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Protein

E3 ubiquitin-protein ligase MIB2

Gene

MIB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors (By similarity).By similarity

Pathwayi: protein ubiquitination

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri143 – 19048ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri890 – 92536RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri969 – 100234RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • Notch signaling pathway Source: UniProtKB-KW
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • protein polyubiquitination Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Notch signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96AX9.
SIGNORiQ96AX9.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MIB2 (EC:6.3.2.-)
Alternative name(s):
Mind bomb homolog 2
Novel zinc finger protein
Short name:
Novelzin
Putative NF-kappa-B-activating protein 002N
Skeletrophin
Zinc finger ZZ type with ankyrin repeat domain protein 1
Gene namesi
Name:MIB2
Synonyms:SKD, ZZANK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30577. MIB2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134924284.

Polymorphism and mutation databases

BioMutaiMIB2.
DMDMi209572707.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10131013E3 ubiquitin-protein ligase MIB2PRO_0000055947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091PhosphoserineCombined sources
Isoform 10 (identifier: Q96AX9-10)
Modified residuei1 – 11N-acetylmethionineCombined sources
Isoform 8 (identifier: Q96AX9-8)
Modified residuei1 – 11N-acetylmethionineCombined sources

Post-translational modificationi

Ubiquitinated. Possibly via autoubiquitination (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96AX9.
MaxQBiQ96AX9.
PaxDbiQ96AX9.
PRIDEiQ96AX9.

PTM databases

iPTMnetiQ96AX9.
PhosphoSiteiQ96AX9.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, and to a lesser extent in heart, brain and kidney.1 Publication

Inductioni

Down-regulated in many primary skin melanomas. Treatment with a demethylating agent, 5'-aza-2-deoxycytidine, restores expression, suggesting that down-regulation is the result of methylation of the gene.1 Publication

Gene expression databases

BgeeiQ96AX9.
ExpressionAtlasiQ96AX9. baseline and differential.
GenevisibleiQ96AX9. HS.

Organism-specific databases

HPAiHPA027871.

Interactioni

Subunit structurei

Interacts with actin monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TBK1Q9UHD22EBI-2130249,EBI-356402

Protein-protein interaction databases

BioGridi126769. 22 interactions.
IntActiQ96AX9. 10 interactions.
MINTiMINT-3050933.
STRINGi9606.ENSP00000426103.

Structurei

3D structure databases

ProteinModelPortaliQ96AX9.
SMRiQ96AX9. Positions 70-134, 212-280, 456-886, 961-1013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 13880MIB/HERC2 1PROSITE-ProRule annotationAdd
BLAST
Domaini207 – 28579MIB/HERC2 2PROSITE-ProRule annotationAdd
BLAST
Repeati522 – 55130ANK 1Add
BLAST
Repeati555 – 58430ANK 2Add
BLAST
Repeati588 – 61730ANK 3Add
BLAST
Repeati621 – 65333ANK 4Add
BLAST
Repeati657 – 68630ANK 5Add
BLAST
Repeati691 – 72131ANK 6Add
BLAST
Repeati725 – 75430ANK 7Add
BLAST
Repeati758 – 78629ANK 8Add
BLAST
Repeati827 – 85630ANK 9Add
BLAST

Sequence similaritiesi

Contains 9 ANK repeats.PROSITE-ProRule annotation
Contains 2 MIB/HERC2 domains.PROSITE-ProRule annotation
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri143 – 19048ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri890 – 92536RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri969 – 100234RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4582. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00790000122981.
HOGENOMiHOG000231158.
HOVERGENiHBG068386.
InParanoidiQ96AX9.
KOiK10645.
OMAiYETAHSQ.
OrthoDBiEOG7WHH8P.
PhylomeDBiQ96AX9.
TreeFamiTF324147.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequences (14)i

Sequence statusi: Complete.

This entry describes 14 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96AX9-1) [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

        10         20         30         40         50
MGWKPSEARG QSQSFQASGL QPRSLKAARR ATGRPDRSRA ARPTMDPSAH
60 70 80 90 100
RSRAAPPNMD PDPQAGVQVG MRVVRGVDWK WGQQDGGEGG VGTVVELGRH
110 120 130 140 150
GSPSTPDRTV VVQWDQGTRT NYRAGYQGAH DLLLYDNAQI GVRHPNIICD
160 170 180 190 200
CCKKHGLRGM RWKCRVCLDY DLCTQCYMHN KHELAHAFDR YETAHSRPVT
210 220 230 240 250
LSPRQGLPRI PLRGIFQGAK VVRGPDWEWG SQDGGEGKPG RVVDIRGWDV
260 270 280 290 300
ETGRSVASVT WADGTTNVYR VGHKGKVDLK CVGEAAGGFY YKDHLPRLGK
310 320 330 340 350
PAELQRRVSA DSQPFQHGDK VKCLLDTDVL REMQEGHGGW NPRMAEFIGQ
360 370 380 390 400
TGTVHRITDR GDVRVQFNHE TRWTFHPGAL TKHHSFWVGD VVRVIGDLDT
410 420 430 440 450
VKRLQAGHGE WTDDMAPALG RVGKVVKVFG DGNLRVAVAG QRWTFSPSCL
460 470 480 490 500
VAYRPEEDAN LDVAERAREN KSSLSVALDK LRAQKSDPEH PGRLVVEVAL
510 520 530 540 550
GNAARALDLL RRRPEQVDTK NQGRTALQVA AYLGQVELIR LLLQARAGVD
560 570 580 590 600
LPDDEGNTAL HYAALGNQPE ATRVLLSAGC RADAINSTQS TALHVAVQRG
610 620 630 640 650
FLEVVRALCE RGCDVNLPDA HSDTPLHSAI SAGTGASGIV EVLTEVPNID
660 670 680 690 700
VTATNSQGFT LLHHASLKGH ALAVRKILAR ARQLVDAKKE DGFTALHLAA
710 720 730 740 750
LNNHREVAQI LIREGRCDVN VRNRKLQSPL HLAVQQAHVG LVPLLVDAGC
760 770 780 790 800
SVNAEDEEGD TALHVALQRH QLLPLVADGA GGDPGPLQLL SRLQASGLPG
810 820 830 840 850
SAELTVGAAV ACFLALEGAD VSYTNHRGRS PLDLAAEGRV LKALQGCAQR
860 870 880 890 900
FRERQAGGGA APGPRQTLGT PNTVTNLHVG AAPGPEAAEC LVCSELALLV
910 920 930 940 950
LFSPCQHRTV CEECARRMKK CIRCQVVVSK KLRPDGSEVA SAAPAPGPPR
960 970 980 990 1000
QLVEELQSRY RQMEERITCP ICIDSHIRLV FQCGHGACAP CGSALSACPI
1010
CRQPIRDRIQ IFV
Length:1,013
Mass (Da):109,939
Last modified:October 14, 2008 - v3
Checksum:i737BA12300091C70
GO
Isoform 2 (identifier: Q96AX9-2) [UniParc]FASTAAdd to basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     37-50: Missing.

Show »
Length:999
Mass (Da):108,404
Checksum:i37BC32E3C342FC75
GO
Isoform 3 (identifier: Q96AX9-3) [UniParc]FASTAAdd to basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     347-350: Missing.

Show »
Length:1,009
Mass (Da):109,493
Checksum:i6A16B37089CF3538
GO
Isoform 4 (identifier: Q96AX9-4) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     234-298: Missing.

Show »
Length:948
Mass (Da):102,967
Checksum:iDDC32F6A7743A6E3
GO
Isoform 5 (identifier: Q96AX9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     383-417: Missing.

Note: No experimental confirmation available.
Show »
Length:978
Mass (Da):106,011
Checksum:i211C2E732319290D
GO
Isoform 10 (identifier: Q96AX9-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     234-298: Missing.
     853-1013: ERQAGGGAAP...PIRDRIQIFV → VRAQDEEVHQVPGGRQQETAPRRL

Note: No experimental confirmation available.Combined sources
Show »
Length:753
Mass (Da):82,129
Checksum:i9447C993AF8726DC
GO
Isoform 7 (identifier: Q96AX9-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.

Show »
Length:854
Mass (Da):92,680
Checksum:iC8390208E6E8CFDF
GO
Isoform 8 (identifier: Q96AX9-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     858-860: GGA → RGR
     861-1013: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:802
Mass (Da):87,273
Checksum:i9142D07056C27DBE
GO
Isoform 9 (identifier: Q96AX9-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     673-1013: Missing.

