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Protein

E3 ubiquitin-protein ligase MYCBP2

Gene

MYCBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (PubMed:29643511). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (PubMed:29643511). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (PubMed:18308511, PubMed:29643511). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (Probable). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required for the formation of major central nervous system axon tracts (By similarity). Required for proper axon growth by regulating axon navigation and axon branching: acts by regulating the subcellular location and stability of MAP3K12/DLK (By similarity). Required for proper localization of retinogeniculate projections but not for eye-specific segregation (By similarity). Regulates axon guidance in the olfactory system (By similarity). Involved in Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons: acts by promoting destabilization of NMNAT2, probably via ubiquitination of NMNAT2 (By similarity). Catalyzes ubiquitination of threonine and/or serine residues on NMNAT2, consequences of threonine and/or serine ubiquitination are however unknown (PubMed:29643511). Regulates the internalization of TRPV1 in peripheral sensory neurons (By similarity). May mediate ubiquitination and subsequent proteasomal degradation of TSC2/tuberin (PubMed:18308511). Independently of the E3 ubiquitin-protein ligase activity, also acts as a guanosine exchange factor (GEF) for RAN in neurons of dorsal root ganglia (PubMed:26304119). May function as a facilitator or regulator of transcriptional activation by MYC (PubMed:9689053).By similarity4 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-threonine.1 Publication
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-serine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-serine.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi4428Zinc 1Combined sources1 Publication1
Metal bindingi4431Zinc 1Combined sources1 Publication1
Metal bindingi4446Zinc 2Combined sources1 Publication1
Metal bindingi4448Zinc 2Combined sources1 Publication1
Metal bindingi4451Zinc 1Combined sources1 Publication1
Metal bindingi4454Zinc 1Combined sources1 Publication1
Metal bindingi4475Zinc 2Combined sources1 Publication1
Metal bindingi4478Zinc 2Combined sources1 Publication1
Metal bindingi4544Zinc 3Combined sources1 Publication1
Metal bindingi4547Zinc 3Combined sources1 Publication1
Active sitei45581 Publication1
Metal bindingi4575Zinc 3Combined sources1 Publication1
Metal bindingi4578Zinc 3Combined sources1 Publication1
Metal bindingi4587Zinc 4Combined sources1 Publication1
Metal bindingi4590Zinc 4Combined sources1 Publication1
Metal bindingi4599Zinc 5Combined sources1 Publication1
Metal bindingi4602Zinc 5Combined sources1 Publication1
Metal bindingi4603Zinc 6Combined sources1 Publication1
Active sitei46101 Publication1
Sitei4611Important for catalysis1 Publication1
Sitei4616Important for catalysis1 Publication1
Metal bindingi4617Zinc 5Combined sources1 Publication1
Metal bindingi4620Zinc 5Combined sources1 Publication1
Sitei4624Important for catalysis1 Publication1
Metal bindingi4638Zinc 6Combined sources1 Publication1
Metal bindingi4652Zinc 6Combined sources1 Publication1
Metal bindingi4658Zinc 6Combined sources1 Publication1
Metal bindingi4669Zinc 4Combined sources1 Publication1
Metal bindingi4672Zinc 4Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri4428 – 4479RING-type; atypicalPROSITE-ProRule annotationAdd BLAST52
Zinc fingeri4582 – 4632B box-typeAdd BLAST51

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGuanine-nucleotide releasing factor, Transferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MYCBP2Curated (EC:2.3.2.-1 Publication)
Alternative name(s):
Myc-binding protein 2Curated
Protein associated with Myc1 Publication
Gene namesi
Name:MYCBP2Imported
Synonyms:KIAA09161 Publication, PAM1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000005810.17
HGNCiHGNC:23386 MYCBP2
MIMi610392 gene
neXtProtiNX_O75592

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4558C → S: Abolished E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi4572E → A or Q: Does not affect E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi4610C → A: Increased thiol-sensitive adduct formation. 1 Publication1
Mutagenesisi4610C → S: Retains activity while also forming a discrete monoubiquitin adduct that is resistant to thiolysis but is reversible after base treatment. 1 Publication1
Mutagenesisi4611F → A: Reduced E3 ubiquitin-protein ligase activity in threonine discharge assay. 1 Publication1
Mutagenesisi4616F → A: Reduced E3 ubiquitin-protein ligase activity in threonine discharge assay. 1 Publication1
Mutagenesisi4621H → N: Abolished E3 ubiquitin-protein ligase activity in threonine discharge assay, associated with enhanced thiol-sensitive ubiquitin adduct formation. 1 Publication1
Mutagenesisi4624F → A: Reduced E3 ubiquitin-protein ligase activity in threonine discharge assay. 1 Publication1

Organism-specific databases

DisGeNETi23077
PharmGKBiPA134871126

Polymorphism and mutation databases

BioMutaiMYCBP2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000559631 – 4678E3 ubiquitin-protein ligase MYCBP2Add BLAST4678

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei127PhosphoserineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei181PhosphoserineCombined sources1
Modified residuei183PhosphoserineCombined sources1
Modified residuei1624PhosphoserineCombined sources1
Disulfide bondi1748 ↔ 1863By similarity
Modified residuei2683PhosphothreonineCombined sources1
Modified residuei2769PhosphoserineCombined sources1
Modified residuei2787PhosphoserineCombined sources1
Modified residuei2789PhosphoserineCombined sources1
Modified residuei2833PhosphoserineCombined sources1
Modified residuei2839PhosphoserineCombined sources1
Modified residuei2869PhosphoserineBy similarity1
Modified residuei2871PhosphoserineCombined sources1
Modified residuei2920PhosphoserineCombined sources1
Modified residuei2985PhosphoserineCombined sources1
Modified residuei3090PhosphoserineCombined sources1
Modified residuei3478PhosphoserineCombined sources1
Modified residuei3505PhosphoserineCombined sources1
Modified residuei3921PhosphothreonineBy similarity1
Modified residuei3931PhosphoserineCombined sources1
Modified residuei3932PhosphoserineCombined sources1

Post-translational modificationi

Autoubiquitinated.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75592
MaxQBiO75592
PaxDbiO75592
PeptideAtlasiO75592
PRIDEiO75592
ProteomicsDBi50101
50102 [O75592-2]

PTM databases

iPTMnetiO75592
PhosphoSitePlusiO75592

Expressioni

Tissue specificityi

Expressed in all tissues examined, expression is exceptionally abundant in brain and thymus. Colocalizes with TSC1 and TSC2 along the neurites and in the growth cones. Highly expressed in peripheral and central neurons. Colocalized with TSC1 in one of the filopodial extensions at the tip of a growth cone.1 Publication

Gene expression databases

BgeeiENSG00000005810 Expressed in 244 organ(s), highest expression level in primary visual cortex
CleanExiHS_MYCBP2
HS_PAM
ExpressionAtlasiO75592 baseline and differential
GenevisibleiO75592 HS

Organism-specific databases

HPAiHPA058807

Interactioni

Subunit structurei

Interacts with MYC (PubMed:9689053). Interacts with TSC2 (tuberin) when TSC2 is in complex with TSC1 (hamartin) (PubMed:14559897). Interacts with FBXO45 (PubMed:19398581). Interacts with RAE1 (PubMed:22357847). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with (sumoylated) RANGAP1; interaction with sumoylated RANGAP1 inhibits E3 ubiquitin-protein ligase activity and promotes MYCBP2 translocation to the nucleus (PubMed:26304119). Interacts with RAN (PubMed:26304119). Interacts with RAN (PubMed:26304119).By similarity5 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116709, 86 interactors
DIPiDIP-28142N
IntActiO75592, 51 interactors
MINTiO75592
STRINGi9606.ENSP00000384288

Structurei

Secondary structure

14678
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO75592
SMRiO75592
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati600 – 655RCC1 1Sequence analysisAdd BLAST56
Repeati699 – 755RCC1 2Sequence analysisAdd BLAST57
Repeati907 – 957RCC1 3Sequence analysisAdd BLAST51
Repeati958 – 1008RCC1 4Sequence analysisAdd BLAST51
Repeati1010 – 1066RCC1 5Sequence analysisAdd BLAST57
Repeati2341 – 2443FilaminSequence analysisAdd BLAST103
Domaini3719 – 3897DOCPROSITE-ProRule annotationAdd BLAST179

