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Protein

Afadin

Gene

MLLT4

Organism
Homo sapiens (Human)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei26 – 261Breakpoint for translocation to form KMT2A/MLL1-MLLT4

GO - Molecular functioni

  • protein C-terminus binding Source: ProtInc
  • Ras GTPase binding Source: UniProtKB

GO - Biological processi

  • adherens junction organization Source: Reactome
  • cell adhesion Source: ProtInc
  • cell-cell junction organization Source: Reactome
  • cell-cell signaling Source: ProtInc
  • cell junction assembly Source: Reactome
  • establishment of endothelial intestinal barrier Source: UniProtKB
  • positive regulation of GTPase activity Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
SignaLinkiP55196.

Names & Taxonomyi

Protein namesi
Recommended name:
Afadin
Alternative name(s):
ALL1-fused gene from chromosome 6 protein
Short name:
Protein AF-6
Gene namesi
Name:MLLT4
Synonyms:AF6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:7137. MLLT4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Proto-oncogene

Polymorphism and mutation databases

BioMutaiMLLT4.
DMDMi288558835.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18241824AfadinPRO_0000215918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161Phosphoserine1 Publication
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei557 – 5571PhosphoserineBy similarity
Modified residuei1107 – 11071Phosphoserine1 Publication
Modified residuei1182 – 11821Phosphoserine5 Publications
Modified residuei1211 – 12111Phosphothreonine1 Publication
Modified residuei1232 – 12321Phosphothreonine1 Publication
Modified residuei1696 – 16961Phosphoserine1 Publication
Modified residuei1721 – 17211Phosphoserine3 Publications
Modified residuei1779 – 17791Phosphoserine2 Publications
Modified residuei1799 – 17991Phosphoserine3 Publications
Modified residuei1807 – 18071N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP55196.
PaxDbiP55196.
PRIDEiP55196.

PTM databases

PhosphoSiteiP55196.

Expressioni

Gene expression databases

BgeeiP55196.
CleanExiHS_MLLT4.
ExpressionAtlasiP55196. baseline and differential.
GenevisibleiP55196. HS.

Organism-specific databases

HPAiCAB013496.
HPA030212.
HPA030213.
HPA030214.
HPA030215.
HPA049868.

Interactioni

Subunit structurei

Homodimer. Interacts with F-actin, nectin and PVRL3/nectin-3. Essential for the association of nectin and E-cadherin. Isoform 1/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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DBN1Q166434EBI-365875,EBI-351394
PVRL2Q926922EBI-365875,EBI-718419
SRCP129317EBI-365875,EBI-621482

Protein-protein interaction databases

BioGridi110447. 55 interactions.
IntActiP55196. 22 interactions.
MINTiMINT-90828.

Structurei

Secondary structure

1
1824
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1006 – 10138Combined sources
Beta strandi1015 – 10173Combined sources
Beta strandi1020 – 10256Combined sources
Beta strandi1028 – 10314Combined sources
Beta strandi1034 – 10407Combined sources
Beta strandi1042 – 10443Combined sources
Helixi1045 – 10495Combined sources
Beta strandi1054 – 10618Combined sources
Helixi1071 – 10799Combined sources
Beta strandi1083 – 10919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2MNMR-A1003-1094[»]
1XZ9NMR-A1001-1096[»]
2AINNMR-A1003-1094[»]
2EXGNMR-A1001-1096[»]
ProteinModelPortaliP55196.
SMRiP55196. Positions 249-348, 374-503, 605-936, 1001-1096, 1521-1687.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55196.

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
Domaini668 – 908241DilutePROSITE-ProRule annotationAdd
BLAST
Domaini1007 – 109387PDZPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili146 – 18540Sequence AnalysisAdd
BLAST
Coiled coili1408 – 144841Sequence AnalysisAdd
BLAST
Coiled coili1523 – 1667145Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi163 – 17513Glu/Lys-richAdd
BLAST
Compositional biasi1346 – 139247Pro-richAdd
BLAST
Compositional biasi1578 – 158811Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi1678 – 170831Pro-richAdd
BLAST

