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Q4U2R1

- HERC2_MOUSE

UniProt

Q4U2R1 - HERC2_MOUSE

Protein

E3 ubiquitin-protein ligase HERC2

Gene

Herc2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei4764 – 47641Glycyl thioester intermediatePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri2703 – 275048ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. ligase activity Source: UniProtKB-KW
    3. SUMO binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB
    3. protein ubiquitination Source: UniProtKB
    4. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
    5. spermatogenesis Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase HERC2 (EC:6.3.2.-)
    Alternative name(s):
    HECT domain and RCC1-like domain-containing protein 2
    Gene namesi
    Name:Herc2Imported
    Synonyms:Jdf2, Kiaa0393Imported, Rjs
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:103234. Herc2.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Nucleus By similarity
    Note: Recruited to sites of DNA damage in response to ionising radiation (IR) via its interaction with RNF8. May loose association with centrosomes during mitosis.By similarity

    GO - Cellular componenti

    1. centriole Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. mitochondrial inner membrane Source: MGI
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Herc2 are the cause of the runty, jerky, sterile phenotype (rjs), also known as the juvenile development and fertility phenotype (jfd2), which is characterized by reduced size, jerky gait, fertility problems including spermatocyte and oocyte abnormalities, defective maternal behavior and reduced lifespan with juvenile lethality.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 48364836E3 ubiquitin-protein ligase HERC2PRO_0000229740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei648 – 6481PhosphothreonineBy similarity
    Modified residuei1578 – 15781Phosphoserine1 Publication
    Modified residuei1945 – 19451PhosphothreonineBy similarity
    Modified residuei2455 – 24551PhosphoserineBy similarity
    Modified residuei2929 – 29291PhosphoserineBy similarity
    Modified residuei4812 – 48121PhosphoserineBy similarity
    Modified residuei4813 – 48131PhosphoserineBy similarity
    Modified residuei4816 – 48161PhosphoserineBy similarity
    Modified residuei4829 – 48291PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-4829 is required for interaction with RNF8.1 Publication
    Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs), promoting the interaction with RNF8.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ4U2R1.
    PaxDbiQ4U2R1.
    PRIDEiQ4U2R1.

    PTM databases

    PhosphoSiteiQ4U2R1.

    Expressioni

    Tissue specificityi

    Highest levels are found in brain and testis with lower levels in heart, lung, liver, skeletal muscle and kidney. Little expression detected in spleen.1 Publication

    Gene expression databases

    BgeeiQ4U2R1.
    GenevestigatoriQ4U2R1.

    Interactioni

    Subunit structurei

    Interacts (when phosphorylated at Thr-4829 and sumoylated) with RNF8 (via FHA domain); this interaction increases after ionising radiation (IR) treatment. Interacts with XPA By similarity. Interacts with NEURL4. Via its interaction with NEURL4, may indirectly interact with CCP110 and CEP97 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200274. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4U2R1.
    SMRiQ4U2R1. Positions 423-780, 1206-1297, 1868-1929, 3955-4320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati416 – 46247RCC1 1-1Add
    BLAST
    Repeati463 – 51351RCC1 1-2Add
    BLAST
    Repeati514 – 56956RCC1 1-3Add
    BLAST
    Repeati570 – 62152RCC1 1-4Add
    BLAST
    Repeati624 – 67552RCC1 1-5Add
    BLAST
    Repeati676 – 72752RCC1 1-6Add
    BLAST
    Repeati729 – 77951RCC1 1-7Add
    BLAST
    Domaini1208 – 128477Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1860 – 193374MIB/HERC2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2760 – 2937178DOCPROSITE-ProRule annotationAdd
    BLAST
    Repeati2959 – 301052RCC1 2-1Add
    BLAST
    Repeati3011 – 306555RCC1 2-2Add
    BLAST
    Repeati3066 – 311752RCC1 2-3Add
    BLAST
    Repeati3119 – 316951RCC1 2-4Add
    BLAST
    Repeati3172 – 322352RCC1 2-5Add
    BLAST
    Repeati3225 – 327551RCC1 2-6Add
    BLAST
    Repeati3276 – 332752RCC1 2-7Add
    BLAST
    Repeati3953 – 400452RCC1 3-1Add
    BLAST
    Repeati4006 – 405853RCC1 3-2Add
    BLAST
    Repeati4060 – 411051RCC1 3-3Add
    BLAST
    Repeati4112 – 416453RCC1 3-4Add
    BLAST
    Repeati4166 – 421651RCC1 3-5Add
    BLAST
    Repeati4218 – 426851RCC1 3-6Add
    BLAST
    Repeati4270 – 432051RCC1 3-7Add
    BLAST
    Domaini4459 – 4796338HECTPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili948 – 98134Sequence AnalysisAdd
    BLAST

