA KQGAIYHGLA TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSTQNGS 

      1150       1160       1170       1180       1190       1200 
PESPQLPWAE YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKSAYA SGTTAKITSV 

      1210       1220       1230       1240       1250       1260 
STGNLCTEEQ TPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQNQWP NYEEKPHMHT 

      1270       1280       1290       1300       1310       1320 
DSNHSSIAIQ RVTRSQEELR EDKAYQLERH RIEAAMDRKS DSDMWINQSS SLDSSTSSQE 

      1330       1340       1350       1360       1370       1380 
HLNHSSKSVT PASTLTKSGP GRWKTPAAIP ATPVAVSQPI RTDLPPPPPP PPVHYAGDFD 

      1390       1400       1410       1420       1430       1440 
GMSMDLPLPP PPSANQIGLP SAQVAAAERR KREEHQRWYE KEKARLEEER ERKRREQERK 

      1450       1460       1470       1480       1490       1500 
LGQMRTQSLN PAPFSPLTAQ QMKPEKPSTL QRPQETVIRE LQPQQQPRTI ERRDLQYITV 

      1510       1520       1530       1540       1550       1560 
SKEELSSGDS LSPDPWKRDA KEKLEKQQQM HIVDMLSKEI QELQSKPDRS AEESDRLRKL 

      1570       1580       1590       1600       1610       1620 
MLEWQFQKRL QESKQKDEDD EEEEDDDVDT MLIMQRLEAE RRARLQDEER RRQQQLEEMR 

      1630       1640       1650       1660       1670       1680 
KREAEDRARQ EEERRRQEEE RTKRDAEEKR RQEEGYYSRL EAERRRQHDE AARRLLEPEA 

      1690       1700       1710       1720       1730       1740 
PGLCRPPLPR DYEPPSPSPA PGAPPPPPQR NASYLKTQVL SPDSLFTAKF VAYNEEEEEE 

      1750       1760       1770       1780       1790       1800 
DCSLAGPNSY PGSTGAAVGA HDACRDAKEK RSKSQDADSP GSSGAPENLT FKERQRLFSQ 

      1810       1820 
GQDVSNKVKA SRKLTELENE LNTK 

« Hide

Isoform 1 (s-afadin) [UniParc].

Checksum: 202D7BEC1E825AB6
Show »

FASTA1,612182,000
Isoform 2 (l-afadin) [UniParc].

Checksum: EB1FE7F04879CE8F
Show »

FASTA1,816205,605
Isoform 3 [UniParc].

Checksum: ECCDE46AD8C401B9
Show »

FASTA1,743197,653
Isoform 6 [UniParc].

Checksum: 6F55A481FC0DB6B3
Show »

FASTA1,651187,672
Isoform 5 [UniParc].

Checksum: 3D57FDBD6A521DFD
Show »