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1235 – 1386PHR domain 1By similarityAdd BLAST152
Regioni1726 – 1884PHR domain 2By similarityAdd BLAST159
Regioni2022 – 2550RAE1 binding1 PublicationAdd BLAST529
Regioni4539 – 4676Tandem cysteine domain1 PublicationAdd BLAST138

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi103 – 126Lys-richSequence analysisAdd BLAST24
Compositional biasi766 – 814Cys-richSequence analysisAdd BLAST49
Compositional biasi2720 – 2844Ser-richSequence analysisAdd BLAST125
Compositional biasi3194 – 3215Lys-richSequence analysisAdd BLAST22
Compositional biasi3262 – 3293Gly-richAdd BLAST32

Domaini

The PHR domains are compact beta-sandwich folds composed of 11 antiparallel strands and decorated with conserved apical loops. They are likely to play a structural role and mediate interactions with substrates or partners (By similarity).By similarity
The tandem cysteine domain region confers threonine specificity and contains the two essential catalytic cysteine residues that relay ubiquitin. It binds four zinc ions in a C5HC7HC2 configuration.1 Publication

Sequence similaritiesi

Belongs to the RING-Cys relay (RCR) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri4428 – 4479RING-type; atypicalPROSITE-ProRule annotationAdd BLAST52
Zinc fingeri4582 – 4632B box-typeAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1428 Eukaryota
ENOG410XP1T LUCA
HOVERGENiHBG053153
InParanoidiO75592
KOiK10693
OMAiTVSVECF
OrthoDBiEOG091G0018
PhylomeDBiO75592
TreeFamiTF313151

Family and domain databases

Gene3Di2.130.10.30, 2 hits
2.60.120.260, 1 hit
2.60.120.820, 2 hits
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR004939 APC_su10/DOC_dom
IPR017868 Filamin/ABP280_repeat-like
IPR008979 Galactose-bd-like_sf
IPR014756 Ig_E-set
IPR012983 PHR
IPR038648 PHR_sf
IPR009091 RCC1/BLIP-II
IPR000408 Reg_chr_condens
IPR003646 SH3-like_bac-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF03256 ANAPC10, 1 hit
PF08005 PHR, 2 hits
PF00415 RCC1, 1 hit
PF08239 SH3_3, 1 hit
PF13639 zf-RING_2, 1 hit
PRINTSiPR00633 RCCNDNSATION
SMARTiView protein in SMART
SM01337 APC10, 1 hit
SM00184 RING, 1 hit
SUPFAMiSSF49785 SSF49785, 1 hit
SSF50985 SSF50985, 2 hits
SSF81296 SSF81296, 2 hits
PROSITEiView protein in PROSITE
PS51284 DOC, 1 hit
PS50194 FILAMIN_REPEAT, 1 hit
PS00626 RCC1_2, 2 hits
PS50012 RCC1_3, 3 hits
PS50089 ZF_RING_2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 11 Publication (identifier: O75592-1) [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.

