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Reviewed, UniProtKB/Swiss-Prot P55196 (AFAD_HUMAN)

Last modified June 16, 2009. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Afadin
Alternative name(s):
    Protein AF-6
Gene names
Name: MLLT4
Synonyms: AF6
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1816 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 2/s-afadin does 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.

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 N-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 MLL/HRX. 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 1492, 1495 and 1684.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcell adhesion

Traceable author statement. Source: ProtInc

cell-cell signaling Ref.1

Traceable author statement. Source: ProtInc

signal transduction Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentadherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell-cell junction

Traceable author statement. Source: ProtInc

   Molecular functionprotein C-terminus binding

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAGP619811EBI-365875,EBI-359832

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P55196-1)

Also known as: l-afadin;

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:
     1031-1031: D → DV
     1588-1611: LQDEERRRQQQLEEMRKREAEDRA → VKGGVLWLCPSVVPILASACFPWG
     1612-1816: Missing.
Isoform 3 (identifier: P55196-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1666-1743: LCRPPLPRDY...SSTRKSHGDL → PNSYPGSTGA...TELENELNTK
     1744-1816: Missing.
Isoform 4 (identifier: P55196-4)

The sequence of this isoform differs from the canonical sequence as follows:
     137-137: P → PK
     391-391: P → PGRRNHFAYYNYHTYE
     1031-1031: D → DV
     1730-1816: QDKYSSTRKS...KRVTNQLSLS → PNSYPGSTGA...TELENELNTK
Isoform 5 (identifier: P55196-5)

The sequence of this isoform differs from the canonical sequence as follows:
     391-391: P → PGRRNHFAYYNYHTYE
     1031-1031: D → DV
     1587-1587: R → RTAMPAISVLDL
     1730-1816: QDKYSSTRKS...KRVTNQLSLS → PNSYPGSTGA...TELENELNTK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18161816Afadin
PRO_0000215918

Regions

Domain39 – 13395Ras-associating 1
Domain245 – 347103Ras-associating 2
Domain425 – 49167FHA
Domain652 – 892241Dilute
Domain991 – 107686PDZ
Coiled coil145 – 18440 Potential
Coiled coil1391 – 143141 Potential
Coiled coil1506 – 1650145 Potential
Compositional bias162 – 17413Glu/Lys-rich
Compositional bias1329 – 137547Pro-rich
Compositional bias1561 – 157111Asp/Glu-rich (acidic)
Compositional bias1661 – 169131Pro-rich

Sites

Site261Breakpoint for translocation to form MLL-MLLT4

Amino acid modifications

Modified residue941Phosphotyrosine Ref.11
Modified residue2151Phosphoserine Ref.14
Modified residue5411Phosphoserine By similarity
Modified residue10901Phosphoserine Ref.14 Ref.9
Modified residue11551Phosphoserine Ref.7
Modified residue11561Phosphoserine Ref.7
Modified residue11651Phosphoserine Ref.14 Ref.8 Ref.12
Modified residue11841Phosphoserine Ref.8
Modified residue12131Phosphotyrosine By similarity
Modified residue12151Phosphothreonine Ref.14
Modified residue12581Phosphoserine By similarity
Modified residue13131Phosphothreonine By similarity
Modified residue13171Phosphothreonine By similarity
Modified residue16791Phosphoserine Ref.13
Modified residue16811Phosphoserine Ref.10
Modified residue17041Phosphoserine Ref.14

Natural variations

Alternative sequence1371P → PK in isoform 4.
VSP_019254
Alternative sequence3911P → PGRRNHFAYYNYHTYE in isoform 4 and isoform 5.
VSP_019255
Alternative sequence10311D → DV in isoform 1, isoform 4 and isoform 5.
VSP_019256
Alternative sequence15871R → RTAMPAISVLDL in isoform 5.
VSP_019257
Alternative sequence1588 – 161124LQDEE…AEDRA → VKGGVLWLCPSVVPILASAC FPWG in isoform 1.
VSP_000217
Alternative sequence1612 – 1816205Missing in isoform 1.
VSP_000218
Alternative sequence1666 – 174378LCRPP…SHGDL → PNSYPGSTGAAVGAHDACRD AKEKRSKSQDADSPGSSGAP ENLTFKERQRLFSQGQDVSN KVKASRKLTELENELNTK in isoform 3.
VSP_000219
Alternative sequence1730 – 181687QDKYS…QLSLS → PNSYPGSTGAAVGAHDACRD AKEKRSKSQDADSPGSSGAP ENLTFKERQRLFSQGQDVSN KVKASRKLTELENELNTK in isoform 4 and isoform 5.
VSP_019258
Alternative sequence1744 – 181673Missing in isoform 3.
VSP_000220

Experimental info

Sequence conflict3731G → V in AAC50059. Ref.1
Sequence conflict14081R → P in AAC50059. Ref.1