Domaini

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

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.
HOVERGENiHBG050463.
InParanoidiP55196.
KOiK05702.
OMAiLIPHTRS.
PhylomeDBiP55196.
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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 4 (identifier: P55196-4) [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 ENDAIPPKKA QSNGPEKQEK
160 170 180 190 200
EGVIQNFKRT LSKKEKKEKK KREKEALRQA SDKDDRPFQG EDVENSRLAA
210 220 230 240 250
EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS DGRPDSGGTL
260 270 280 290 300
RIYADSLKPN IPYKTILLST TDPADFAVAE ALEKYGLEKE NPKDYCIARV
310 320 330 340 350
MLPPGAQHSD EKGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDH
360 370 380 390 400
IPKKTKKHLE GKTPKGKERA DGSGYGSTLP PEKLPYLVEL SPGRRNHFAY
410 420 430 440 450
YNYHTYEDGS DSRDKPKLYR LQLSVTEVGT EKLDDNSIQL FGPGIQPHHC
460 470 480 490 500
DLTNMDGVVT VTPRSMDAET YVEGQRISET TMLQSGMKVQ FGASHVFKFV
510 520 530 540 550
DPSQDHALAK RSVDGGLMVK GPRHKPGIVQ ETTFDLGGDI HSGTALPTSK
560 570 580 590 600
STTRLDSDRV SSASSTAERG MVKPMIRVEQ QPDYRRQESR TQDASGPELI
610 620 630 640 650
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSNQY
660 670 680 690 700
RPDISPTERT HKVIAVVNKM 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
TLLTMDKYAP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
910 920 930 940 950
NVVTVAENTA DELARSDGRE VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN
960 970 980 990 1000
GLQEFLDPLC QRGFCRLIPH TRSPGTWTIY FEGADYESHL LRENTELAQP
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 LYNNSTQNGS PESPQLPWAE
1160 1170 1180 1190 1200
YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKSAYA SGTTAKITSV
1210 1220 1230 1240 1250
STGNLCTEEQ TPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQNQWP
1260 1270 1280 1290 1300
NYEEKPHMHT DSNHSSIAIQ RVTRSQEELR EDKAYQLERH RIEAAMDRKS
1310 1320 1330 1340 1350
DSDMWINQSS SLDSSTSSQE HLNHSSKSVT PASTLTKSGP GRWKTPAAIP
1360 1370 1380 1390 1400
ATPVAVSQPI RTDLPPPPPP PPVHYAGDFD GMSMDLPLPP PPSANQIGLP
1410 1420 1430 1440 1450
SAQVAAAERR KREEHQRWYE KEKARLEEER ERKRREQERK LGQMRTQSLN
1460 1470 1480 1490 1500
PAPFSPLTAQ QMKPEKPSTL QRPQETVIRE LQPQQQPRTI ERRDLQYITV
1510 1520 1530 1540 1550
SKEELSSGDS LSPDPWKRDA KEKLEKQQQM HIVDMLSKEI QELQSKPDRS
1560 1570 1580 1590 1600
AEESDRLRKL MLEWQFQKRL QESKQKDEDD EEEEDDDVDT MLIMQRLEAE
1610 1620 1630 1640 1650
RRARLQDEER RRQQQLEEMR KREAEDRARQ EEERRRQEEE RTKRDAEEKR
1660 1670 1680 1690 1700
RQEEGYYSRL EAERRRQHDE AARRLLEPEA PGLCRPPLPR DYEPPSPSPA
1710 1720 1730 1740 1750
PGAPPPPPQR NASYLKTQVL SPDSLFTAKF VAYNEEEEEE DCSLAGPNSY
1760 1770 1780 1790 1800
PGSTGAAVGA HDACRDAKEK RSKSQDADSP GSSGAPENLT FKERQRLFSQ
1810 1820
GQDVSNKVKA SRKLTELENE LNTK
Length:1,824
Mass (Da):206,804
Last modified:February 9, 2010 - v3
Checksum:i51486232F183A3BA
GO
Isoform 1 (identifier: P55196-2) [UniParc]FASTAAdd to basket

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.Curated
Show »
Length:1,612
Mass (Da):182,000
Checksum:i202D7BEC1E825AB6
GO
Isoform 2 (identifier: P55196-1) [UniParc]FASTAAdd to basket

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.
Show »
Length:1,816
Mass (Da):205,605
Checksum:iEB1FE7F04879CE8F
GO
Isoform 3 (identifier: P55196-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:1,743
Mass (Da):197,653
Checksum:iECCDE46AD8C401B9
GO
Isoform 6 (identifier: P55196-6) [UniParc]FASTAAdd to basket

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

Show »
Length:1,651
Mass (Da):187,672
Checksum:i6F55A481FC0DB6B3
GO
Isoform 5 (identifier: P55196-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: Missing.
     1604-1604: R → RTAMPAISVLDL

