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Protein

E3 ubiquitin-protein ligase MIB1

Gene

Mib1

Organism
Mus musculus (Mouse)
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. Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation (By similarity). Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis.By similarity1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri79 – 12648ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri819 – 85436RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri866 – 90136RING-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 99634RING-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin-protein transferase activity Source: GO_Central
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. blood vessel development Source: MGI
  2. heart development Source: MGI
  3. heart looping Source: MGI
  4. in utero embryonic development Source: MGI
  5. negative regulation of neuron differentiation Source: MGI
  6. neural tube formation Source: MGI
  7. Notch signaling pathway Source: MGI
  8. positive regulation of endocytosis Source: MGI
  9. protein ubiquitination Source: GO_Central
  10. somitogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Notch signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MIB1 (EC:6.3.2.-)
Alternative name(s):
DAPK-interacting protein 1
Short name:
DIP-1
Mind bomb homolog 1
Gene namesi
Name:Mib1
Synonyms:Dip1, Kiaa1323, Mib
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:2443157. Mib1.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity. Cytoplasm. Cell membrane
Note: Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (By similarity). Localizes to the plasma membrane.By similarity

GO - Cellular componenti

  1. centrosome Source: MGI
  2. cytoplasmic vesicle Source: MGI
  3. plasma membrane Source: UniProtKB-SubCell
  4. postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10061006E3 ubiquitin-protein ligase MIB1PRO_0000055944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei408 – 4081PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated; this modification is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (By similarity). Ubiquitinated; possibly via autoubiquitination.By similarity2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ80SY4.
PaxDbiQ80SY4.
PRIDEiQ80SY4.

PTM databases

PhosphoSiteiQ80SY4.

Expressioni

Tissue specificityi

Detected in all tissues tested. Present in embryo, embryonic stem cells, bladder, skeletal muscle, bladder, uterus, testis, stomach, colon, ileum, trachea, lung, aorta, kidney, spleen, liver and vas deferens (at protein level). Highly expressed in testis.2 Publications

Developmental stagei

Highly expressed both in embryos and adult tissues. In E9.5 and E10.5 embryos, it is expressed in the tail bud, limb buds and somites. Expressed in the same pattern than MIB2 in the skin and intestine at postnatal day 1 (P1) and in the hair follicle in the skin in the adult.1 Publication

Gene expression databases

BgeeiQ80SY4.
CleanExiMM_MIB1.
ExpressionAtlasiQ80SY4. baseline and differential.
GenevestigatoriQ80SY4.

Interactioni

Subunit structurei

Interacts with CEP131 and PCM1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CMIPQ8IY222EBI-645227,EBI-7689652From a different organism.
snx5Q6DI324EBI-645227,EBI-8574974From a different organism.

Protein-protein interaction databases

BioGridi230365. 17 interactions.
IntActiQ80SY4. 5 interactions.
MINTiMINT-1550820.

Structurei

3D structure databases

ProteinModelPortaliQ80SY4.
SMRiQ80SY4. Positions 15-70, 154-216, 382-779, 851-908, 953-1003.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 7469MIB/HERC2 1PROSITE-ProRule annotationAdd
BLAST
Domaini143 – 22179MIB/HERC2 2PROSITE-ProRule annotationAdd
BLAST
Repeati430 – 46031ANK 1Add
BLAST
Repeati463 – 49230ANK 2Add
BLAST
Repeati496 – 52530ANK 3Add
BLAST
Repeati529 – 55830ANK 4Add
BLAST
Repeati562 – 59130ANK 5Add
BLAST
Repeati595 – 62733ANK 6Add
BLAST
Repeati631 – 66131ANK 7Add
BLAST
Repeati665 – 69430ANK 8Add
BLAST
Repeati698 – 72932ANK 9Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili935 – 96228Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 9 ANK repeats.PROSITE-ProRule annotation
Contains 2 MIB/HERC2 domains.PROSITE-ProRule annotation
Contains 3 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 fingeri79 – 12648ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri819 – 85436RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri866 – 90136RING-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 99634RING-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00780000121974.
HOVERGENiHBG068386.
InParanoidiQ80SY4.
KOiK10645.
OMAiHDAISKE.
OrthoDBiEOG7WHH8P.
PhylomeDBiQ80SY4.
TreeFamiTF324147.

Family and domain databases

Gene3Di1.25.40.20. 3 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]
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 3 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80SY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV
60 70 80 90 100
VWDNGTAANY RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC
110 120 130 140 150
AECTNYDLCT VCYHGDKHHL RHRFYRITTP GSERVLLESR RKSKKITARG
160 170 180 190 200
IFAGARVVRG VDWQWEDQDG GNGRRGKVTE IQDWSASSPH SAAYVLWDNG
210 220 230 240 250
AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN RNPGGLQIGD
260 270 280 290 300
LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
310 320 330 340 350
GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL
360 370 380 390 400
LQRGHGEWAE AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV
410 420 430 440 450
APAGSAISNA SGERLSQLLK KLFETQESGD LNEELVKAAA NGDVAKVEDL
460 470 480 490 500
LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL KLLLKQNVDV EAEDKDGDRA
510 520 530 540 550
VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK GHLQVVKTLL
560 570 580 590 600
DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
610 620 630 640 650
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL
660 670 680 690 700
LVHQGNANLD IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD
710 720 730 740 750
TPLHEALRHH TLSQLRQLQD MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK
760 770 780 790 800
SAASIACFLA ANGADLSIRN KKGQSPLDLC PDPSLCKALA KCHKEKVSGQ
810 820 830 840 850
VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC SLCSPRVKKC
860 870 880 890 900
LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ASLMKKCVQC
910 920 930 940 950
RAVVERRVPF ITCCGGKSSE DPSDEISSGN IPVLQKDKDN TNVNADVQKL
960 970 980 990 1000
QQQLQDIKEQ TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE

RRILLY
Length:1,006
Mass (Da):110,088
Last modified:June 1, 2003 - v1
Checksum:i5A8FE2A1BEE638DE
GO

Sequence cautioni

The sequence AAH11287.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH69870.1 differs from that shown.Chimeric cDNA.Curated
The sequence AAN18022.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC38042.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti742 – 7421L → F in BAC38042 (PubMed:16141072).Curated
Sequence conflicti907 – 9071R → K in AAN18022 (PubMed:15824097).Curated
Sequence conflicti907 – 9071R → K in AAX84653 (PubMed:15824097).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245539 mRNA. Translation: AAO91933.1.
AY149907 mRNA. Translation: AAN75492.1.
AY147848 mRNA. Translation: AAN18022.1. Different initiation.
AY974091 mRNA. Translation: AAX84653.1.
AK053035 mRNA. Translation: BAC35245.1.
AK080847 mRNA. Translation: BAC38042.1. Sequence problems.
BC011287 mRNA. Translation: AAH11287.1. Different initiation.
BC069870 mRNA. Translation: AAH69870.1. Sequence problems.
BC083072 mRNA. Translation: AAH83072.1.
AK129331 mRNA. Translation: BAC98141.1.
CCDSiCCDS29058.1.
RefSeqiNP_659109.2. NM_144860.2.
XP_006525873.1. XM_006525810.1.
XP_006525874.1. XM_006525811.1.
UniGeneiMm.21500.

Genome annotation databases

EnsembliENSMUST00000052838; ENSMUSP00000054428; ENSMUSG00000024294.
ENSMUST00000165555; ENSMUSP00000131712; ENSMUSG00000024294.
GeneIDi225164.
KEGGimmu:225164.
UCSCiuc008ebc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245539 mRNA. Translation: AAO91933.1.
AY149907 mRNA. Translation: AAN75492.1.
AY147848 mRNA. Translation: AAN18022.1. Different initiation.
AY974091 mRNA. Translation: AAX84653.1.
AK053035 mRNA. Translation: BAC35245.1.
AK080847 mRNA. Translation: BAC38042.1. Sequence problems.
BC011287 mRNA. Translation: AAH11287.1. Different initiation.
BC069870 mRNA. Translation: AAH69870.1. Sequence problems.
BC083072 mRNA. Translation: AAH83072.1.
AK129331 mRNA. Translation: BAC98141.1.
CCDSiCCDS29058.1.
RefSeqiNP_659109.2. NM_144860.2.
XP_006525873.1. XM_006525810.1.
XP_006525874.1. XM_006525811.1.
UniGeneiMm.21500.

3D structure databases

ProteinModelPortaliQ80SY4.
SMRiQ80SY4. Positions 15-70, 154-216, 382-779, 851-908, 953-1003.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230365. 17 interactions.
IntActiQ80SY4. 5 interactions.
MINTiMINT-1550820.

PTM databases

PhosphoSiteiQ80SY4.

Proteomic databases

MaxQBiQ80SY4.
PaxDbiQ80SY4.
PRIDEiQ80SY4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052838; ENSMUSP00000054428; ENSMUSG00000024294.
ENSMUST00000165555; ENSMUSP00000131712; ENSMUSG00000024294.
GeneIDi225164.
KEGGimmu:225164.
UCSCiuc008ebc.1. mouse.

Organism-specific databases

CTDi57534.
MGIiMGI:2443157. Mib1.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00780000121974.
HOVERGENiHBG068386.
InParanoidiQ80SY4.
KOiK10645.
OMAiHDAISKE.
OrthoDBiEOG7WHH8P.
PhylomeDBiQ80SY4.
TreeFamiTF324147.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.

Miscellaneous databases

ChiTaRSiMib1. mouse.
NextBioi377558.
PROiQ80SY4.
SOURCEiSearch...

Gene expression databases

BgeeiQ80SY4.
CleanExiMM_MIB1.
ExpressionAtlasiQ80SY4. baseline and differential.
GenevestigatoriQ80SY4.

Family and domain databases

Gene3Di1.25.40.20. 3 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]
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 3 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of DAPK."
    Jin Y., Blue E.K., Dixon S., Shao Z., Gallagher P.J.
    J. Biol. Chem. 277:46980-46986(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, UBIQUITINATION.
    Tissue: Urinary bladder.
  2. "Mind bomb is a ubiquitin ligase that is essential for efficient activation of Notch signaling by Delta."
    Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D., Yeo S.-Y., Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M., Lewis J., Chandrasekharappa S.C., Chitnis A.B.
    Dev. Cell 4:67-82(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, UBIQUITINATION.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1006.
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Head.
  5. "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] OF 547-1006.
    Strain: 129 and FVB/N.
    Tissue: Embryo and Mammary tumor.
  6. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 864-1006.
    Tissue: Embryonic tail.

Entry informationi

Entry nameiMIB1_MOUSE
AccessioniPrimary (citable) accession number: Q80SY4
Secondary accession number(s): Q5XK51
, Q6IS57, Q6YI52, Q6ZPT8, Q8BNR1, Q8C6W2, Q921Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: March 4, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.