FASTA1,834207,788

References

« Hide 'large scale' references
[1]"Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation."
Prasad R., Gu Y., Alder H., Nakamura T., Canaani O., Saito H., Huebner K., Gale R.P., Nowell P.C., Kuriyama K., Miyazaki Y., Croce C.M., Canaani E.
Cancer Res. 53:5624-5628(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH KMT2A.
[2]"Complete genomic structure, DNA polymorphisms, and alternative splicing of the human AF-6 gene."
Saito S., Matsushima M., Shirahama S., Minaguchi T., Kanamori Y., Minami M., Nakamura Y.
DNA Res. 5:115-120(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3).
Tissue: Fetal brain.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-1824 (ISOFORM 6).
Tissue: Brain.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-1824 (ISOFORM 5).
Tissue: Amygdala.
[7]"Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin."
Reymond N., Borg J.-P., Lecocq E., Adelaide J., Campadelli-Fiume G., Dubreuil P., Lopez M.
Gene 255:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PVRL3.
[8]"Nectin and afadin: novel organizers of intercellular junctions."
Takai Y., Nakanishi H.
J. Cell Sci. 116:17-27(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON INTERACTION.
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-1107; SER-1182; THR-1232; SER-1721; SER-1779 AND SER-1799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182 AND SER-1721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1721; SER-1779 AND SER-1799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution structure of AF-6 PDZ domain and its interaction with the C-terminal peptides from Neurexin and Bcr."
Zhou H., Xu Y., Yang Y., Huang A., Wu J., Shi Y.
J. Biol. Chem. 280:13841-13847(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1003-1094 IN COMPLEX WITH NRXN1 AND BCR.
[18]"Discovery of low-molecular-weight ligands for the AF6 PDZ domain."
Joshi M., Vargas C., Boisguerin P., Diehl A., Krause G., Schmieder P., Moelling K., Hagen V., Schade M., Oschkinat H.
Angew. Chem. Int. Ed. 45:3790-3795(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1001-1095.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02478 mRNA. Translation: AAC50059.1.
AB011399 Genomic DNA. Translation: BAA32483.1.
AB011399 Genomic DNA. Translation: BAA32484.1.
AB011399 Genomic DNA. Translation: BAA32485.1.
AL009178, AL049698, AL731868 Genomic DNA. Translation: CAI20900.1.
AL009178, AL049698, AL731868 Genomic DNA. Translation: CAI20902.1.
AL731868, AL009178, AL049698 Genomic DNA. Translation: CAI40824.1.
AL731868, AL009178, AL049698 Genomic DNA. Translation: CAI40826.1.
AL049698, AL009178, AL731868 Genomic DNA. Translation: CAI42812.1.
AL049698, AL009178, AL731868 Genomic DNA. Translation: CAI42814.1.
CH471051 Genomic DNA. Translation: EAW47482.1.
AB209420 mRNA. Translation: BAD92657.1.
AL161973 mRNA. Translation: CAB82312.1. Frameshift.
PIRT47137.
RefSeqNP_001035089.1. NM_001040000.2.
NP_001193937.1. NM_001207008.1.
XP_005267053.1. XM_005266996.1.
UniGeneHs.614974.
Hs.728849.
Hs.741785.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2MNMR-A1003-1094[»]
1XZ9NMR-A1001-1096[»]
2AINNMR-A1003-1094[»]
2EXGNMR-A1001-1096[»]
ProteinModelPortalP55196.
SMRP55196. Positions 11-138, 249-348, 374-503, 603-952, 1001-1096, 1521-1687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110447. 46 interactions.
IntActP55196. 22 interactions.
MINTMINT-90828.
STRING9606.ENSP00000383623.

PTM databases

PhosphoSiteP55196.

Polymorphism databases

DMDM288558835.

Proteomic databases

PaxDbP55196.
PRIDEP55196.

Protocols and materials databases

DNASU4301.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392108; ENSP00000375956; ENSG00000130396. [P55196-6]
ENST00000400822; ENSP00000383623; ENSG00000130396. [P55196-5]
ENST00000447894; ENSP00000404595; ENSG00000130396. [P55196-4]
GeneID4301.
KEGGhsa:4301.
UCSCuc003qwb.1. human. [P55196-2]
uc003qwc.2. human. [P55196-6]
uc003qwg.1. human. [P55196-4]
uc021zij.1. human. [P55196-3]

Organism-specific databases

CTD4301.
GeneCardsGC06P168227.
HGNCHGNC:7137. MLLT4.
HPACAB013496.
HPA030212.
HPA030213.
HPA030214.
HPA030215.
HPA049868.
MIM159559. gene.
neXtProtNX_P55196.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291597.
HOVERGENHBG050463.
KOK05702.
OMAFAYYNYH.
PhylomeDBP55196.
TreeFamTF350731.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkP55196.

Gene expression databases

ArrayExpressP55196.
BgeeP55196.
CleanExHS_MLLT4.
GenevestigatorP55196.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProIPR028842. Afadin.
IPR018444. Dil_domain.
IPR002710. Dilute.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. Ras-assoc.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR10398:SF0. PTHR10398:SF0. 1 hit.
PfamPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLLT4. human.
EvolutionaryTraceP55196.
GeneWikiMLLT4.
GenomeRNAi4301.
NextBio16931.
PROP55196.
SOURCESearch...

Entry information

Entry nameAFAD_HUMAN
AccessionPrimary (citable) accession number: P55196
Secondary accession number(s): O75087 expand/collapse secondary AC list , O75088, O75089, Q59FP0, Q5TIG6, Q5TIG7, Q9NSN7, Q9NU92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM