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Q4U2R1

- HERC2_MOUSE

UniProt

Q4U2R1 - HERC2_MOUSE

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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

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
Complete GO annotation...

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. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: MGI
  4. nucleus Source: UniProtKB
Complete GO annotation...

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.
GeneTreeiENSGT00760000118918.
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.

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        10         20         30         40         50
MPSESFCLAA QSRLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT
60 70 80 90 100
ELAQNRELPL RKDDGVDAQS GTKKEDLNDK EKKEEEETPA PVYRAKSILE
110 120 130 140 150
SWVWGRQPDV NELKECLSVL VKEQQALAVQ SATTTLSALR LKQRLVILER
160 170 180 190 200
YFIALNRTVF QENVKVKWKS SSISVPPTEK KSARPTGRGV EGLARVGSRA
210 220 230 240 250
ALSFAFAFLR RAWRSGEDAD LCSELLQESL DALRALPEAS LFDESTVSSV
260 270 280 290 300
WLEVVERATR FLRSVVTGDV HGTPGTKGPG GVPLQDQHLA LAILLELAVQ
310 320 330 340 350
RGTLSQMLSA ILLLLQLWDS GAQETDNERS AQGTSAPLLP LLQRFQSIIC
360 370 380 390 400
SKDVPHTESD MHLLSGPLSP NESFLRYLTL PQDNELAIDL RQTAVVVMAH
410 420 430 440 450
LDRLATPCMP PLCSSPTSHK GSLQEVIGWG LIGWKYYANV IGPIQCEGLA
460 470 480 490 500
SLGVMQVACA EKRFLILSRN GRVYTQAYNS DMLAPQLVQG LASRNIVKIA
510 520 530 540 550
AHSDGHHYLA LAATGEVYSW GCGDGGRLGH GDTVPLEEPK VISAFSGKQA
560 570 580 590 600
GKHVVHIACG STYSAAITAE GELYTWGRGN YGRLGHGSSE DEAIPMLVAG
610 620 630 640 650
LKGLKVIDVA CGSGDAQTLA VTENGQVWSW GDGDYGKLGR GGSDGCKTPK
660 670 680 690 700
LIEKLQDLDV IKVRCGSQFS IALTKDGQVY SWGKGDNQRL GHGTEEHVRY
710 720 730 740 750
PKLLEGLQGK KVIDVAAGST HCLALTEDSE VHSWGSNDQC QHFDTLRVTK
760 770 780 790 800
PEPTALPGLD SKHIVGIACG PAQSFAWSSC SEWSIGLRVP FVVDICSMTF
810 820 830 840 850
EQLDLLLRQV SEGMDGTADW PPPQEKECMA VATLNLLRLQ LHAAISHQVD
860 870 880 890 900
PEFLGLGLGS VLLNSLKQTV VTLASSAGVL STVQSAAQAV LQSGWSVLLP
910 920 930 940 950
TAEERARALS ALLPCTVSGN EVNISPGRRF MIDLLVGSLM ADGGLESALN
