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Q8NEZ4

- KMT2C_HUMAN

UniProt

Q8NEZ4 - KMT2C_HUMAN

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Protein

Histone-lysine N-methyltransferase 2C

Gene
KMT2C, HALR, KIAA1506, MLL3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. KMT2C/MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei4825 – 48251S-adenosyl-L-methionine By similarity
Metal bindingi4851 – 48511Zinc By similarity
Metal bindingi4899 – 48991Zinc By similarity
Metal bindingi4901 – 49011Zinc By similarity
Metal bindingi4906 – 49061Zinc By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi34 – 4613A.T hookAdd
BLAST
Zinc fingeri341 – 39151PHD-type 1Add
BLAST
Zinc fingeri344 – 38946RING-typeAdd
BLAST
Zinc fingeri388 – 43851PHD-type 2Add
BLAST
Zinc fingeri436 – 48954DHHC-typeAdd
BLAST
Zinc fingeri464 – 52057PHD-type 3Add
BLAST
Zinc fingeri957 – 101054PHD-type 4Add
BLAST
Zinc fingeri1007 – 105751PHD-type 5Add
BLAST
Zinc fingeri1084 – 113956PHD-type 6Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. histone methyltransferase activity (H3-K4 specific) Source: MGI
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3-K4 methylation Source: GOC
  2. intracellular signal transduction Source: InterPro
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase 2C (EC:2.1.1.43)
Short name:
Lysine N-methyltransferase 2C
Alternative name(s):
Homologous to ALR protein
Myeloid/lymphoid or mixed-lineage leukemia protein 3
Gene namesi
Name:KMT2C
Synonyms:HALR, KIAA1506, MLL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:13726. KMT2C.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. histone methyltransferase complex Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 49114911Histone-lysine N-methyltransferase 2CPRO_0000124879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei89 – 891Phosphoserine1 Publication
Modified residuei758 – 7581N6-acetyllysine1 Publication
Modified residuei1301 – 13011Phosphoserine1 Publication
Modified residuei1508 – 15081N6-acetyllysine1 Publication
Modified residuei1772 – 17721N6-acetyllysine1 Publication
Modified residuei2009 – 20091N6-acetyllysine1 Publication
Modified residuei2802 – 28021N6-acetyllysine1 Publication
Modified residuei2809 – 28091N6-acetyllysine1 Publication
Modified residuei2832 – 28321N6-acetyllysine1 Publication
Modified residuei2867 – 28671N6-acetyllysine By similarity
Modified residuei3714 – 37141N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8NEZ4.
PaxDbiQ8NEZ4.
PRIDEiQ8NEZ4.

PTM databases

PhosphoSiteiQ8NEZ4.

Expressioni

Tissue specificityi

Highly expressed in testis and ovary, followed by brain and liver. Also expressed in placenta, peripherical blood, fetal thymus, heart, lung and kidney. Within brain, expression was highest in hippocampus, caudate nucleus, and substantia nigra. Not detected in skeletal muscle and fetal liver.

Gene expression databases

ArrayExpressiQ8NEZ4.
BgeeiQ8NEZ4.
CleanExiHS_MLL3.
GenevestigatoriQ8NEZ4.

Interactioni

Subunit structurei

Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with histone H3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCOA6Q146865EBI-1042997,EBI-78670

Protein-protein interaction databases

BioGridi121835. 20 interactions.
DIPiDIP-48649N.
IntActiQ8NEZ4. 10 interactions.
MINTiMINT-3042700.
STRINGi9606.ENSP00000262189.

Structurei

Secondary structure

1
4911
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni345 – 3473
Turni353 – 3553
Beta strandi356 – 3583
Beta strandi360 – 3623
Turni368 – 3725
Turni377 – 3793
Turni386 – 3883
Turni392 – 3943
Beta strandi403 – 4053
Beta strandi407 – 4093
Beta strandi412 – 4143
Helixi415 – 4173
Beta strandi418 – 4203
Helixi433 – 4364
Helixi1636 – 164510
Helixi1646 – 16483
Beta strandi1650 – 16523
Helixi1653 – 16608
Helixi1664 – 16674
Helixi1671 – 168414
Helixi1687 – 170620
Beta strandi4707 – 47093

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YSMNMR-A342-439[»]
2YUKNMR-A1631-1713[»]
3UVLX-ray2.20B4707-4717[»]
4ERYX-ray1.30D4703-4716[»]
ProteinModelPortaliQ8NEZ4.
SMRiQ8NEZ4. Positions 245-331, 342-439, 482-518, 960-1057, 1086-1138, 1624-1713, 4399-4507, 4761-4911.

Miscellaneous databases

EvolutionaryTraceiQ8NEZ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4545 – 460561FYR N-terminalAdd
BLAST
Domaini4606 – 469186FYR C-terminalAdd
BLAST
Domaini4771 – 4887117SETAdd
BLAST
Domaini4895 – 491117Post-SETAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4848 – 48492S-adenosyl-L-methionine binding By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili92 – 11221 Reviewed predictionAdd
BLAST
Coiled coili644 – 67229 Reviewed predictionAdd
BLAST
Coiled coili1338 – 136629 Reviewed predictionAdd
BLAST
Coiled coili1754 – 178734 Reviewed predictionAdd
BLAST
Coiled coili3054 – 308128 Reviewed predictionAdd
BLAST
Coiled coili3173 – 3272100 Reviewed predictionAdd
BLAST
Coiled coili3391 – 343343 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1719 – 179678Gln-richAdd
BLAST
Compositional biasi1834 – 2281448Pro-richAdd
BLAST
Compositional biasi2412 – 2630219Pro-richAdd
BLAST
Compositional biasi2690 – 278697Asp-richAdd
BLAST
Compositional biasi3012 – 3509498Gln-richAdd
BLAST
Compositional biasi3277 – 3381105Pro-richAdd
BLAST

Domaini

The SET domain interacts with histone H3 but not H2A, H2B and H4, and may have a H3 lysine specific methylation activity.

Sequence similaritiesi

Contains 1 post-SET domain.
Contains 1 SET domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 39151PHD-type 1Add
BLAST
Zinc fingeri344 – 38946RING-typeAdd
BLAST
Zinc fingeri388 – 43851PHD-type 2Add
BLAST
Zinc fingeri436 – 48954DHHC-typeAdd
BLAST
Zinc fingeri464 – 52057PHD-type 3Add
BLAST
Zinc fingeri957 – 101054PHD-type 4Add
BLAST
Zinc fingeri1007 – 105751PHD-type 5Add
BLAST
Zinc fingeri1084 – 113956PHD-type 6Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
HOVERGENiHBG045586.
InParanoidiQ8NEZ4.
KOiK09188.
OMAiMPSLPGW.
PhylomeDBiQ8NEZ4.
TreeFamiTF354317.

Family and domain databases

Gene3Di3.30.40.10. 6 hits.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR009071. HMG_box_dom.
IPR000637. HMGI/Y_DNA-bd_CS.
IPR003616. Post-SET_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR001214. SET_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00384. AT_hook. 2 hits.
SM00109. C1. 2 hits.
SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00398. HMG. 1 hit.
SM00249. PHD. 8 hits.
SM00508. PostSET. 1 hit.
SM00184. RING. 4 hits.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF57903. SSF57903. 6 hits.
PROSITEiPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS50216. ZF_DHHC. 1 hit.
PS01359. ZF_PHD_1. 5 hits.
PS50016. ZF_PHD_2. 6 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NEZ4-1) [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