    Domaini

    The ZZ-type zinc finger mediates binding to SUMO1, and at lowe level SUMO2.By similarity
    The RCC1 repeats are grouped into three seven-bladed beta-propeller regions.By similarity

    Sequence similaritiesi

    Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
    Contains 1 DOC domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 1 MIB/HERC2 domain.PROSITE-ProRule annotation
    Contains 21 RCC1 repeats.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri2703 – 275048ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5021.
    GeneTreeiENSGT00750000117470.
    HOVERGENiHBG081598.
    InParanoidiQ4U2R1.
    KOiK10595.
    OMAiGHGTDVH.
    OrthoDBiEOG70KGNN.
    TreeFamiTF320636.

    Family and domain databases

    Gene3Di2.130.10.30. 3 hits.
    2.30.30.30. 1 hit.
    2.60.120.260. 1 hit.
    3.10.120.10. 1 hit.
    InterProiIPR004939. APC_su10/DOC_dom.
    IPR006624. Beta-propeller_rpt_TECPR.
    IPR021097. CPH_domain.
    IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR008979. Galactose-bd-like.
    IPR000569. HECT.
    IPR010606. Mib_Herc2.
    IPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    IPR014722. Rib_L2_dom2.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF03256. APC10. 1 hit.
    PF11515. Cul7. 1 hit.
    PF00173. Cyt-b5. 1 hit.
    PF00632. HECT. 1 hit.
    PF06701. MIB_HERC2. 1 hit.
    PF00415. RCC1. 18 hits.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    PRINTSiPR00633. RCCNDNSATION.
    SMARTiSM00119. HECTc. 1 hit.
    SM00706. TECPR. 4 hits.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF50985. SSF50985. 3 hits.
    SSF55856. SSF55856. 1 hit.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
    PS51284. DOC. 1 hit.
    PS50237. HECT. 1 hit.
    PS51416. MIB_HERC2. 1 hit.
    PS00626. RCC1_2. 1 hit.
    PS50012. RCC1_3. 19 hits.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 12 Publications (identifier: Q4U2R1-1) [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