960 970 980 990 1000
AAITAEIQDI EAKKEAQKEK EIDEQEASAS TFHRSRTPLD KDLINTGIYE
1010 1020 1030 1040 1050
SSGKQCLPLV QLIQQLLRNI ASQTVARLKD VARRISSCLD FEQQSCERSA
1060 1070 1080 1090 1100
SLDLLLRFQR LLISKLYPGE KIGPISDTSS PELMGVGSLL KKYTALVCTH
1110 1120 1130 1140 1150
IGDILPVAAS IASSSWQHFA EVACVMEGDF TGVLLPELVV SIVLLLSKNA
1160 1170 1180 1190 1200
SLMQEAGAIP LLGGLLEHLD RFNHLAPGKE RDDHEELAWP GIMESFFTGQ
1210 1220 1230 1240 1250
NCRNNEEVTL IRKADLENHN KDGGFWTVID GKVYGIKDFQ TQSLTGNSIL
1260 1270 1280 1290 1300
AQFAGEDPVV ALEAALQFED TQESMHAFCV GQYLEPDQEV VTIPDLGSLS
1310 1320 1330 1340 1350
SPLIDTERNL GLLLGLHASY LAMSTPLSPV EVECAKWLQS SIFSGGLQTS
1360 1370 1380 1390 1400
QIHYSYNEEK DEDHCSSPGG TPISKSRLCS HRWALGDHSQ AFLQAIADNN
1410 1420 1430 1440 1450
IQDYNVKDFL CQIERYCRQC HLTTPITFPP EHPVEEVGRL LLCCLLKHED
1460 1470 1480 1490 1500
LGHVALSLVH VGTLGIEQVK HRTLPKSVVD VCRVVYQAKC SLIKTHQEQG
1510 1520 1530 1540 1550
RSYKEVCAPV IERLRFLFNE LRPAVCSDLS IMSKFKLLGS LPRWRRIAQK
1560 1570 1580 1590 1600
IIRERRKKRV PKKPESIDSE EKIGNEESDL EEACVLPHSP INVDKRPISM
1610 1620 1630 1640 1650
KSPKDKWQPL LNTVTGVHKY KWLKQNVQGL YPQSALLNTI VEFALKEEPV
1660 1670 1680 1690 1700
DVEKMRKCLL KQLERAEVRL EGIDTILKLA AKSFLLPSVQ YAMFCGWQRL
1710 1720 1730 1740 1750
IPEGIDIGEP LTDCLRDVDL IPPFNRMLLE VTFGKLYAWA VQNIRSVLMD
1760 1770 1780 1790 1800
ASARFKELGI QPVPLQTITN ENPAGPSLGT IPQARFLLVM LSMLTLQHGA
1810 1820 1830 1840 1850
NNLDLLLNSG TLALTQTALR LIGPTCDSVE DDMNASARGA SATVLEETRK
1860 1870 1880 1890 1900
ETAPVQLPVS GPELAAMMKI GTRVMRGVDW KWGDQDGPPP GLGRVIGELG
1910 1920 1930 1940 1950
EDGWIRVQWD TGSTNSYRMG KEGKYDLKLV ELPVSSQPSA EDSDTEDDSE
1960 1970 1980 1990 2000
AEQGERNIHP TAMMLTSVIN LLQTLCLSVG VHADIMQSEA TKTLCGLLRM
2010 2020 2030 2040 2050
LVESGTTDKP APPDRLVARE QHRSWCTLGF VRSIALTPQA CGALSSPRWI
2060 2070 2080 2090 2100
TLLMKVVEGH APFTAASLQR QILAVHLLQA VLPSWDKTER ARDMKCLVEK
2110 2120 2130 2140 2150
LFGFLGSLLT TCSSDVPLLR ESTLRKRRAR PQASLTATHS STLAEEVVGL
2160 2170 2180 2190 2200
LRTLHSLTQW NGLINKYINS QLCSVTQSYA GKTSERAQLE DYFPDSENLE
2210 2220 2230 2240 2250
VGGLMAVLAV IGGIDGRLRL GGQVMHDEFG EGTVTRITPK GRITVQFCDM
2260 2270 2280 2290 2300
RMCRVCPLNQ LKPLPAVAFS VNNLPFTEPM LSVWAELVNL AGSKLEKHKT