Show »
Length:672
Mass (Da):73,542
Checksum:i1257E008401D9FF9
GO
Isoform 6 (identifier: Q96AX9-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     347-382: Missing.

Note: No experimental confirmation available.
Show »
Length:977
Mass (Da):105,777
Checksum:i80A370887F8655CE
GO
Isoform 11 (identifier: Q96AX9-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAGALRRGRALGSRPSGPTVSSRRSPQCPVAQEGLGARSRPRVAPRSLARCGPSSRLM
     42-55: Missing.

Note: No experimental confirmation available.
Show »
Length:1,056
Mass (Da):114,326
Checksum:iCF351D9EC0CF7592
GO
Isoform 12 (identifier: Q96AX9-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAGALRRGRALGSRPSGPTVSSRRSPQCPVAQEGLGARSRPRVAPRSLARCGPSSRLM
     234-298: Missing.

Note: No experimental confirmation available.
Show »
Length:1,005
Mass (Da):108,889
Checksum:i1DFA3D2E0A3ADDAE
GO
Isoform 13 (identifier: Q96AX9-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAGALRRGRALGSRPSGPTVSSRRSPQCPVAQEGLGARSRPRVAPRSLARCGPSSRLM
     347-350: Missing.

Note: No experimental confirmation available.
Show »
Length:1,066
Mass (Da):115,415
Checksum:i5A269C248614C73A
GO
Isoform 14 (identifier: Q96AX9-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAGALRRGRALGSRPSGPTVSSRRSPQCPVAQEGLGARSRPRVAPRSLARCGPSSRLM

Note: No experimental confirmation available.
Show »
Length:1,070
Mass (Da):115,861
Checksum:i7A4B6B4050393324
GO

Sequence cautioni

The sequence AAH16490.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB82979.1 differs from that shown. Reason: Frameshift at positions 193 and 205. Curated
The sequence BAC03707.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC04646.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC04752.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC04952.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801K → N in AAH16490 (PubMed:15489334).Curated
Sequence conflicti176 – 1772CY → SN in BAB82979 (Ref. 2) Curated
Sequence conflicti221 – 2211V → A in BAB82979 (Ref. 2) Curated
Sequence conflicti226 – 2261D → F in BAC77353 (PubMed:12761501).Curated
Sequence conflicti235 – 2351G → R in BAG63969 (PubMed:14702039).Curated
Sequence conflicti273 – 2731H → Y in AAH37542 (PubMed:15489334).Curated
Sequence conflicti375 – 3751F → L in BAC04646 (PubMed:14702039).Curated
Sequence conflicti508 – 5081D → G in AAH37542 (PubMed:15489334).Curated
Sequence conflicti637 – 6371S → G in AAH37542 (PubMed:15489334).Curated
Sequence conflicti689 – 6891K → E in BAC04752 (PubMed:14702039).Curated
Sequence conflicti692 – 6921G → D in BAG53705 (PubMed:14702039).Curated
Sequence conflicti937 – 9371S → F in BAC04646 (PubMed:14702039).Curated
Sequence conflicti975 – 9751S → R in BAC77353 (PubMed:12761501).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151F → L.2 Publications
Corresponds to variant rs7418389 [ dbSNP | Ensembl ].
VAR_046668
Natural varianti45 – 451M → T.3 Publications
Corresponds to variant rs12755088 [ dbSNP | Ensembl ].
VAR_046669