    MPSESFCLAA QSRLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT     50
    ELAQNRELPL RKDDGVDAQS GTKKEDLNDK EKKEEEETPA PVYRAKSILE 100
    SWVWGRQPDV NELKECLSVL VKEQQALAVQ SATTTLSALR LKQRLVILER 150
    YFIALNRTVF QENVKVKWKS SSISVPPTEK KSARPTGRGV EGLARVGSRA 200
    ALSFAFAFLR RAWRSGEDAD LCSELLQESL DALRALPEAS LFDESTVSSV 250
    WLEVVERATR FLRSVVTGDV HGTPGTKGPG GVPLQDQHLA LAILLELAVQ 300
    RGTLSQMLSA ILLLLQLWDS GAQETDNERS AQGTSAPLLP LLQRFQSIIC 350
    SKDVPHTESD MHLLSGPLSP NESFLRYLTL PQDNELAIDL RQTAVVVMAH 400
    LDRLATPCMP PLCSSPTSHK GSLQEVIGWG LIGWKYYANV IGPIQCEGLA 450
    SLGVMQVACA EKRFLILSRN GRVYTQAYNS DMLAPQLVQG LASRNIVKIA 500
    AHSDGHHYLA LAATGEVYSW GCGDGGRLGH GDTVPLEEPK VISAFSGKQA 550
    GKHVVHIACG STYSAAITAE GELYTWGRGN YGRLGHGSSE DEAIPMLVAG 600
    LKGLKVIDVA CGSGDAQTLA VTENGQVWSW GDGDYGKLGR GGSDGCKTPK 650
    LIEKLQDLDV IKVRCGSQFS IALTKDGQVY SWGKGDNQRL GHGTEEHVRY 700
    PKLLEGLQGK KVIDVAAGST HCLALTEDSE VHSWGSNDQC QHFDTLRVTK 750
    PEPTALPGLD SKHIVGIACG PAQSFAWSSC SEWSIGLRVP FVVDICSMTF 800
    EQLDLLLRQV SEGMDGTADW PPPQEKECMA VATLNLLRLQ LHAAISHQVD 850
    PEFLGLGLGS VLLNSLKQTV VTLASSAGVL STVQSAAQAV LQSGWSVLLP 900
    TAEERARALS ALLPCTVSGN EVNISPGRRF MIDLLVGSLM ADGGLESALN 950
    AAITAEIQDI EAKKEAQKEK EIDEQEASAS TFHRSRTPLD KDLINTGIYE 1000
    SSGKQCLPLV QLIQQLLRNI ASQTVARLKD VARRISSCLD FEQQSCERSA 1050
    SLDLLLRFQR LLISKLYPGE KIGPISDTSS PELMGVGSLL KKYTALVCTH 1100
    IGDILPVAAS IASSSWQHFA EVACVMEGDF TGVLLPELVV SIVLLLSKNA 1150
    SLMQEAGAIP LLGGLLEHLD RFNHLAPGKE RDDHEELAWP GIMESFFTGQ 1200
    NCRNNEEVTL IRKADLENHN KDGGFWTVID GKVYGIKDFQ TQSLTGNSIL 1250
    AQFAGEDPVV ALEAALQFED TQESMHAFCV GQYLEPDQEV VTIPDLGSLS 1300
    SPLIDTERNL GLLLGLHASY LAMSTPLSPV EVECAKWLQS SIFSGGLQTS 1350
    QIHYSYNEEK DEDHCSSPGG TPISKSRLCS HRWALGDHSQ AFLQAIADNN 1400
    IQDYNVKDFL CQIERYCRQC HLTTPITFPP EHPVEEVGRL LLCCLLKHED 1450
    LGHVALSLVH VGTLGIEQVK HRTLPKSVVD VCRVVYQAKC SLIKTHQEQG 1500
    RSYKEVCAPV IERLRFLFNE LRPAVCSDLS IMSKFKLLGS LPRWRRIAQK 1550
    IIRERRKKRV PKKPESIDSE EKIGNEESDL EEACVLPHSP INVDKRPISM 1600
    KSPKDKWQPL LNTVTGVHKY KWLKQNVQGL YPQSALLNTI VEFALKEEPV 1650
    DVEKMRKCLL KQLERAEVRL EGIDTILKLA AKSFLLPSVQ YAMFCGWQRL 1700
    IPEGIDIGEP LTDCLRDVDL IPPFNRMLLE VTFGKLYAWA VQNIRSVLMD 1750
    ASARFKELGI QPVPLQTITN ENPAGPSLGT IPQARFLLVM LSMLTLQHGA 1800
    NNLDLLLNSG TLALTQTALR LIGPTCDSVE DDMNASARGA SATVLEETRK 1850
    ETAPVQLPVS GPELAAMMKI GTRVMRGVDW KWGDQDGPPP GLGRVIGELG 1900
    EDGWIRVQWD TGSTNSYRMG KEGKYDLKLV ELPVSSQPSA EDSDTEDDSE 1950
    AEQGERNIHP TAMMLTSVIN LLQTLCLSVG VHADIMQSEA TKTLCGLLRM 2000
    LVESGTTDKP APPDRLVARE QHRSWCTLGF VRSIALTPQA CGALSSPRWI 2050
    TLLMKVVEGH APFTAASLQR QILAVHLLQA VLPSWDKTER ARDMKCLVEK 2100
    LFGFLGSLLT TCSSDVPLLR ESTLRKRRAR PQASLTATHS STLAEEVVGL 2150
    LRTLHSLTQW NGLINKYINS QLCSVTQSYA GKTSERAQLE DYFPDSENLE 2200
    VGGLMAVLAV IGGIDGRLRL GGQVMHDEFG EGTVTRITPK GRITVQFCDM 2250
    RMCRVCPLNQ LKPLPAVAFS VNNLPFTEPM LSVWAELVNL AGSKLEKHKT 2300
    KKSAKPAFAG QVDLDLLRSQ QLKLYILKAG RALLSHQDKL RQILSQPAVQ 2350
    GTGTLQTDDG AAASPDLGDM SPEGPQPPMI LLQQLLSSAT QPSPVKAIFD 2400
    KQELEAAALA LCQCLAVEST HPSSPGCEDC SSSEATTPVS VQHIHLARAK 2450