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        10         20         30         40         50
MMMCAATASP AAASSGLGGD GFYPAATFSS SPAPGALFMP VPDGSVAAAG
60 70 80 90 100
LGLGLPAADS RGHYQLLLSG RALADRYRRI YTAALNDRDQ GGGSAGHPAS
110 120 130 140 150
RNKKILNKKK LKRKQKSKSK VKTRSKSENL ENTVIIPDIK LHSNPSAFNI
160 170 180 190 200
YCNVRHCVLE WQKKEISLAA ASKNSVQSGE SDSDEEEESK EPPIKLPKII
210 220 230 240 250
EVGLCEVFEL IKETRFSHPS LCLRSLQALL NVLQGQQPEG LQSEPPEVLE
260 270 280 290 300
SLFQLLLEIT VRSTGMNDST GQSLTALSCA CLFSLVASWG ETGRTLQAIS
310 320 330 340 350
AILTNNGSHA CQTIQVPTIL NSLQRSVQAV LVGKIQIQDW FSNGIKKAAL
360 370 380 390 400
MHKWPLKEIS VDEDDQCLLQ NDGFFLYLLC KDGLYKIGSG YSGTVRGHIY
410 420 430 440 450
NSTSRIRNRK EKKSWLGYAQ GYLLYRDVNN HSMTAIRISP ETLEQDGTVM
460 470 480 490 500
LPDCHTEGQN ILFTDGEYIN QIAASRDDGF VVRIFATSTE PVLQQELQLK
510 520 530 540 550
LARKCLHACG ISLFDLEKDL HIISTGFDEE SAILGAGREF ALMKTANGKI
560 570 580 590 600
YYTGKYQSLG IKQGGPSAGK WVELPITKSP KIVHFSVGHD GSHALLVAED
610 620 630 640 650
GSIFFTGSAS KGEDGESTKS RRQSKPYKPK KIIKMEGKIV VYTACNNGSS
660 670 680 690 700
SVISKDGELY MFGKDAIYSD SSSLVTDLKG HFVTQVAMGK AHTCVLMKNG
710 720 730 740 750
EVWTFGVNNK GQCGRDTGAM NQGGKGFGVE NMATAMDEDL EEELDEKDEK
760 770 780 790 800
SMMCPPGMHK WKLEQCMVCT VCGDCTGYGA SCVSSGRPDR VPGGICGCGS
810 820 830 840 850
GESGCAVCGC CKACARELDG QEARQRGILD AVKEMIPLDL LLAVPVPGVN
860 870 880 890 900
IEEHLQLRQE EKRQRVIRRH RLEEGRGPLV FAGPIFMNHR EQALARLRSH
910 920 930 940 950
PAQLKHKRDK HKDGSGERGE KDASKITTYP PGSVRFDCEL RAVQVSCGFH
960 970 980 990 1000
HSVVLMENGD VYTFGYGQHG QLGHGDVNSR GCPTLVQALP GPSTQVTAGS
1010 1020 1030 1040 1050
NHTAVLLMDG QVFTFGSFSK GQLGRPILDV PYWNAKPAPM PNIGSKYGRK
1060 1070 1080 1090 1100
ATWIGASGDQ TFLRIDEALI NSHVLATSEI FASKHIIGLV PASISEPPPF
1110 1120 1130 1140 1150
KCLLINKVDG SCKTFNDSEQ EDLQGFGVCL DPVYDVIWRF RPNTRELWCY
1160 1170 1180 1190 1200
NAVVADARLP SAADMQSRCS ILSPELALPT GSRALTTRSH AALHILGCLD
1210 1220 1230 1240 1250
TLAAMQDLKM GVASTEEETQ AVMKVYSKED YSVVNRFESH GGGWGYSAHS
1260 1270 1280 1290 1300
VEAIRFSADT DILLGGLGLF GGRGEYTAKI KLFELGPDGG DHETDGDLLA
1310 1320 1330 1340 1350
ETDVLAYDCA AREKYAMMFD EPVLLQAGWW YVAWARVSGP SSDCGSHGQA
1360 1370 1380 1390 1400
SITTDDGVVF QFKSSKKSNN GTDVNAGQIP QLLYRLPTSD GSASKGKQQT
1410 1420 1430 1440 1450
SEPVHILKRS FARTVSVECF ESLLSILHWS WTTLVLGVEE LRGLKGFQFT
1460 1470 1480 1490 1500
ATLLDLERLR FVGTCCLRLL RVYTCEIYPV SATGKAVVEE TSKLAECIGK
1510 1520 1530 1540 1550
TRTLLRKILS EGVDHCMVKL DNDPQGYLSQ PLSLLEAVLQ ECHNTFTACF
1560 1570 1580 1590 1600
HSFYPTPALQ WACLCDLLNC LDQDIQEANF KTSSSRLLAA VMSALCHTSV