MSSEEDKSVE QPQPPPPPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR     50
ARKKPRSRGK TAVEDEDSMD GLETTETETI VETEIKEQSA EEDAEAEVDN 100
SKQLIPTLQR SVSEESANSL VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL 150
KQFRITPGFI LPWRNQPSNK KDIDDNSNGT YEKMQNSAPR KQRGQRKERS 200
PQQNIVSCVS VSTQTASDDQ AGKLWDELSL VGLPDAIDIQ ALFDSTGTCW 250
AHHRCVEWSL GVCQMEEPLL VNVDKAVVSG STERCAFCKH LGATIKCCEE 300
KCTQMYHYPC AAGAGTFQDF SHIFLLCPEH IDQAPERSKE DANCAVCDSP 350
GDLLDQFFCT TCGQHYHGMC LDIAVTPLKR AGWQCPECKV CQNCKQSGED 400
SKMLVCDTCD KGYHTFCLQP VMKSVPTNGW KCKNCRICIE CGTRSSSQWH 450
HNCLICDNCY QQQDNLCPFC GKCYHPELQK DMLHCNMCKR WVHLECDKPT 500
DHELDTQLKE EYICMYCKHL GAEMDRLQPG EEVEIAELTT DYNNEMEVEG 550
PEDQMVFSEQ AANKDVNGQE STPGIVPDAV QVHTEEQQKS HPSESLDTDS 600
LLIAVSSQHT VNTELEKQIS NEVDSEDLKM SSEVKHICGE DQIEDKMEVT 650
ENIEVVTHQI TVQQEQLQLL EEPETVVSRE ESRPPKLVME SVTLPLETLV 700
SPHEESISLC PEEQLVIERL QGEKEQKENS ELSTGLMDSE MTPTIEGCVK 750
DVSYQGGKSI KLSSETESSF SSSADISKAD VSSSPTPSSD LPSHDMLHNY 800
PSALSSSAGN IMPTTYISVT PKIGMGKPAI TKRKFSPGRP RSKQGAWSTH 850
NTVSPPSWSP DISEGREIFK PRQLPGSAIW SIKVGRGSGF PGKRRPRGAG 900
LSGRGGRGRS KLKSGIGAVV LPGVSTADIS SNKDDEENSM HNTVVLFSSS 950
DKFTLNQDMC VVCGSFGQGA EGRLLACSQC GQCYHPYCVS IKITKVVLSK 1000
GWRCLECTVC EACGKATDPG RLLLCDDCDI SYHTYCLDPP LQTVPKGGWK 1050
CKWCVWCRHC GATSAGLRCE WQNNYTQCAP CASLSSCPVC YRNYREEDLI 1100
LQCRQCDRWM HAVCQNLNTE EEVENVADIG FDCSMCRPYM PASNVPSSDC 1150
CESSLVAQIV TKVKELDPPK TYTQDGVCLT ESGMTQLQSL TVTVPRRKRS 1200
KPKLKLKIIN QNSVAVLQTP PDIQSEHSRD GEMDDSREGE LMDCDGKSES 1250
SPEREAVDDE TKGVEGTDGV KKRKRKPYRP GIGGFMVRQR SRTGQGKTKR 1300
SVIRKDSSGS ISEQLPCRDD GWSEQLPDTL VDESVSVTES TEKIKKRYRK 1350
RKNKLEETFP AYLQEAFFGK DLLDTSRQSK ISLDNLSEDG AQLLYKTNMN 1400
TGFLDPSLDP LLSSSSAPTK SGTHGPADDP LADISEVLNT DDDILGIISD 1450
DLAKSVDHSD IGPVTDDPSS LPQPNVNQSS RPLSEEQLDG ILSPELDKMV 1500
TDGAILGKLY KIPELGGKDV EDLFTAVLSP ANTQPTPLPQ PPPPTQLLPI 1550
HNQDAFSRMP LMNGLIGSSP HLPHNSLPPG SGLGTFSAIA QSSYPDARDK 1600
NSAFNPMASD PNNSWTSSAP TVEGENDTMS NAQRSTLKWE KEEALGEMAT 1650
VAPVLYTNIN FPNLKEEFPD WTTRVKQIAK LWRKASSQER APYVQKARDN 1700