    KRRQSPAPAL PIVVQLMEMG FPRKNIEFAL KSLTGTSGNA SGLPGVEALV 2500
    GWLLDHSDVQ VTEFSDAETL SDEYSDEEVV EDVDDTPYPV AAGAVVTESQ 2550
    TYKKRADFLS NDDYAVYVRE NVQVGMMVRC CRTYEEVCEG DVGKVIKLDR 2600
    DGLHDLNVQC DWQQKGGTYW VRYIHVELIG YPPPSSSSHI KIGDKVRVKA 2650
    SVTTPKYKWG SVTHQSVGLV KAFSANGKDI IVDFPQQSHW TGLLSEMELV 2700
    PSIHPGVTCD GCQTFPINGS RFKCRNCDDF DFCETCFKTK KHNTRHTFGR 2750
    INEPGQSAVF CGRSGKQLKR CHSSQPGMLL DSWSRMVKSL NVSSSVNQAS 2800
    RLIDGSEPCW QSSGSQGKHW IRLEIFPDVL VHRLKMIVDP ADSSYMPSLV 2850
    VVSGGNSLNN LIELKTININ QTDTTVPLLS DCAEYHRYIE IAIKQCRSSG 2900
    IDCKIHGLIL LGRIRAEEED LAAVPFLASD NEEEEDDKGS TGSLIRKKTP 2950
    GLESTATIRT KVFVWGLNDK DQLGGLKGSK IKVPSFSETL SALNVVQVAG 3000
    GSKSLFAVTV EGKVYSCGEA TNGRLGLGMS SGTVPIPRQI TALSSYVVKK 3050
    VAVHSGGRHA TALTVDGKVF SWGEGDDGKL GHFSRMNCDK PRLIEALKTK 3100
    RIRDIACGSS HSAALTSSGE LYTWGLGEYG RLGHGDNTTQ LKPKMVKVLL 3150
    GHRVIQVACG SRDAQTLALT DEGLVFSWGD GDFGKLGRGG SEGCNIPQNI 3200
    ERLNGQGVCQ IECGAQFSLA LTKSGVVWTW GKGDYFRLGH GSDVHVRKPQ 3250
    VVEGLRGKKI VHVAVGALHC LAVTDSGQVY AWGDNDHGQQ GNGTTTVNRK 3300
    PTLVQGLEGQ KITRVACGSS HSVAWTTVDV ATPSVHEPVL FQTARDPLGA 3350
    SYLGVPSDAD SSSSSNKISG ANNCKPNRPS LAKILLSLEG NLAKQQALSH 3400
    ILTALQIMYA RDAVVGALMP AGMLAPVECP SFSSSAPASD VSAMASPMHM 3450
    EDSTLAADLE DRLSPNLWQE KREIVSSEDA VTPSAVTPSA PSASSRPFIP 3500
    VTDDPGAASI IAETMTKTKE DVESQNKTSG PEPQSLDEFT SLLIPDDTRV 3550
    VVELLKLSVC SRAGDKGREV LSAVLSGMGT AYPQVADMLL ELCVTELEDV 3600
    ATDSQSGRLS SQPVVVESSH PYTDDTSTSG TVKIPGAEGL RVEFDRQCST 3650
    ERRHDPLTVM DGVNRIVSVR SGREWSDWSS ELRIPGDELK WKFISDGSVN 3700
    GWGWRFTVYP IMPAAGPKDL LSDRCVLSCP SMDLVTCLLD FRLNLTSNRS 3750
    IVPRLAASLA ACAQLSALAA SHRMWALQRL RRLLTTEFGQ SININRLLGE 3800
    NDGESRALSF TGSALAALVK GLPEALQRQF EYEDPIVRGG KQLLHSPFFK 3850
    VLVALACDLE LDTLPCCAET HKWAWFRRYC MASRVAVALD KRTPLPRLFL 3900
    DEVAKKIREL MADSESMDVL HESHSIFKRE QDEQLVQWMN RRPDDWTLSA 3950
    GGSGTIYGWG HNHRGQLGGI EGAKVKVPTP CEALATLRPV QLIGGEQTLF 4000
    AVTADGKLYA TGYGAGGRLG IGGTESVSTP TLLESIQHVF IKKVAVNSGG 4050
    KHCLALSSEG EVYSWGEAED GKLGHGNRSP CDRPRVIESL RGIEVVDVAA 4100
    GGAHSACVTA AGDLYTWGKG RYGRLGHSDS EDQLKPKLVE ALQGHRVIDI 4150
    ACGSGDAQTL CLTDDDTVWS WGDGDYGKLG RGGSDGCKVP MKIDSLTGLG 4200
    VVKVECGSQF SVALTKSGAV YTWGKGDYHR LGHGSDDHVR RPRQVQGLQG 4250
    KKVIAIATGS LHCVCCTEDG EVYTWGDNDE GQLGDGTTNA IQRPRLVAAL 4300
    QGKKVNRVAC GSAHTLAWST SKPASAGKLP AQVPMEYNHL QEIPIIALRN 4350
    RLLLLHHISE LFCPCIPMFD LEGSLDETGL GPSVGFDTLR GILISQGKEA 4400
    AFRKVVQATM VRDRQHGPVV ELNRIQVKRS RSKGGLAGPD GTKSVFGQMC 4450
    AKMSSFSPDS LLLPHRVWKV KFVGESVDDC GGGYSESIAE ICEELQNGLT 4500
    PLLIVTPNGR DESGANRDCY LLNPATRAPV HCSMFRFLGV LLGIAIRTGS 4550
    PLSLNLAEPV WKQLAGMSLT IADLSEVDKD FIPGLMYIRD NEATSEEFEA 4600
    MSLPFTVPSA SGQDIQLSSK HTHITLDNRA EYVRLAINYR LHEFDEQVAA 4650
    VREGMARVVP VPLLSLFTGY ELETMVCGSP DIPLHLLKSV ATYKGIEPSA 4700
    SLVQWFWEVM ESFSNTERSL FLRFVWGRTR LPRTIADFRG RDFVIQVLDK 4750
    YNPPDHFLPE SYTCFFLLKL PRYSCKQVLE EKLKYAIHFC KSIDTDDYAR 4800
    IALTGEPAAD DSSEDSDNED ADSFASDSTQ DYLTGH 4836
    Length:4,836
    Mass (Da):527,456
    Last modified:July 27, 2011 - v3
    Checksum:i481BC90E231C93D8
    GO