1610 1620 1630 1640 1650
KLTSIFPIAY DGEVLLRSIV KQVSTENDST LVHRFPLLVA HMEKLSQSEE
1660 1670 1680 1690 1700
NISGMTSFRE VLEKMLVIVV LPVRNSLRRE NELFSSHLVS NTCGLLASIV
1710 1720 1730 1740 1750
SELTASALGS EVDGLNSLHS VKASANRFTK TSQGRSWNTG NGSPDAICFS
1760 1770 1780 1790 1800
VDKPGIVVVG FSVYGGGGIH EYELEVLVDD SEHAGDSTHS HRWTSLELVK
1810 1820 1830 1840 1850
GTYTTDDSPS DIAEIRLDKV VPLKENVKYA VRLRNYGSRT ANGDGGMTTV
1860 1870 1880 1890 1900
QCPDGVTFTF STCSLSSNGT NQTRGQIPQI LYYRSEFDGD LQSQLLSKAN
1910 1920 1930 1940 1950
EEDKNCSRAL SVVSTVVRAS KDLLHRALAV DADDIPELLS SSSLFSMLLP
1960 1970 1980 1990 2000
LIIAYIGPVA AAIPKVAVEV FGLVQQLLPS VAILNQKYAP PAFNPNQSTD
2010 2020 2030 2040 2050
STTGNQPEQG LSACTTSSHY AVIESEHPYK PACVMHYKVT FPECVRWMTI
2060 2070 2080 2090 2100
EFDPQCGTAQ SEDVLRLLIP VRTVQNSGYG PKLTSVHENL NSWIELKKFS
2110 2120 2130 2140 2150
GSSGWPTMVL VLPGNEALFS LETASDYVKD DKASFYGFKC FAIGYEFSPG
2160 2170 2180 2190 2200
PDEGVIQLEK ELANLGGVCA AALMKKDLAL PIGNELEEDL EILEEAALQV
2210 2220 2230 2240 2250
CKTHSGILGK GLALSHSPTI LEALEGNLPL QIQSNEQSFL DDFIACVPGS
2260 2270 2280 2290 2300
SGGRLARWLQ PDSYADPQKT SLILNKDDIR CGWPTTITVQ TKDQYGDVVH
2310 2320 2330 2340 2350
VPNMKVEVKA VPVSQKKMSL QQDQAKKPQR IPGSPAVTAA SSNTDMTYGG
2360 2370 2380 2390 2400
LASPKLDVSY EPMIVKEARY IAITMMKVYE NYSFEELRFA SPTPKRPSEN
2410 2420 2430 2440 2450
MLIRVNNDGT YCANWTPGAI GLYTLHVTID GIEIDAGLEV KVKDPPKGMI
2460 2470 2480 2490 2500
PPGTQLVKPK SEPQPNKVRK FVAKDSAGLR IRSHPSLQSE QIGIVKVNGT
2510 2520 2530 2540 2550
ITFIDEIHND DGVWLRLNDE TIKKYVPNMN GYTEAWCLSF NQHLGKSLLV
2560 2570 2580 2590 2600
PVDESKTNTD DFFKDINSCC PQEATMQEQD MPFLRGGPGM YKVVKTGPSG
2610 2620 2630 2640 2650
HNIRSCPNLR GIPIGMLVLG NKVKAVGEVT NSEGTWVQLD QNSMVEFCES
2660 2670 2680 2690 2700
DEGEAWSLAR DRGGNQYLRH EDEQALLDQN SQTPPPSPFS VQAFNKGASC
2710 2720 2730 2740 2750
SAQGFDYGLG NSKGDRGNIS TSSKPASTSG KSELSSKHSR SLKPDGRMSR
2760 2770 2780 2790 2800
TTADQKKPRG TESLSASESL ILKSDAAKLR SDSHSRSLSP NHNTLQTLKS
2810 2820 2830 2840 2850
DGRMPSSSRA ESPGPGSRLS SPKPKTLPAN RSSPSGASSP RSSSPHDKNL
2860 2870 2880 2890 2900
PQKSTAPVKT KLDPPRERSK SDSYTLDPDT LRKKKMPLTE PLRGRSTSPK
2910 2920 2930 2940 2950
PKSVPKDSTD SPGSENRAPS PHVVQENLHS EVVEVCTSST LKTNSLTDST
2960 2970 2980 2990 3000
CDDSSEFKSV DEGSNKVHFS IGKAPLKDEQ EMRASPKISR KCANRHTRPK
3010 3020 3030 3040 3050
KEKSSFLFKG DGSKPLEPAK QAMSPSVAEC ARAVFASFLW HEGIVHDAMA
3060 3070 3080 3090 3100
CSSFLKFHPE LSKEHAPIRS SLNSQQPTEE KETKLKNRHS LEISSALNMF
3110 3120 3130 3140 3150
NIAPHGPDIS KMGSINKNKV LSMLKEPPLH EKCEDGKTET TFEMSMHNTM
3160 3170 3180 3190 3200
KSKSPLPLTL QHLVAFWEDI SLATIKAASQ NMIFPSPGSC AVLKKKECEK