RAALRINKVQ MSNDSMKRQQ QQDSIDPSSR IDSELFKDPL KQRESEHEQE 1750
WKFRQQMRQK SKQQAKIEAT QKLEQVKNEQ QQQQQQQFGS QHLLVQSGSD 1800
TPSSGIQSPL TPQPGNGNMS PAQSFHKELF TKQPPSTPTS TSSDDVFVKP 1850
QAPPPPPAPS RIPIQDSLSQ AQTSQPPSPQ VFSPGSSNSR PPSPMDPYAK 1900
MVGTPRPPPV GHSFSRRNSA APVENCTPLS SVSRPLQMNE TTANRPSPVR 1950
DLCSSSTTNN DPYAKPPDTP RPVMTDQFPK SLGLSRSPVV SEQTAKGPIA 2000
AGTSDHFTKP SPRADVFQRQ RIPDSYARPL LTPAPLDSGP GPFKTPMQPP 2050
PSSQDPYGSV SQASRRLSVD PYERPALTPR PIDNFSHNQS NDPYSQPPLT 2100
PHPAVNESFA HPSRAFSQPG TISRPTSQDP YSQPPGTPRP VVDSYSQSSG 2150
TARSNTDPYS QPPGTPRPTT VDPYSQQPQT PRPSTQTDLF VTPVTNQRHS 2200
DPYAHPPGTP RPGISVPYSQ PPATPRPRIS EGFTRSSMTR PVLMPNQDPF 2250
LQAAQNRGPA LPGPLVRPPD TCSQTPRPPG PGLSDTFSRV SPSAARDPYD 2300
QSPMTPRSQS DSFGTSQTAH DVADQPRPGS EGSFCASSNS PMHSQGQQFS 2350
GVSQLPGPVP TSGVTDTQNT VNMAQADTEK LRQRQKLREI ILQQQQQKKI 2400
AGRQEKGSQD SPAVPHPGPL QHWQPENVNQ AFTRPPPPYP GNIRSPVAPP 2450
LGPRYAVFPK DQRGPYPPDV ASMGMRPHGF RFGFPGGSHG TMPSQERFLV 2500
PPQQIQGSGV SPQLRRSVSV DMPRPLNNSQ MNNPVGLPQH FSPQSLPVQQ 2550
HNILGQAYIE LRHRAPDGRQ RLPFSAPPGS VVEASSNLRH GNFIPRPDFP 2600
GPRHTDPMRR PPQGLPNQLP VHPDLEQVPP SQQEQGHSVH SSSMVMRTLN 2650
HPLGGEFSEA PLSTSVPSET TSDNLQITTQ PSDGLEEKLD SDDPSVKELD 2700
VKDLEGVEVK DLDDEDLENL NLDTEDGKVV ELDTLDNLET NDPNLDDLLR 2750
SGEFDIIAYT DPELDMGDKK SMFNEELDLP IDDKLDNQCV SVEPKKKEQE 2800
NKTLVLSDKH SPQKKSTVTN EVKTEVLSPN SKVESKCETE KNDENKDNVD 2850
TPCSQASAHS DLNDGEKTSL HPCDPDLFEK RTNRETAGPS ANVIQASTQL 2900
PAQDVINSCG ITGSTPVLSS LLANEKSDNS DIRPSGSPPP PTLPASPSNH 2950
VSSLPPFIAP PGRVLDNAMN SNVTVVSRVN HVFSQGVQVN PGLIPGQSTV 3000
NHSLGTGKPA TQTGPQTSQS GTSSMSGPQQ LMIPQTLAQQ NRERPLLLEE 3050
QPLLLQDLLD QERQEQQQQR QMQAMIRQRS EPFFPNIDFD AITDPIMKAK 3100
MVALKGINKV MAQNNLGMPP MVMSRFPFMG QVVTGTQNSE GQNLGPQAIP 3150
QDGSITHQIS RPNPPNFGPG FVNDSQRKQY EEWLQETQQL LQMQQKYLEE 3200
QIGAHRKSKK ALSAKQRTAK KAGREFPEED AEQLKHVTEQ QSMVQKQLEQ 3250
IRKQQKEHAE LIEDYRIKQQ QQCAMAPPTM MPSVQPQPPL IPGATPPTMS 3300
QPTFPMVPQQ LQHQQHTTVI SGHTSPVRMP SLPGWQPNSA PAHLPLNPPR 3350
IQPPIAQLPI KTCTPAPGTV SNANPQSGPP PRVEFDDNNP FSESFQERER 3400
KERLREQQER QRIQLMQEVD RQRALQQRME MEQHGMVGSE ISSSRTSVSQ 3450