    Isoform 21 Publication (identifier: Q4U2R1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3637-3672: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:4,800
    Mass (Da):523,388
    Checksum:i3E3BA1D6DE63BAF7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti692 – 6921H → L in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti724 – 7241A → V in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti747 – 7471R → G in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti756 – 7561L → F in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti929 – 9291R → P in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti1114 – 11141S → N in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti1235 – 12351G → D in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti2348 – 23481A → P in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti2470 – 24701G → S in BAE36828. (PubMed:16141072)Curated
    Sequence conflicti2523 – 25231E → D in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti2567 – 25671Y → F in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti2572 – 25721V → L in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti3095 – 30951E → Q in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti3107 – 31071C → Y in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti3114 – 31141A → P in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti3161 – 31611S → T in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti3385 – 33862LL → VV in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti3508 – 35081A → V in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti4069 – 40691E → K in BAD90404. 1 PublicationCurated
    Sequence conflicti4187 – 41871C → S in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti4604 – 46041P → S in BAE36593. (PubMed:16141072)Curated
    Sequence conflicti4716 – 47161T → A in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti4723 – 47231R → C in AAD08658. (PubMed:9949213)Curated
    Sequence conflicti4730 – 47301R → S in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti4752 – 47521N → Y in AAC31431. (PubMed:9689098)Curated
    Sequence conflicti4790 – 47901C → S in AAC31431. (PubMed:9689098)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei3637 – 367236Missing in isoform 2. 1 PublicationVSP_051975Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061529 mRNA. Translation: AAC31431.1.
    AF071173 mRNA. Translation: AAD08658.1.
    AC102121 Genomic DNA. No translation available.
    AC102150 Genomic DNA. No translation available.
    AK141515 mRNA. Translation: BAE24711.1.
    AK148361 mRNA. Translation: BAE28504.1.
    AK161826 mRNA. Translation: BAE36593.1.
    AK162270 mRNA. Translation: BAE36828.1.
    AK162708 mRNA. Translation: BAE37031.1.
    AK220338 mRNA. Translation: BAD90404.1.
    BC044667 mRNA. Translation: AAH44667.1.
    BC054829 mRNA. Translation: AAH54829.1.
    CCDSiCCDS21318.1. [Q4U2R1-1]
    RefSeqiNP_034548.2. NM_010418.2. [Q4U2R1-1]
    XP_006540700.1. XM_006540637.1. [Q4U2R1-1]
    XP_006540701.1. XM_006540638.1. [Q4U2R1-1]
    XP_006540702.1. XM_006540639.1. [Q4U2R1-2]
    UniGeneiMm.20929.