3210 3220 3230 3240 3250
ENKKSKKEKK KKEKAEVRPR GNLFGEMAQL AVGGPEKDTI CELCGESHPY
3260 3270 3280 3290 3300
PVTYHMRQAH PGCGRYAGGQ GYNSIGHFCG GWAGNCGDGG IGGSTWYLVC
3310 3320 3330 3340 3350
DRCREKYLRE KQAAAREKVK QSRRKPMQVK TPRALPTMEA HQVIKANALF
3360 3370 3380 3390 3400
LLSLSSAAEP SILCYHPAKP FQSQLPSVKE GISEDLPVKM PCLYLQTLAR
3410 3420 3430 3440 3450
HHHENFVGYQ DDNLFQDEMR YLRSTSVPAP YISVTPDASP NVFEEPESNM
3460 3470 3480 3490 3500
KSMPPSLETS PITDTDLAKR TVFQRSYSVV ASEYDKQHSI LPARVKAIPR
3510 3520 3530 3540 3550
RRVNSGDTEV GSSLLRHPSP ELSRLISAHS SLSKGERNFQ WPVLAFVIQH
3560 3570 3580 3590 3600
HDLEGLEIAM KQALRKSACR VFAMEAFNWL LCNVIQTTSL HDILWHFVAS
3610 3620 3630 3640 3650
LTPAPVEPEE EEDEENKTSK ENSEQEKDTR VCEHPLSDIV IAGEAAHPLP
3660 3670 3680 3690 3700
HTFHRLLQTI SDLMMSLPSG SSLQQMALRC WSLKFKQSDH QFLHQSNVFH
3710 3720 3730 3740 3750
HINNILSKSD DGDSEESFSI SIQSGFEAMS QELCIVMCLK DLTSIVDIKT
3760 3770 3780 3790 3800
SSRPAMIGSL TDGSTETFWE SGDEDKNKTK NITINCVKGI NARYVSVHVD
3810 3820 3830 3840 3850
NSRDLGNKVT SMTFLTGKAV EDLCRIKQVD LDSRHIGWVT SELPGGDNHI
3860 3870 3880 3890 3900
IKIELKGPEN TLRVRQVKVL GWKDGESTKI AGQISASVAQ QRNCEAETLR
3910 3920 3930 3940 3950
VFRLITSQVF GKLISGDAEP TPEQEEKALL SSPEGEEKVY NATSDADLKE
3960 3970 3980 3990 4000
HMVGIIFSRS KLTNLQKQVC AHIVQAIRME ATRVREEWEH AISSKENANS
4010 4020 4030 4040 4050
QPNDEDASSD AYCFELLSMV LALSGSNVGR QYLAQQLTLL QDLFSLLHTA
4060 4070 4080 4090 4100
SPRVQRQVTS LLRRVLPEVT PSRLASIIGV KSLPPADISD IIHSTEKGDW
4110 4120 4130 4140 4150
NKLGILDMFL GCIAKALTVQ LKAKGTTITG TAGTTVGKGV TTVTLPMIFN
4160 4170 4180 4190 4200
SSYLRRGESH WWMKGSTPTQ ISEIIIKLIK DMAAGHLSEA WSRVTKNAIA
4210 4220 4230 4240 4250
ETIIALTKME EEFRSPVRCI ATTRLWLALA SLCVLDQDHV DRLSSGRWMG
4260 4270 4280 4290 4300
KDGQQKQMPM CDNHDDGETA AIILCNVCGN LCTDCDRFLH LHRRTKTHQR
4310 4320 4330 4340 4350
QVFKEEEEAI KVDLHEGCGR TKLFWLMALA DSKTMKAMVE FREHTGKPTT
4360 4370 4380 4390 4400
SSSEACRFCG SRSGTELSAV GSVCSDADCQ EYAKIACSKT HPCGHPCGGV
4410 4420 4430 4440 4450
KNEEHCLPCL HGCDKSATSL KQDADDMCMI CFTEALSAAP AIQLDCSHIF
4460 4470 4480 4490 4500
HLQCCRRVLE NRWLGPRITF GFISCPICKN KINHIVLKDL LDPIKELYED
4510 4520 4530 4540 4550
VRRKALMRLE YEGLHKSEAI TTPGVRFYND PAGYAMNRYA YYVCYKCRKA
4560 4570 4580 4590 4600
YFGGEARCDA EAGRGDDYDP RELICGACSD VSRAQMCPKH GTDFLEYKCR
4610 4620 4630 4640 4650
YCCSVAVFFC FGTTHFCNAC HDDFQRMTSI PKEELPHCPA GPKGKQLEGT
4660 4670
ECPLHVVHPP TGEEFALGCG VCRNAHTF
Length:4,678
Mass (Da):513,636
Last modified:June 20, 2018 - v4
Checksum:iF76B95A12613E74B
GO
Isoform 2Curated (identifier: O75592-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3939-3941: Missing.