IPFYSSDLPC DFMQPLGPLQ QSPQHQQQMG QVLQQQNIQQ GSINSPSTQT 3500
FMQTNERRQV GPPSFVPDSP SIPVGSPNFS SVKQGHGNLS GTSFQQSPVR 3550
PSFTPALPAA PPVANSSLPC GQDSTITHGH SYPGSTQSLI QLYSDIIPEE 3600
KGKKKRTRKK KRDDDAESTK APSTPHSDIT APPTPGISET TSTPAVSTPS 3650
ELPQQADQES VEPVGPSTPN MAAGQLCTEL ENKLPNSDFS QATPNQQTYA 3700
NSEVDKLSME TPAKTEEIKL EKAETESCPG QEEPKLEEQN GSKVEGNAVA 3750
CPVSSAQSPP HSAGAPAAKG DSGNELLKHL LKNKKSSSLL NQKPEGSICS 3800
EDDCTKDNKL VEKQNPAEGL QTLGAQMQGG FGCGNQLPKT DGGSETKKQR 3850
SKRTQRTGEK AAPRSKKRKK DEEEKQAMYS STDTFTHLKQ QNNLSNPPTP 3900
PASLPPTPPP MACQKMANGF ATTEELAGKA GVLVSHEVTK TLGPKPFQLP 3950
FRPQDDLLAR ALAQGPKTVD VPASLPTPPH NNQEELRIQD HCGDRDTPDS 4000
FVPSSSPESV VGVEVSRYPD LSLVKEEPPE PVPSPIIPIL PSTAGKSSES 4050
RRNDIKTEPG TLYFASPFGP SPNGPRSGLI SVAITLHPTA AENISSVVAA 4100
FSDLLHVRIP NSYEVSSAPD VPSMGLVSSH RINPGLEYRQ HLLLRGPPPG 4150
SANPPRLVSS YRLKQPNVPF PPTSNGLSGY KDSSHGIAES AALRPQWCCH 4200
CKVVILGSGV RKSFKDLTLL NKDSRESTKR VEKDIVFCSN NCFILYSSTA 4250
QAKNSENKES IPSLPQSPMR ETPSKAFHQY SNNISTLDVH CLPQLPEKAS 4300
PPASPPIAFP PAFEAAQVEA KPDELKVTVK LKPRLRAVHG GFEDCRPLNK 4350
KWRGMKWKKW SIHIVIPKGT FKPPCEDEID EFLKKLGTSL KPDPVPKDYR 4400
KCCFCHEEGD GLTDGPARLL NLDLDLWVHL NCALWSTEVY ETQAGALINV 4450
ELALRRGLQM KCVFCHKTGA TSGCHRFRCT NIYHFTCAIK AQCMFFKDKT 4500
MLCPMHKPKG IHEQELSYFA VFRRVYVQRD EVRQIASIVQ RGERDHTFRV 4550
GSLIFHTIGQ LLPQQMQAFH SPKALFPVGY EASRLYWSTR YANRRCRYLC 4600
SIEEKDGRPV FVIRIVEQGH EDLVLSDISP KGVWDKILEP VACVRKKSEM 4650
LQLFPAYLKG EDLFGLTVSA VARIAESLPG VEACENYTFR YGRNPLMELP 4700
LAVNPTGCAR SEPKMSAHVK RFVLRPHTLN STSTSKSFQS TVTGELNAPY 4750
SKQFVHSKSS QYRKMKTEWK SNVYLARSRI QGLGLYAARD IEKHTMVIEY 4800
IGTIIRNEVA NRKEKLYESQ NRGVYMFRMD NDHVIDATLT GGPARYINHS 4850
CAPNCVAEVV TFERGHKIII SSSRRIQKGE ELCYDYKFDF EDDQHKIPCH 4900
CGAVNCRKWM N 4911
Length:4,911
Mass (Da):541,370
Last modified:January 20, 2009 - v3
Checksum:i898CEE324772BD75
GO
Isoform 2 (identifier: Q8NEZ4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-939: Missing.
     3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK
     4721-4724: Missing.