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 159159Missing in isoform 7. 1 PublicationVSP_035508Add
BLAST
Alternative sequencei1 – 5858Missing in isoform 8 and isoform 10. 1 PublicationVSP_035509Add
BLAST
Alternative sequencei1 – 11M → MAGALRRGRALGSRPSGPTV SSRRSPQCPVAQEGLGARSR PRVAPRSLARCGPSSRLM in isoform 11, isoform 12, isoform 13 and isoform 14. 1 PublicationVSP_046405
Alternative sequencei37 – 5014Missing in isoform 2. 3 PublicationsVSP_014392Add
BLAST
Alternative sequencei42 – 5514Missing in isoform 11. 1 PublicationVSP_046406Add
BLAST
Alternative sequencei234 – 29865Missing in isoform 4, isoform 10 and isoform 12. 2 PublicationsVSP_014393Add
BLAST
Alternative sequencei347 – 38236Missing in isoform 6. CuratedVSP_014394Add
BLAST
Alternative sequencei347 – 3504Missing in isoform 3 and isoform 13. 1 PublicationVSP_014395
Alternative sequencei383 – 41735Missing in isoform 5. 1 PublicationVSP_014396Add
BLAST
Alternative sequencei673 – 1013341Missing in isoform 9. 1 PublicationVSP_035510Add
BLAST
Alternative sequencei853 – 1013161ERQAG…IQIFV → VRAQDEEVHQVPGGRQQETA PRRL in isoform 10. 1 PublicationVSP_045186Add
BLAST
Alternative sequencei858 – 8603GGA → RGR in isoform 8. 1 PublicationVSP_035511
Alternative sequencei861 – 1013153Missing in isoform 8. 1 PublicationVSP_035512Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074480 mRNA. Translation: BAB92950.1.
AB064367 mRNA. Translation: BAB82979.1. Frameshift.
AB076691 mRNA. Translation: BAC00992.1.
AB076692 mRNA. Translation: BAC00993.1.
AB076693 mRNA. Translation: BAC00994.1.
AB097000 mRNA. Translation: BAC77353.1.
AK091610 mRNA. Translation: BAC03707.1. Different initiation.
AK095914 mRNA. Translation: BAC04646.1. Different initiation.
AK096295 mRNA. Translation: BAC04752.1. Different initiation.
AK097106 mRNA. Translation: BAC04952.1. Different initiation.
AK098785 mRNA. Translation: BAC05413.1.
AK122751 mRNA. Translation: BAG53705.1.
AK122863 mRNA. Translation: BAG53766.1.
AK128167 mRNA. Translation: BAG54643.1.
AK302757 mRNA. Translation: BAG63969.1.
AL691432 Genomic DNA. No translation available.
BC016490 mRNA. Translation: AAH16490.1. Different initiation.
BC037542 mRNA. Translation: AAH37542.1.
AL834527 mRNA. Translation: CAD39183.1.
CCDSiCCDS41224.2. [Q96AX9-14]
CCDS53261.1. [Q96AX9-13]
CCDS53262.1. [Q96AX9-12]
CCDS53263.1. [Q96AX9-11]
CCDS53264.1. [Q96AX9-10]
RefSeqiNP_001164157.1. NM_001170686.1. [Q96AX9-13]
NP_001164158.1. NM_001170687.1. [Q96AX9-11]
NP_001164159.1. NM_001170688.1. [Q96AX9-12]
NP_001164160.1. NM_001170689.1. [Q96AX9-10]
NP_543151.2. NM_080875.2. [Q96AX9-14]
UniGeneiHs.135805.
Hs.593430.

Genome annotation databases

EnsembliENST00000355826; ENSP00000348081; ENSG00000197530. [Q96AX9-11]
ENST00000378712; ENSP00000367984; ENSG00000197530. [Q96AX9-10]
ENST00000505820; ENSP00000426103; ENSG00000197530. [Q96AX9-14]
ENST00000518681; ENSP00000428264; ENSG00000197530. [Q96AX9-12]
ENST00000520777; ENSP00000428660; ENSG00000197530. [Q96AX9-13]
GeneIDi142678.
KEGGihsa:142678.
UCSCiuc001agg.4. human. [Q96AX9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074480 mRNA. Translation: BAB92950.1.
AB064367 mRNA. Translation: BAB82979.1. Frameshift.
AB076691 mRNA. Translation: BAC00992.1.
AB076692 mRNA. Translation: BAC00993.1.
AB076693 mRNA. Translation: BAC00994.1.
AB097000 mRNA. Translation: BAC77353.1.
AK091610 mRNA. Translation: BAC03707.1. Different initiation.
AK095914 mRNA. Translation: BAC04646.1. Different initiation.
AK096295 mRNA. Translation: BAC04752.1. Different initiation.
AK097106 mRNA. Translation: BAC04952.1. Different initiation.
AK098785 mRNA. Translation: BAC05413.1.
AK122751 mRNA. Translation: BAG53705.1.
AK122863 mRNA. Translation: BAG53766.1.
AK128167 mRNA. Translation: BAG54643.1.
AK302757 mRNA. Translation: BAG63969.1.
AL691432 Genomic DNA. No translation available.
BC016490 mRNA. Translation: AAH16490.1. Different initiation.
BC037542 mRNA. Translation: AAH37542.1.
AL834527 mRNA. Translation: CAD39183.1.
CCDSiCCDS41224.2. [Q96AX9-14]
CCDS53261.1. [Q96AX9-13]
CCDS53262.1. [Q96AX9-12]
CCDS53263.1. [Q96AX9-11]
CCDS53264.1. [Q96AX9-10]
RefSeqiNP_001164157.1. NM_001170686.1. [Q96AX9-13]
NP_001164158.1. NM_001170687.1. [Q96AX9-11]
NP_001164159.1. NM_001170688.1. [Q96AX9-12]
NP_001164160.1. NM_001170689.1. [Q96AX9-10]
NP_543151.2. NM_080875.2. [Q96AX9-14]
UniGeneiHs.135805.
Hs.593430.