    Genome annotation databases

    EnsembliENSMUST00000076226; ENSMUSP00000075579; ENSMUSG00000030451. [Q4U2R1-1]
    ENSMUST00000164095; ENSMUSP00000131573; ENSMUSG00000030451. [Q4U2R1-1]
    GeneIDi15204.
    KEGGimmu:15204.
    UCSCiuc009hdv.1. mouse. [Q4U2R1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061529 mRNA. Translation: AAC31431.1 .
    AF071173 mRNA. Translation: AAD08658.1 .
    AC102121 Genomic DNA. No translation available.
    AC102150 Genomic DNA. No translation available.
    AK141515 mRNA. Translation: BAE24711.1 .
    AK148361 mRNA. Translation: BAE28504.1 .
    AK161826 mRNA. Translation: BAE36593.1 .
    AK162270 mRNA. Translation: BAE36828.1 .
    AK162708 mRNA. Translation: BAE37031.1 .
    AK220338 mRNA. Translation: BAD90404.1 .
    BC044667 mRNA. Translation: AAH44667.1 .
    BC054829 mRNA. Translation: AAH54829.1 .
    CCDSi CCDS21318.1. [Q4U2R1-1 ]
    RefSeqi NP_034548.2. NM_010418.2. [Q4U2R1-1 ]
    XP_006540700.1. XM_006540637.1. [Q4U2R1-1 ]
    XP_006540701.1. XM_006540638.1. [Q4U2R1-1 ]
    XP_006540702.1. XM_006540639.1. [Q4U2R1-2 ]
    UniGenei Mm.20929.

    3D structure databases

    ProteinModelPortali Q4U2R1.
    SMRi Q4U2R1. Positions 423-780, 1206-1297, 1868-1929, 3955-4320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200274. 3 interactions.

    PTM databases

    PhosphoSitei Q4U2R1.