Note: No experimental confirmation available.
Show »
Length:1,834
Mass (Da):207,788
Checksum:i3D57FDBD6A521DFD
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti374 – 3741G → V in AAC50059 (PubMed:8242616).Curated
Sequence conflicti1425 – 14251R → P in AAC50059 (PubMed:8242616).Curated
Isoform 1 (identifier: P55196-2)
Sequence conflicti1031 – 10322DV → D in AAC50059 (PubMed:8242616).Curated
Sequence conflicti1031 – 10322DV → D in BAA32485 (PubMed:9679199).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 1391Missing in isoform 1, isoform 2, isoform 3 and isoform 5. 2 PublicationsVSP_038707
Alternative sequencei393 – 40715Missing in isoform 1, isoform 2 and isoform 3. 1 PublicationVSP_038708Add
BLAST
Alternative sequencei1048 – 10481Missing in isoform 2 and isoform 3. CuratedVSP_038709
Alternative sequencei1604 – 16041R → RTAMPAISVLDL in isoform 5. 1 PublicationVSP_019257
Alternative sequencei1605 – 162824LQDEE…AEDRA → VKGGVLWLCPSVVPILASAC FPWG in isoform 1. 1 PublicationVSP_000217Add
BLAST
Alternative sequencei1605 – 16062Missing in isoform 6. 1 PublicationVSP_041197
Alternative sequencei1629 – 1824196Missing in isoform 1. 1 PublicationVSP_000218Add
BLAST
Alternative sequencei1650 – 16534RRQE → VMVL in isoform 6. 1 PublicationVSP_041198
Alternative sequencei1654 – 1824171Missing in isoform 6. 1 PublicationVSP_041199Add
BLAST
Alternative sequencei1683 – 174664Missing in isoform 3. CuratedVSP_038710Add
BLAST
Alternative sequencei1747 – 182478PNSYP…ELNTK → QDKYSSTRKSHGDLLPAPLK PRPPPCQPRPASDGVFLSNS FQPPSAKANSTAHKKGQPLP PPKKSSSYHPSHCKGRGKRV TNQLSLS in isoform 2. CuratedVSP_038711Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47517.1. [P55196-6]
CCDS75553.1. [P55196-3]
PIRiT47137.
RefSeqiNP_001035089.1. NM_001040000.2. [P55196-6]
NP_001193937.1. NM_001207008.1. [P55196-3]
NP_001278893.1. NM_001291964.1.
XP_005267053.1. XM_005266996.2. [P55196-4]
UniGeneiHs.614974.
Hs.728849.
Hs.741785.

Genome annotation databases

EnsembliENST00000392108; ENSP00000375956; ENSG00000130396. [P55196-6]
ENST00000392112; ENSP00000375960; ENSG00000130396. [P55196-3]
ENST00000400822; ENSP00000383623; ENSG00000130396. [P55196-5]
ENST00000447894; ENSP00000404595; ENSG00000130396. [P55196-4]
GeneIDi4301.
KEGGihsa:4301.
UCSCiuc003qwb.1. human. [P55196-2]
uc003qwc.2. human. [P55196-6]
uc003qwg.1. human. [P55196-4]
uc021zij.1. human. [P55196-3]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47517.1. [P55196-6]
CCDS75553.1. [P55196-3]
PIRiT47137.
RefSeqiNP_001035089.1. NM_001040000.2. [P55196-6]
NP_001193937.1. NM_001207008.1. [P55196-3]
NP_001278893.1. NM_001291964.1.
XP_005267053.1. XM_005266996.2. [P55196-4]
UniGeneiHs.614974.
Hs.728849.
Hs.741785.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2MNMR-A1003-1094[»]
1XZ9NMR-A1001-1096[»]
2AINNMR-A1003-1094[»]
2EXGNMR-A1001-1096[»]
ProteinModelPortaliP55196.
SMRiP55196. Positions 249-348, 374-503, 605-936, 1001-1096, 1521-1687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110447. 55 interactions.
IntActiP55196. 22 interactions.
MINTiMINT-90828.

PTM databases

PhosphoSiteiP55196.

Polymorphism and mutation databases

BioMutaiMLLT4.
DMDMi288558835.

Proteomic databases

MaxQBiP55196.
PaxDbiP55196.
PRIDEiP55196.

Protocols and materials databases

DNASUi4301.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392108; ENSP00000375956; ENSG00000130396. [P55196-6]
ENST00000392112; ENSP00000375960; ENSG00000130396. [P55196-3]
ENST00000400822; ENSP00000383623; ENSG00000130396. [P55196-5]
ENST00000447894; ENSP00000404595; ENSG00000130396. [P55196-4]
GeneIDi4301.
KEGGihsa:4301.
UCSCiuc003qwb.1. human. [P55196-2]
uc003qwc.2. human. [P55196-6]
uc003qwg.1. human. [P55196-4]
uc021zij.1. human. [P55196-3]

Organism-specific databases

CTDi4301.
GeneCardsiGC06P168227.
HGNCiHGNC:7137. MLLT4.
HPAiCAB013496.
HPA030212.
HPA030213.
HPA030214.
HPA030215.
HPA049868.
MIMi159559. gene.
neXtProtiNX_P55196.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG291597.
GeneTreeiENSGT00390000010033.
HOVERGENiHBG050463.
InParanoidiP55196.
KOiK05702.
OMAiLIPHTRS.
PhylomeDBiP55196.
TreeFamiTF350731.

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
SignaLinkiP55196.

Miscellaneous databases

ChiTaRSiMLLT4. human.
EvolutionaryTraceiP55196.
GeneWikiiMLLT4.
GenomeRNAii4301.
NextBioi16931.
PROiP55196.
SOURCEiSearch...

Gene expression databases

BgeeiP55196.
CleanExiHS_MLLT4.
ExpressionAtlasiP55196. baseline and differential.
GenevisibleiP55196. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-1182; THR-1211; SER-1696 AND SER-1799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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.
  19. Cited for: STRUCTURE BY NMR OF 1001-1095.

Entry informationi

Entry nameiAFAD_HUMAN
AccessioniPrimary (citable) accession number: P55196
Secondary accession number(s): O75087
, O75088, O75089, Q59FP0, Q5TIG6, Q5TIG7, Q9NSN7, Q9NU92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 9, 2010
Last modified: June 24, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.