2310 2320 2330 2340 2350
KKSAKPAFAG QVDLDLLRSQ QLKLYILKAG RALLSHQDKL RQILSQPAVQ
2360 2370 2380 2390 2400
GTGTLQTDDG AAASPDLGDM SPEGPQPPMI LLQQLLSSAT QPSPVKAIFD
2410 2420 2430 2440 2450
KQELEAAALA LCQCLAVEST HPSSPGCEDC SSSEATTPVS VQHIHLARAK
2460 2470 2480 2490 2500
KRRQSPAPAL PIVVQLMEMG FPRKNIEFAL KSLTGTSGNA SGLPGVEALV
2510 2520 2530 2540 2550
GWLLDHSDVQ VTEFSDAETL SDEYSDEEVV EDVDDTPYPV AAGAVVTESQ
2560 2570 2580 2590 2600
TYKKRADFLS NDDYAVYVRE NVQVGMMVRC CRTYEEVCEG DVGKVIKLDR
2610 2620 2630 2640 2650
DGLHDLNVQC DWQQKGGTYW VRYIHVELIG YPPPSSSSHI KIGDKVRVKA
2660 2670 2680 2690 2700
SVTTPKYKWG SVTHQSVGLV KAFSANGKDI IVDFPQQSHW TGLLSEMELV
2710 2720 2730 2740 2750
PSIHPGVTCD GCQTFPINGS RFKCRNCDDF DFCETCFKTK KHNTRHTFGR
2760 2770 2780 2790 2800
INEPGQSAVF CGRSGKQLKR CHSSQPGMLL DSWSRMVKSL NVSSSVNQAS
2810 2820 2830 2840 2850
RLIDGSEPCW QSSGSQGKHW IRLEIFPDVL VHRLKMIVDP ADSSYMPSLV
2860 2870 2880 2890 2900
VVSGGNSLNN LIELKTININ QTDTTVPLLS DCAEYHRYIE IAIKQCRSSG
2910 2920 2930 2940 2950
IDCKIHGLIL LGRIRAEEED LAAVPFLASD NEEEEDDKGS TGSLIRKKTP
2960 2970 2980 2990 3000
GLESTATIRT KVFVWGLNDK DQLGGLKGSK IKVPSFSETL SALNVVQVAG
3010 3020 3030 3040 3050
GSKSLFAVTV EGKVYSCGEA TNGRLGLGMS SGTVPIPRQI TALSSYVVKK
3060 3070 3080 3090 3100
VAVHSGGRHA TALTVDGKVF SWGEGDDGKL GHFSRMNCDK PRLIEALKTK
3110 3120 3130 3140 3150
RIRDIACGSS HSAALTSSGE LYTWGLGEYG RLGHGDNTTQ LKPKMVKVLL
3160 3170 3180 3190 3200
GHRVIQVACG SRDAQTLALT DEGLVFSWGD GDFGKLGRGG SEGCNIPQNI
3210 3220 3230 3240 3250
ERLNGQGVCQ IECGAQFSLA LTKSGVVWTW GKGDYFRLGH GSDVHVRKPQ
3260 3270 3280 3290 3300
VVEGLRGKKI VHVAVGALHC LAVTDSGQVY AWGDNDHGQQ GNGTTTVNRK
3310 3320 3330 3340 3350
PTLVQGLEGQ KITRVACGSS HSVAWTTVDV ATPSVHEPVL FQTARDPLGA
3360 3370 3380 3390 3400
SYLGVPSDAD SSSSSNKISG ANNCKPNRPS LAKILLSLEG NLAKQQALSH
3410 3420 3430 3440 3450
ILTALQIMYA RDAVVGALMP AGMLAPVECP SFSSSAPASD VSAMASPMHM
3460 3470 3480 3490 3500
EDSTLAADLE DRLSPNLWQE KREIVSSEDA VTPSAVTPSA PSASSRPFIP
3510 3520 3530 3540 3550
VTDDPGAASI IAETMTKTKE DVESQNKTSG PEPQSLDEFT SLLIPDDTRV
3560 3570 3580 3590 3600
VVELLKLSVC SRAGDKGREV LSAVLSGMGT AYPQVADMLL ELCVTELEDV
3610 3620 3630 3640 3650