    Proteomic databases

    MaxQBi Q4U2R1.
    PaxDbi Q4U2R1.
    PRIDEi Q4U2R1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000076226 ; ENSMUSP00000075579 ; ENSMUSG00000030451 . [Q4U2R1-1 ]
    ENSMUST00000164095 ; ENSMUSP00000131573 ; ENSMUSG00000030451 . [Q4U2R1-1 ]
    GeneIDi 15204.
    KEGGi mmu:15204.
    UCSCi uc009hdv.1. mouse. [Q4U2R1-1 ]

    Organism-specific databases

    CTDi 8924.
    MGIi MGI:103234. Herc2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5021.
    GeneTreei ENSGT00750000117470.
    HOVERGENi HBG081598.
    InParanoidi Q4U2R1.
    KOi K10595.
    OMAi GHGTDVH.
    OrthoDBi EOG70KGNN.
    TreeFami TF320636.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi HERC2. mouse.
    NextBioi 287753.
    PROi Q4U2R1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q4U2R1.
    Genevestigatori Q4U2R1.

    Family and domain databases

    Gene3Di 2.130.10.30. 3 hits.
    2.30.30.30. 1 hit.
    2.60.120.260. 1 hit.
    3.10.120.10. 1 hit.
    InterProi IPR004939. APC_su10/DOC_dom.
    IPR006624. Beta-propeller_rpt_TECPR.
    IPR021097. CPH_domain.
    IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR008979. Galactose-bd-like.
    IPR000569. HECT.
    IPR010606. Mib_Herc2.
    IPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    IPR014722. Rib_L2_dom2.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF03256. APC10. 1 hit.
    PF11515. Cul7. 1 hit.
    PF00173. Cyt-b5. 1 hit.
    PF00632. HECT. 1 hit.
    PF06701. MIB_HERC2. 1 hit.
    PF00415. RCC1. 18 hits.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    PRINTSi PR00633. RCCNDNSATION.
    SMARTi SM00119. HECTc. 1 hit.
    SM00706. TECPR. 4 hits.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF50985. SSF50985. 3 hits.
    SSF55856. SSF55856. 1 hit.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50255. CYTOCHROME_B5_2. 1 hit.
    PS51284. DOC. 1 hit.
    PS50237. HECT. 1 hit.
    PS51416. MIB_HERC2. 1 hit.
    PS00626. RCC1_2. 1 hit.
    PS50012. RCC1_3. 19 hits.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DISEASE.
      Strain: C57BL/6Imported.
    2. "The ancestral gene for transcribed, low-copy repeats in the Prader-Willi/Angelman region encodes a large protein implicated in protein trafficking, which is deficient in mice with neuromuscular and spermiogenic abnormalities."
      Ji Y., Walkowicz M.J., Buiting K., Johnson D.K., Tarvin R.E., Rinchik E.M., Horsthemke B., Stubbs L., Nicholls R.D.
      Hum. Mol. Genet. 8:533-542(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISEASE.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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 953-1553; 1845-2470 AND 4123-4836.
      Strain: C57BL/6JImported.
      Tissue: Spinal cordImported, TestisImported and VaginaImported.
    5. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2966-4836 (ISOFORM 1).
      Tissue: BrainImported.
    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] OF 3618-4836 (ISOFORM 2).
      Strain: C57BL/6Imported and Czech IIImported.
      Tissue: Mammary glandImported and Olfactory epitheliumImported.
    7. "Molecular characterization of radiation- and chemically induced mutations associated with neuromuscular tremors, runting, juvenile lethality, and sperm defects in jdf2 mice."
      Walkowicz M., Ji Y., Ren X., Horsthemke B., Russell L.B., Johnson D., Rinchik E.M., Nicholls R.D., Stubbs L.
      Mamm. Genome 10:870-878(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiHERC2_MOUSE
    AccessioniPrimary (citable) accession number: Q4U2R1
    Secondary accession number(s): E9PZT6
    , O88473, Q3TRJ8, Q3TS47, Q3TST2, Q3UFQ6, Q3URH7, Q5DU32, Q7TPR5, Q80VV7, Q9QYT1, Q9Z168, Q9Z171
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 92 of the entry and version 3 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