3D structure databases

ProteinModelPortaliQ96AX9.
SMRiQ96AX9. Positions 70-134, 212-280, 456-886, 961-1013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126769. 22 interactions.
IntActiQ96AX9. 10 interactions.
MINTiMINT-3050933.
STRINGi9606.ENSP00000426103.

PTM databases

iPTMnetiQ96AX9.
PhosphoSiteiQ96AX9.

Polymorphism and mutation databases

BioMutaiMIB2.
DMDMi209572707.

Proteomic databases

EPDiQ96AX9.
MaxQBiQ96AX9.
PaxDbiQ96AX9.
PRIDEiQ96AX9.

Protocols and materials databases

DNASUi142678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355826; ENSP00000348081; ENSG00000197530. [Q96AX9-11]
ENST00000378712; ENSP00000367984; ENSG00000197530. [Q96AX9-10]
ENST00000505820; ENSP00000426103; ENSG00000197530. [Q96AX9-14]
ENST00000518681; ENSP00000428264; ENSG00000197530. [Q96AX9-12]
ENST00000520777; ENSP00000428660; ENSG00000197530. [Q96AX9-13]
GeneIDi142678.
KEGGihsa:142678.
UCSCiuc001agg.4. human. [Q96AX9-1]

Organism-specific databases

CTDi142678.
GeneCardsiMIB2.
HGNCiHGNC:30577. MIB2.
HPAiHPA027871.
MIMi611141. gene.
neXtProtiNX_Q96AX9.
PharmGKBiPA134924284.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4582. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00790000122981.
HOGENOMiHOG000231158.
HOVERGENiHBG068386.
InParanoidiQ96AX9.
KOiK10645.
OMAiYETAHSQ.
OrthoDBiEOG7WHH8P.
PhylomeDBiQ96AX9.
TreeFamiTF324147.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96AX9.
SIGNORiQ96AX9.

Miscellaneous databases

ChiTaRSiMIB2. human.
GeneWikiiMIB2_(gene).
GenomeRNAii142678.
PROiQ96AX9.
SOURCEiSearch...

Gene expression databases

BgeeiQ96AX9.
ExpressionAtlasiQ96AX9. baseline and differential.
GenevisibleiQ96AX9. HS.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma."
    Takeuchi T., Heng H.H.Q., Ye C.J., Liang S.-B., Iwata J., Sonobe H., Ohtsuki Y.
    Am. J. Pathol. 163:1395-1404(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH ACTIN, VARIANT THR-45.
  2. "A novel zinc finger protein."
    Takeuchi T.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), VARIANT THR-45.
  3. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LEU-15.
    Tissue: Lung fibroblast.
  4. "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] (ISOFORMS 7; 8; 9; 10 AND 11), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-1013 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-1013 (ISOFORMS 1/2/6/7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-1013 (ISOFORM 4), VARIANTS LEU-15 AND THR-45.
    Tissue: Brain, Heart, Spleen, Teratocarcinoma, Testis and Tongue.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain and Lymph.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-1013 (ISOFORMS 1/2).
    Tissue: Testis.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 10 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMIB2_HUMAN
AccessioniPrimary (citable) accession number: Q96AX9
Secondary accession number(s): A2AGM5
, A2AGM6, B3KV93, B3KVF4, B3KXY1, B4DZ57, E9PGU1, E9PHQ1, F8WA73, J3KNZ7, Q7Z437, Q8IY62, Q8N786, Q8N897, Q8N8R2, Q8N911, Q8NB36, Q8NCY1, Q8NG59, Q8NG60, Q8NG61, Q8NI59, Q8WYN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 14, 2008
Last modified: June 8, 2016
This is version 143 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.