ATDSQSGRLS SQPVVVESSH PYTDDTSTSG TVKIPGAEGL RVEFDRQCST
3660 3670 3680 3690 3700
ERRHDPLTVM DGVNRIVSVR SGREWSDWSS ELRIPGDELK WKFISDGSVN
3710 3720 3730 3740 3750
GWGWRFTVYP IMPAAGPKDL LSDRCVLSCP SMDLVTCLLD FRLNLTSNRS
3760 3770 3780 3790 3800
IVPRLAASLA ACAQLSALAA SHRMWALQRL RRLLTTEFGQ SININRLLGE
3810 3820 3830 3840 3850
NDGESRALSF TGSALAALVK GLPEALQRQF EYEDPIVRGG KQLLHSPFFK
3860 3870 3880 3890 3900
VLVALACDLE LDTLPCCAET HKWAWFRRYC MASRVAVALD KRTPLPRLFL
3910 3920 3930 3940 3950
DEVAKKIREL MADSESMDVL HESHSIFKRE QDEQLVQWMN RRPDDWTLSA
3960 3970 3980 3990 4000
GGSGTIYGWG HNHRGQLGGI EGAKVKVPTP CEALATLRPV QLIGGEQTLF
4010 4020 4030 4040 4050
AVTADGKLYA TGYGAGGRLG IGGTESVSTP TLLESIQHVF IKKVAVNSGG
4060 4070 4080 4090 4100
KHCLALSSEG EVYSWGEAED GKLGHGNRSP CDRPRVIESL RGIEVVDVAA
4110 4120 4130 4140 4150
GGAHSACVTA AGDLYTWGKG RYGRLGHSDS EDQLKPKLVE ALQGHRVIDI
4160 4170 4180 4190 4200
ACGSGDAQTL CLTDDDTVWS WGDGDYGKLG RGGSDGCKVP MKIDSLTGLG
4210 4220 4230 4240 4250
VVKVECGSQF SVALTKSGAV YTWGKGDYHR LGHGSDDHVR RPRQVQGLQG
4260 4270 4280 4290 4300
KKVIAIATGS LHCVCCTEDG EVYTWGDNDE GQLGDGTTNA IQRPRLVAAL
4310 4320 4330 4340 4350
QGKKVNRVAC GSAHTLAWST SKPASAGKLP AQVPMEYNHL QEIPIIALRN
4360 4370 4380 4390 4400
RLLLLHHISE LFCPCIPMFD LEGSLDETGL GPSVGFDTLR GILISQGKEA
4410 4420 4430 4440 4450
AFRKVVQATM VRDRQHGPVV ELNRIQVKRS RSKGGLAGPD GTKSVFGQMC
4460 4470 4480 4490 4500
AKMSSFSPDS LLLPHRVWKV KFVGESVDDC GGGYSESIAE ICEELQNGLT
4510 4520 4530 4540 4550
PLLIVTPNGR DESGANRDCY LLNPATRAPV HCSMFRFLGV LLGIAIRTGS
4560 4570 4580 4590 4600
PLSLNLAEPV WKQLAGMSLT IADLSEVDKD FIPGLMYIRD NEATSEEFEA
4610 4620 4630 4640 4650
MSLPFTVPSA SGQDIQLSSK HTHITLDNRA EYVRLAINYR LHEFDEQVAA
4660 4670 4680 4690 4700
VREGMARVVP VPLLSLFTGY ELETMVCGSP DIPLHLLKSV ATYKGIEPSA
4710 4720 4730 4740 4750
SLVQWFWEVM ESFSNTERSL FLRFVWGRTR LPRTIADFRG RDFVIQVLDK
4760 4770 4780 4790 4800
YNPPDHFLPE SYTCFFLLKL PRYSCKQVLE EKLKYAIHFC KSIDTDDYAR
4810 4820 4830
IALTGEPAAD DSSEDSDNED ADSFASDSTQ DYLTGH
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 ENSGT00760000118918.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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