Note: No experimental confirmation available.

Show »
Length:4,025
Mass (Da):443,538
Checksum:i41624149C28E4BDE
GO
Isoform 3 (identifier: Q8NEZ4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK

Note: No experimental confirmation available.

Show »
Length:4,968
Mass (Da):547,633
Checksum:i7D6E36D9FA78714B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti291 – 2911L → F.
Corresponds to variant rs56850341 [ dbSNP | Ensembl ].
VAR_061911
Natural varianti316 – 3161T → S.
Corresponds to variant rs10454320 [ dbSNP | Ensembl ].
VAR_061912
Natural varianti347 – 3471C → G in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036311
Natural varianti400 – 4001D → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036312
Natural varianti478 – 4781L → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036313
Natural varianti526 – 5261R → P.1 Publication
Corresponds to variant rs3735156 [ dbSNP | Ensembl ].
VAR_057360
Natural varianti823 – 8231I → N.
Corresponds to variant rs2838171 [ dbSNP | Ensembl ].
VAR_017118
Natural varianti823 – 8231I → T.
Corresponds to variant rs2838171 [ dbSNP | Ensembl ].
VAR_017117
Natural varianti1836 – 18361S → N.
Corresponds to variant rs11771635 [ dbSNP | Ensembl ].
VAR_057361
Natural varianti2008 – 20081T → A.
Corresponds to variant rs6951159 [ dbSNP | Ensembl ].
VAR_057362
Natural varianti2412 – 24121P → T.
Corresponds to variant rs13231116 [ dbSNP | Ensembl ].
VAR_057363
Natural varianti2600 – 26001P → A.
Corresponds to variant rs2270234 [ dbSNP | Ensembl ].
VAR_057364
Natural varianti3698 – 36981T → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036314

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 939939Missing in isoform 2. VSP_008561Add
BLAST
Alternative sequencei3890 – 38901Q → QVRQLSLLPLMEPIIGVNFA HFLPYGSGQFNSGNRLLGTF GSATLEGVSDYYSQLIYK in isoform 2 and isoform 3. VSP_008562
Alternative sequencei4721 – 47244Missing in isoform 2. VSP_036223

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti579 – 5791A → T in AAK00583. 1 Publication
Sequence conflicti1286 – 12861M → V in AAK00583. 1 Publication
Sequence conflicti2360 – 23601P → S in AAK00583. 1 Publication
Sequence conflicti2797 – 27971K → R in AAK00583. 1 Publication
Sequence conflicti2882 – 28821T → A in AAK00583. 1 Publication
Sequence conflicti3289 – 32891P → S in BAC11409. 1 Publication
Sequence conflicti3428 – 34281R → W in BAC11409. 1 Publication
Sequence conflicti4613 – 46131I → V in AK022687. 1 Publication
Sequence conflicti4866 – 48661H → P in AK022687. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY024361 mRNA. Translation: AAK00583.1.
AF264750 mRNA. Translation: AAF74766.2.
AC006017 Genomic DNA. Translation: AAD45822.1.
AC104692 Genomic DNA. No translation available.
AC005631 Genomic DNA. No translation available.
AB040939 mRNA. Translation: BAA96030.2.
AK022687 mRNA. No translation available.
AK075113 mRNA. Translation: BAC11409.1.
AL833924 mRNA. Translation: CAD38780.1.
CCDSiCCDS5931.1. [Q8NEZ4-1]
RefSeqiNP_733751.2. NM_170606.2. [Q8NEZ4-1]
UniGeneiHs.647120.

Genome annotation databases

EnsembliENST00000262189; ENSP00000262189; ENSG00000055609. [Q8NEZ4-1]
ENST00000355193; ENSP00000347325; ENSG00000055609. [Q8NEZ4-3]
GeneIDi58508.
KEGGihsa:58508.
UCSCiuc003wkz.3. human. [Q8NEZ4-2]
uc003wla.3. human. [Q8NEZ4-1]

Polymorphism databases

DMDMi221222521.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY024361 mRNA. Translation: AAK00583.1 .
AF264750 mRNA. Translation: AAF74766.2 .
AC006017 Genomic DNA. Translation: AAD45822.1 .
AC104692 Genomic DNA. No translation available.
AC005631 Genomic DNA. No translation available.
AB040939 mRNA. Translation: BAA96030.2 .
AK022687 mRNA. No translation available.
AK075113 mRNA. Translation: BAC11409.1 .
AL833924 mRNA. Translation: CAD38780.1 .
CCDSi CCDS5931.1. [Q8NEZ4-1 ]
RefSeqi NP_733751.2. NM_170606.2. [Q8NEZ4-1 ]
UniGenei Hs.647120.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YSM NMR - A 342-439 [» ]
2YUK NMR - A 1631-1713 [» ]
3UVL X-ray 2.20 B 4707-4717 [» ]
4ERY X-ray 1.30 D 4703-4716 [» ]
ProteinModelPortali Q8NEZ4.
SMRi Q8NEZ4. Positions 245-331, 342-439, 482-518, 960-1057, 1086-1138, 1624-1713, 4399-4507, 4761-4911.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121835. 20 interactions.
DIPi DIP-48649N.
IntActi Q8NEZ4. 10 interactions.
MINTi MINT-3042700.
STRINGi 9606.ENSP00000262189.