Secondary structure

................. 1816
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (l-afadin) [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: EB1FE7F04879CE8F

FASTA1,816205,605
        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 ENDAIPPKAQ SNGPEKQEKE GVIQNFKRTL SKKEKKEKKK REKEALRQAS 

       190        200        210        220        230        240 
DKDDRPFQGE DVENSRLAAE VYKDMPETSF TRTISNPEVV MKRRRQQKLE KRMQEFRSSD 

       250        260        270        280        290        300 
GRPDSGGTLR IYADSLKPNI PYKTILLSTT DPADFAVAEA LEKYGLEKEN PKDYCIARVM 

       310        320        330        340        350        360 
LPPGAQHSDE KGAKEIILDD DECPLQIFRE WPSDKGILVF QLKRRPPDHI PKKTKKHLEG 

       370        380        390        400        410        420 
KTPKGKERAD GSGYGSTLPP EKLPYLVELS PDGSDSRDKP KLYRLQLSVT EVGTEKLDDN 

       430        440        450        460        470        480 
SIQLFGPGIQ PHHCDLTNMD GVVTVTPRSM DAETYVEGQR ISETTMLQSG MKVQFGASHV 

       490        500        510        520        530        540 
FKFVDPSQDH ALAKRSVDGG LMVKGPRHKP GIVQETTFDL GGDIHSGTAL PTSKSTTRLD 

       550        560        570        580        590        600 
SDRVSSASST AERGMVKPMI RVEQQPDYRR QESRTQDASG PELILPASIE FRESSEDSFL 

       610        620        630        640        650        660 
SAIINYTNSS TVHFKLSPTY VLYMACRYVL SNQYRPDISP TERTHKVIAV VNKMVSMMEG 

       670        680        690        700        710        720 
VIQKQKNIAG ALAFWMANAS ELLNFIKQDR DLSRITLDAQ DVLAHLVQMA FKYLVHCLQS 

       730        740        750        760        770        780 
ELNNYMPAFL DDPEENSLQR PKIDDVLHTL TGAMSLLRRC RVNAALTIQL FSQLFHFINM 

       790        800        810        820        830        840 
WLFNRLVTDP DSGLCSHYWG AIIRQQLGHI EAWAEKQGLE LAADCHLSRI VQATTLLTMD 

       850        860        870        880        890        900 
KYAPDDIPNI NSTCFKLNSL QLQALLQNYH CAPDEPFIPT DLIENVVTVA ENTADELARS 

       910        920        930        940        950        960 
DGREVQLEED PDLQLPFLLP EDGYSCDVVR NIPNGLQEFL DPLCQRGFCR LIPHTRSPGT 

       970        980        990       1000       1010       1020 
WTIYFEGADY ESHLLRENTE LAQPLRKEPE IITVTLKKQN GMGLSIVAAK GAGQDKLGIY 

      1030       1040       1050       1060       1070       1080 
VKSVVKGGAA DDGRLAAGDQ LLSVDGRSLV GLSQERAAEL MTRTSSVVTL EVAKQGAIYH 

      1090       1100       1110       1120       1130       1140 
GLATLLNQPS PMMQRISDRR GSGKPRPKSE GFELYNNSTQ NGSPESPQLP WAEYSEPKKL 

      1150       1160       1170       1180       1190       1200 
PGDDRLMKNR ADHRSSPNVA NQPPSPGGKS AYASGTTAKI TSVSTGNLCT EEQTPPPRPE 

      1210       1220       1230       1240       1250       1260 
AYPIPTQTYT REYFTFPASK SQDRMAPPQN QWPNYEEKPH MHTDSNHSSI AIQRVTRSQE 

      1270       1280       1290       1300       1310       1320 
ELREDKAYQL ERHRIEAAMD RKSDSDMWIN QSSSLDSSTS SQEHLNHSSK SVTPASTLTK 

      1330       1340       1350       1360       1370       1380 
SGPGRWKTPA AIPATPVAVS QPIRTDLPPP PPPPPVHYAG DFDGMSMDLP LPPPPSANQI 

      1390       1400       1410       1420       1430       1440 
GLPSAQVAAA ERRKREEHQR WYEKEKARLE EERERKRREQ ERKLGQMRTQ SLNPAPFSPL 

      1450       1460       1470       1480       1490       1500 
TAQQMKPEKP STLQRPQETV IRELQPQQQP RTIERRDLQY ITVSKEELSS GDSLSPDPWK 

      1510       1520       1530       1540       1550       1560 
RDAKEKLEKQ QQMHIVDMLS KEIQELQSKP DRSAEESDRL RKLMLEWQFQ KRLQESKQKD 

      1570       1580       1590       1600       1610       1620 
EDDEEEEDDD VDTMLIMQRL EAERRARLQD EERRRQQQLE EMRKREAEDR ARQEEERRRQ 

      1630       1640       1650       1660       1670       1680 
EEERTKRDAE EKRRQEEGYY SRLEAERRRQ HDEAARRLLE PEAPGLCRPP LPRDYEPPSP 

      1690       1700       1710       1720       1730       1740 
SPAPGAPPPP PQRNASYLKT QVLSPDSLFT AKFVAYNEEE EEEDCSLAGQ DKYSSTRKSH 

      1750       1760       1770       1780       1790       1800 
GDLLPAPLKP RPPPCQPRPA SDGVFLSNSF QPPSAKANST AHKKGQPLPP PKKSSSYHPS 

      1810 
HCKGRGKRVT NQLSLS 

« Hide

Isoform 1 (s-afadin).