Note: Derived from EST data.Curated
Show »
Length:4,675
Mass (Da):513,260
Checksum:iC2B0203596870213
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C3U4H7C3U4_HUMAN
E3 ubiquitin-protein ligase MYCBP2
MYCBP2
1,061Annotation score:
A0A0C4DGY7A0A0C4DGY7_HUMAN
E3 ubiquitin-protein ligase MYCBP2
MYCBP2
275Annotation score:
A0A087WY34A0A087WY34_HUMAN
E3 ubiquitin-protein ligase MYCBP2
MYCBP2
83Annotation score:

Sequence cautioni

The sequence AAD39842 differs from that shown. Reason: Frameshift at position 4674.Curated
The sequence AAH37971 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAI39758 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61R → P in AAC39928 (PubMed:9689053).Curated1
Sequence conflicti240G → V in AAC39928 (PubMed:9689053).Curated1
Sequence conflicti510G → R in AAC39928 (PubMed:9689053).Curated1
Sequence conflicti618T → I in AAC39928 (PubMed:9689053).Curated1
Sequence conflicti903 – 904QL → HV in AAC39928 (PubMed:9689053).Curated2
Sequence conflicti1512 – 1513GV → PL in AAC39928 (PubMed:9689053).Curated2
Sequence conflicti2139K → M in AAC39928 (PubMed:9689053).Curated1
Sequence conflicti3201E → GR in AAC39928 (PubMed:9689053).Curated1
Sequence conflicti3645A → R in AAC39928 (PubMed:9689053).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0520861919A → S. Corresponds to variant dbSNP:rs35887505Ensembl.1
Natural variantiVAR_0300702626V → M. Corresponds to variant dbSNP:rs9574002Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0141833939 – 3941Missing in isoform 2. Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF075587 mRNA Translation: AAC39928.1
AL159154
, AL159158, AL359257, AC001226 Genomic DNA Translation: CAH73736.1
AL159158
, AL159154, AL359257, AC001226 Genomic DNA Translation: CAI16842.1
AL359257
, AL159158, AL159154, AC001226 Genomic DNA Translation: CAI39759.1
AL359257, AC001226 Genomic DNA Translation: CAI39758.1 Sequence problems.
CH471093 Genomic DNA Translation: EAW80565.1
AB020723 mRNA Translation: BAA74939.1
BC037971 mRNA Translation: AAH37971.1 Different initiation.
AF083244 mRNA Translation: AAD39842.1 Frameshift.
RefSeqiNP_055872.4, NM_015057.4 [O75592-1]
UniGeneiHs.591221

Genome annotation databases

EnsembliENST00000357337; ENSP00000349892; ENSG00000005810
ENST00000544440; ENSP00000444596; ENSG00000005810
GeneIDi23077
KEGGihsa:23077
UCSCiuc058xok.1 human [O75592-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF075587 mRNA Translation: AAC39928.1
AL159154
, AL159158, AL359257, AC001226 Genomic DNA Translation: CAH73736.1
AL159158
, AL159154, AL359257, AC001226 Genomic DNA Translation: CAI16842.1
AL359257
, AL159158, AL159154, AC001226 Genomic DNA Translation: CAI39759.1
AL359257, AC001226 Genomic DNA Translation: CAI39758.1 Sequence problems.
CH471093 Genomic DNA Translation: EAW80565.1
AB020723 mRNA Translation: BAA74939.1
BC037971 mRNA Translation: AAH37971.1 Different initiation.
AF083244 mRNA Translation: AAD39842.1 Frameshift.
RefSeqiNP_055872.4, NM_015057.4 [O75592-1]
UniGeneiHs.591221

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5O6CX-ray1.75A4416-4678[»]
ProteinModelPortaliO75592
SMRiO75592
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116709, 86 interactors
DIPiDIP-28142N
IntActiO75592, 51 interactors
MINTiO75592
STRINGi9606.ENSP00000384288

PTM databases

iPTMnetiO75592
PhosphoSitePlusiO75592

Polymorphism and mutation databases

BioMutaiMYCBP2

Proteomic databases

EPDiO75592
MaxQBiO75592
PaxDbiO75592
PeptideAtlasiO75592
PRIDEiO75592
ProteomicsDBi50101
50102 [O75592-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357337; ENSP00000349892; ENSG00000005810
ENST00000544440; ENSP00000444596; ENSG00000005810
GeneIDi23077
KEGGihsa:23077
UCSCiuc058xok.1 human [O75592-1]

Organism-specific databases

CTDi23077
DisGeNETi23077
EuPathDBiHostDB:ENSG00000005810.17
GeneCardsiMYCBP2
HGNCiHGNC:23386 MYCBP2
HPAiHPA058807
MIMi610392 gene
neXtProtiNX_O75592
PharmGKBiPA134871126
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1428 Eukaryota
ENOG410XP1T LUCA
HOVERGENiHBG053153
InParanoidiO75592
KOiK10693
OMAiTVSVECF
OrthoDBiEOG091G0018
PhylomeDBiO75592
TreeFamiTF313151

Enzyme and pathway databases

UniPathwayi
UPA00143

Miscellaneous databases

ChiTaRSiMYCBP2 human
GeneWikiiMYCBP2
GenomeRNAii23077
PROiPR:O75592
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000005810 Expressed in 244 organ(s), highest expression level in primary visual cortex
CleanExiHS_MYCBP2
HS_PAM
ExpressionAtlasiO75592 baseline and differential
GenevisibleiO75592 HS

Family and domain databases

Gene3Di2.130.10.30, 2 hits
2.60.120.260, 1 hit
2.60.120.820, 2 hits
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR004939 APC_su10/DOC_dom
IPR017868 Filamin/ABP280_repeat-like
IPR008979 Galactose-bd-like_sf
IPR014756 Ig_E-set
IPR012983 PHR
IPR038648 PHR_sf
IPR009091 RCC1/BLIP-II
IPR000408 Reg_chr_condens
IPR003646 SH3-like_bac-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF03256 ANAPC10, 1 hit
PF08005 PHR, 2 hits
PF00415 RCC1, 1 hit
PF08239 SH3_3, 1 hit
PF13639 zf-RING_2, 1 hit
PRINTSiPR00633 RCCNDNSATION
SMARTiView protein in SMART
SM01337 APC10, 1 hit
SM00184 RING, 1 hit
SUPFAMiSSF49785 SSF49785, 1 hit
SSF50985 SSF50985, 2 hits
SSF81296 SSF81296, 2 hits
PROSITEiView protein in PROSITE
PS51284 DOC, 1 hit
PS50194 FILAMIN_REPEAT, 1 hit
PS00626 RCC1_2, 2 hits
PS50012 RCC1_3, 3 hits
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMYCB2_HUMAN
AccessioniPrimary (citable) accession number: O75592
Secondary accession number(s): A6NJC6
, Q5JSX8, Q5VZN6, Q6PIB6, Q9UQ11, Q9Y6E4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 20, 2018
Last modified: October 10, 2018
This is version 176 of the entry and version 4 of the sequence. See 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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