Chemistry

ChEMBLi CHEMBL2189113.

PTM databases

PhosphoSitei Q8NEZ4.

Polymorphism databases

DMDMi 221222521.

Proteomic databases

MaxQBi Q8NEZ4.
PaxDbi Q8NEZ4.
PRIDEi Q8NEZ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262189 ; ENSP00000262189 ; ENSG00000055609 . [Q8NEZ4-1 ]
ENST00000355193 ; ENSP00000347325 ; ENSG00000055609 . [Q8NEZ4-3 ]
GeneIDi 58508.
KEGGi hsa:58508.
UCSCi uc003wkz.3. human. [Q8NEZ4-2 ]
uc003wla.3. human. [Q8NEZ4-1 ]

Organism-specific databases

CTDi 58508.
GeneCardsi GC07M151835.
H-InvDB HIX0007238.
HIX0016202.
HIX0080234.
HGNCi HGNC:13726. KMT2C.
MIMi 606833. gene.
neXtProti NX_Q8NEZ4.
PharmGKBi PA30847.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
HOVERGENi HBG045586.
InParanoidi Q8NEZ4.
KOi K09188.
OMAi MPSLPGW.
PhylomeDBi Q8NEZ4.
TreeFami TF354317.

Miscellaneous databases

ChiTaRSi MLL3. human.
EvolutionaryTracei Q8NEZ4.
GeneWikii MLL3.
GenomeRNAii 58508.
NextBioi 65023.
PROi Q8NEZ4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8NEZ4.
Bgeei Q8NEZ4.
CleanExi HS_MLL3.
Genevestigatori Q8NEZ4.

Family and domain databases

Gene3Di 3.30.40.10. 6 hits.
InterProi IPR017956. AT_hook_DNA-bd_motif.
IPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR009071. HMG_box_dom.
IPR000637. HMGI/Y_DNA-bd_CS.
IPR003616. Post-SET_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR001214. SET_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00384. AT_hook. 2 hits.
SM00109. C1. 2 hits.
SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00398. HMG. 1 hit.
SM00249. PHD. 8 hits.
SM00508. PostSET. 1 hit.
SM00184. RING. 4 hits.
SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 1 hit.
SSF57903. SSF57903. 6 hits.
PROSITEi PS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS50216. ZF_DHHC. 1 hit.
PS01359. ZF_PHD_1. 5 hits.
PS50016. ZF_PHD_2. 6 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia."
    Ruault M., Brun M.-E., Ventura M., Roizes G., De Sario A.
    Gene 284:73-81(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-526.
    Tissue: Fetal thymus.
  2. "Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with leukemia and developmental defects."
    Tan Y.C., Chow V.T.
    Cancer Detect. Prev. 25:454-469(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Cervix carcinoma.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-3865 (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3193-3865 AND 4460-4911.
    Tissue: Placenta.
  7. Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Testis.
  8. "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins."
    Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J., Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.
    Mol. Cell. Biol. 23:140-149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MLL2/3 COMPLEX (ISOFORM 2).
    Tissue: Cervix carcinoma.
  9. "Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases."
    Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K., Roeder R.G., Lee J.W.
    Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
  10. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
    Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
    J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-758; LYS-1508; LYS-1772; LYS-2009; LYS-2802; LYS-2809; LYS-2832 AND LYS-3714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-1301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Solution structure of the first and second PHD domain from myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 342-439.
  16. "Solution structure of the HMG box of human myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1624-1713.
  17. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-347; ASN-400; TRP-478 AND SER-3698.

Entry informationi

Entry nameiKMT2C_HUMAN
AccessioniPrimary (citable) accession number: Q8NEZ4
Secondary accession number(s): Q8NC02
, Q8NDF6, Q9H9P4, Q9NR13, Q9P222, Q9UDR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: January 20, 2009
Last modified: July 9, 2014
This is version 130 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

Miscellaneous

Found in a critical region of chromosome 7, which is commonly deleted in malignant myeloid disorders. Partial duplication of the KMT2C gene are found in the juxtacentromeric region of chromosomes 1, 2, 13 and 21. Juxtacentromeric reshuffling of the KMT2C gene has generated the BAGE genes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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