Checksum: 202D7BEC1E825AB6
Show »

FASTA1,612182,000
Isoform 3.

Checksum: ECCDE46AD8C401B9
Show »

FASTA1,743197,653
Isoform 4.

Checksum: 51486232F183A3BA
Show »

FASTA1,824206,804
Isoform 5.

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: 8242616] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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: 9679199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[4]"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-1816 (ISOFORM 4).
Tissue: Amygdala.
[5]"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: 11024295] [Abstract]
Cited for: INTERACTION WITH PVRL3.
[6]"Nectin and afadin: novel organizers of intercellular junctions."
Takai Y., Nakanishi H.
J. Cell Sci. 116:17-27(2003) [PubMed: 12456712] [Abstract]
Cited for: REVIEW ON INTERACTION.
[7]"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: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155 AND SER-1156, MASS SPECTROMETRY.
Tissue: T-cell.
[8]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1165 AND SER-1184, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1090, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1681, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, MASS SPECTROMETRY.
[12]"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: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1165, MASS SPECTROMETRY.
[13]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1679, MASS SPECTROMETRY.
[14]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-1090; SER-1165; THR-1215 AND SER-1704, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1698 AND SER-1718 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779 AND SER-1799 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1789 AND SER-1809 (ISOFORM 5), MASS SPECTROMETRY.
[15]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]"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: 15684424] [Abstract]
Cited for: STRUCTURE BY NMR OF 987-1077 IN COMPLEX WITH NRXN1 AND BCR.
[17]"Structure of AF-6 PDZ domain."
Joshi M., Boisguerin P., Leitner D., Volkmer-Engert R., Moelling K., Schade M., Schmieder P., Krause G., Oschkinat H.
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 985-1078.
+Additional computationally mapped references.

Cross-references

Sequence databases

U02478 mRNA. Translation: AAC50059.1.
AB011399 Genomic DNA. Translation: BAA32483.1.
AB011399 Genomic DNA. Translation: BAA32484.1.
AB011399 Genomic DNA. Translation: BAA32485.1.
AL009178, AL731868, AL049698 Genomic DNA. Translation: CAI20900.1.
AL731868, AL009178, AL049698 Genomic DNA. Translation: CAI40824.1.
AL049698, AL009178, AL731868 Genomic DNA. Translation: CAI42812.1.
AL161973 mRNA. Translation: CAB82312.1. Frameshift.
IPIIPI00023461.
IPI00216505.
IPI00398718.
IPI00552765.
IPI00759546.
PIRT47137.
RefSeqNP_001035090.1.
NP_005927.2.
UniGeneHs.644024
Hs.715090

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1T2MNMR-A987-1077[»]
1XZ9NMR-A985-1079[»]
2AINNMR-A987-1077[»]
2EXGNMR-A985-1079[»]
SMRP55196. Positions 248-347, 373-487.
ModBaseSearch...

Protein-protein interaction databases

IntActP55196. 6 interactions.

PTM databases

PhosphoSiteP55196.

Proteomic databases

PRIDEP55196.

Genome annotation databases

EnsemblENSG00000130396. Homo sapiens. [Contig view]
GeneID4301.

Organism-specific databases

GeneCardsGC06P167970.
GC06P168046.
HGNCHGNC:7137. MLLT4.
MIM159559. gene.
PharmGKBPA30853.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP55196.

Gene expression databases

ArrayExpressP55196.
BgeeP55196.
CleanExHS_MLLT4.
GermOnlineENSG00000130396. Homo sapiens.

Family and domain databases

InterProIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000253. FHA.
IPR001478. PDZ/DHR/GLGF.
IPR000159. Ras-assoc.
[Graphical view]
PfamPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
ProDomPD003376. DIL. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
PROSITEPS51126. DILUTE. 1 hit.
PS50006. FHA_DOMAIN. False negative.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio16931.
SOURCESearch...

Entry information

Entry nameAFAD_HUMAN
AccessionPrimary (citable) accession number: P55196
Secondary accession number(s): O75087 expand/collapse secondary AC list , O75088, O75089, Q5TIG6, Q9NSN7, Q9NU92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2001
Last modified: June 16, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents