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Protein

Probable E3 ubiquitin-protein ligase HERC1

Gene

HERC1

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

Functioni

Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.3 Publications

Pathway:iprotein 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei4811 – 48111Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor, Ligase

Keywords - Biological processi

Transport, Ubl conjugation pathway

Enzyme and pathway databases

SignaLinkiQ15751.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable E3 ubiquitin-protein ligase HERC1 (EC:6.3.2.-)
Alternative name(s):
HECT domain and RCC1-like domain-containing protein 1
p532
p619
Gene namesi
Name:HERC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:4867. HERC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: UniProtKB-SubCell
  • Golgi apparatus Source: ProtInc
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29242.

Polymorphism and mutation databases

BioMutaiHERC1.
DMDMi296434522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 48614861Probable E3 ubiquitin-protein ligase HERC1PRO_0000328871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1406 – 14061Phosphoserine1 Publication
Modified residuei1491 – 14911Phosphoserine1 Publication
Modified residuei1512 – 15121Phosphoserine1 Publication
Modified residuei1517 – 15171Phosphoserine1 Publication
Modified residuei1521 – 15211Phosphoserine3 Publications
Modified residuei2701 – 27011Phosphothreonine3 Publications
Modified residuei2706 – 27061Phosphoserine1 Publication
Modified residuei2710 – 27101Phosphoserine1 Publication
Modified residuei4857 – 48571Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15751.
PaxDbiQ15751.
PRIDEiQ15751.

PTM databases

PhosphoSiteiQ15751.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ15751.
CleanExiHS_HERC1.
ExpressionAtlasiQ15751. baseline and differential.
GenevisibleiQ15751. HS.

Organism-specific databases

HPAiHPA049749.

Interactioni

Subunit structurei

Interacts with TSC2; interaction is inhibited by TSC1. Interacts with PKM, ARF1 and ARF6. Forms a ternary complex with clathrin heavy chain (CLTC) and HSPA1A.5 Publications

Protein-protein interaction databases

BioGridi114439. 27 interactions.
IntActiQ15751. 6 interactions.
MINTiMINT-8330052.
STRINGi9606.ENSP00000390158.

Structurei

Secondary structure

1
4861
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2035 – 204612Combined sources
Turni2047 – 20493Combined sources
Beta strandi2050 – 20534Combined sources
Beta strandi2055 – 206511Combined sources
Beta strandi2069 – 208012Combined sources
Beta strandi2088 – 20936Combined sources
Turni2102 – 21043Combined sources
Beta strandi2106 – 21127Combined sources
Turni2113 – 21153Combined sources
Beta strandi2117 – 212711Combined sources
Beta strandi2136 – 21427Combined sources
Turni2143 – 21464Combined sources
Beta strandi2147 – 21526Combined sources
Beta strandi2158 – 21614Combined sources
Beta strandi2167 – 21759Combined sources
Beta strandi2178 – 21803Combined sources
Beta strandi2183 – 21875Combined sources
Beta strandi3999 – 40046Combined sources
Helixi4011 – 40133Combined sources
Beta strandi4015 – 40228Combined sources
Helixi4024 – 40263Combined sources
Beta strandi4029 – 40346Combined sources
Beta strandi4036 – 40438Combined sources
Beta strandi4048 – 40525Combined sources
Helixi4055 – 40573Combined sources
Beta strandi4060 – 40634Combined sources
Beta strandi4067 – 40726Combined sources
Helixi4074 – 40763Combined sources
Beta strandi4081 – 40866Combined sources
Beta strandi4093 – 40986Combined sources
Beta strandi4103 – 41075Combined sources
Helixi4110 – 41123Combined sources
Beta strandi4116 – 41183Combined sources
Beta strandi4122 – 41276Combined sources
Helixi4129 – 41313Combined sources
Beta strandi4136 – 41416Combined sources
Beta strandi4143 – 41508Combined sources
Beta strandi4155 – 41595Combined sources
Helixi4162 – 41643Combined sources
Beta strandi4168 – 41703Combined sources
Beta strandi4174 – 41796Combined sources
Helixi4181 – 41833Combined sources
Beta strandi4188 – 41936Combined sources
Beta strandi4195 – 42028Combined sources
Beta strandi4208 – 42125Combined sources
Helixi4215 – 42173Combined sources
Beta strandi4221 – 42233Combined sources
Beta strandi4227 – 42326Combined sources
Helixi4234 – 42363Combined sources
Beta strandi4237 – 42393Combined sources
Beta strandi4241 – 42466Combined sources
Beta strandi4248 – 42558Combined sources
Beta strandi4260 – 42645Combined sources
Helixi4266 – 42683Combined sources
Helixi4273 – 42786Combined sources
Helixi4286 – 42883Combined sources
Beta strandi4293 – 42986Combined sources
Beta strandi4300 – 43078Combined sources
Beta strandi4312 – 43165Combined sources
Beta strandi4325 – 43273Combined sources
Beta strandi4331 – 43366Combined sources
Helixi4338 – 43403Combined sources
Beta strandi4347 – 43504Combined sources
Beta strandi4352 – 43587Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O2WX-ray2.00A/B/C/D3975-4360[»]
4QT6X-ray1.64A2035-2192[»]
ProteinModelPortaliQ15751.
SMRiQ15751. Positions 2035-2192, 3996-4360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati371 – 42050RCC1 1Add
BLAST
Repeati421 – 47555RCC1 2Add
BLAST
Repeati476 – 52853RCC1 3Add
BLAST
Repeati529 – 57850RCC1 4Add
BLAST
Repeati580 – 63152RCC1 5Add
BLAST
Repeati633 – 68250RCC1 6Add
BLAST
Repeati683 – 73553RCC1 7Add
BLAST
Domaini2002 – 2193192B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Repeati3426 – 346540WD 1Add
BLAST
Repeati3484 – 352239WD 2Add
BLAST
Repeati3524 – 357249WD 3Add
BLAST
Repeati3580 – 361940WD 4Add
BLAST
Repeati3624 – 366340WD 5Add
BLAST
Repeati3667 – 371347WD 6Add
BLAST
Repeati3745 – 378440WD 7Add
BLAST
Repeati3996 – 404449RCC1 8Add
BLAST
Repeati4046 – 409954RCC1 9Add
BLAST
Repeati4101 – 415151RCC1 10Add
BLAST
Repeati4153 – 420351RCC1 11Add
BLAST
Repeati4205 – 425652RCC1 12Add
BLAST
Repeati4258 – 430851RCC1 13Add
BLAST
Repeati4310 – 436051RCC1 14Add
BLAST
Domaini4501 – 4848348HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1349 – 137830Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 14 RCC1 repeats.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00790000122949.
HOGENOMiHOG000168589.
HOVERGENiHBG053919.
InParanoidiQ15751.
KOiK10594.
OMAiHHYQDGI.
OrthoDBiEOG70KGNN.
PhylomeDBiQ15751.
TreeFamiTF106426.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
2.130.10.30. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR000569. HECT.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR003877. SPRY_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
PF00415. RCC1. 12 hits.
PF00622. SPRY. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SMARTiSM00119. HECTc. 1 hit.
SM00449. SPRY. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50978. SSF50978. 2 hits.
SSF50985. SSF50985. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50237. HECT. 1 hit.
PS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 14 hits.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATMIPPVKL KWLEHLNSSW ITEDSESIAT REGVAVLYSK LVSNKEVVPL
60 70 80 90 100
PQQVLCLKGP QLPDFERESL SSDEQDHYLD ALLSSQLALA KMVCSDSPFA
110 120 130 140 150
GALRKRLLVL QRVFYALSNK YHDKGKVKQQ QHSPESSSGS ADVHSVSERP
160 170 180 190 200
RSSTDALIEM GVRTGLSLLF ALLRQSWMMP VSGPGLSLCN DVIHTAIEVV
210 220 230 240 250
SSLPPLSLAN ESKIPPMGLD CLSQVTTFLK GVTIPNSGAD TLGRRLASEL
260 270 280 290 300
LLGLAAQRGS LRYLLEWIEM ALGASAVVHT MEKGKLLSSQ EGMISFDCFM
310 320 330 340 350
TILMQMRRSL GSSADRSQWR EPTRTSDGLC SLYEAALCLF EEVCRMASDY
360 370 380 390 400
SRTCASPDSI QTGDAPIVSE TCEVYVWGSN SSHQLVEGTQ EKILQPKLAP
410 420 430 440 450
SFSDAQTIEA GQYCTFVIST DGSVRACGKG SYGRLGLGDS NNQSTLKKLT
460 470 480 490 500
FEPHRSIKKV SSSKGSDGHT LAFTTEGEVF SWGDGDYGKL GHGNSSTQKY
510 520 530 540 550
PKLIQGPLQG KVVVCVSAGY RHSAAVTEDG ELYTWGEGDF GRLGHGDSNS
560 570 580 590 600
RNIPTLVKDI SNVGEVSCGS SHTIALSKDG RTVWSFGGGD NGKLGHGDTN
610 620 630 640 650
RVYKPKVIEA LQGMFIRKVC AGSQSSLALT STGQVYAWGC GACLGCGSSE
660 670 680 690 700
ATALRPKLIE ELAATRIVDV SIGDSHCLAL SHDNEVYAWG NNSMGQCGQG
710 720 730 740 750
NSTGPITKPK KVSGLDGIAI QQISAGTSHS LAWTALPRDR QVVAWHRPYC
760 770 780 790 800
VDLEESTFSH LRSFLERYCD KINSEIPPLP FPSSREHHSF LKLCLKLLSN
810 820 830 840 850
HLALALAGGV ATSILGRQAG PLRNLLFRLM DSTVPDEIQE VVIETLSVGA
860 870 880 890 900
TMLLPPLRER MELLHSLLPQ GPDRWESLSK GQRMQLDIIL TSLQDHTHVA
910 920 930 940 950
SLLGYSSPSD AADLSSVCTG YGNLSDQPYG TQSCHPDTHL AEILMKTLLR
960 970 980 990 1000
NLGFYTDQAF GELEKNSDKF LLGTSSSENS QPAHLHELLC SLQKQLLAFC
1010 1020 1030 1040 1050
HINNISENSS SVALLHKHLQ LLLPHATDIY SRSANLLKES PWNGSVGEKL
1060 1070 1080 1090 1100
RDVIYVSAAG SMLCQIVNSL LLLPVSVARP LLSYLLDLLP PLDCLNRLLP
1110 1120 1130 1140 1150
AADLLEDQEL QWPLHGGPEL IDPAGLPLPQ PAQSWVWLVD LERTIALLIG
1160 1170 1180 1190 1200
RCLGGMLQGS PVSPEEQDTA YWMKTPLFSD GVEMDTPQLD KCMSCLLEVA
1210 1220 1230 1240 1250
LSGNEEQKPF DYKLRPEIAV YVDLALGCSK EPARSLWISM QDYAVSKDWD
1260 1270 1280 1290 1300
SATLSNESLL DTVSRFVLAA LLKHTNLLSQ ACGESRYQPG KHLSEVYRCV
1310 1320 1330 1340 1350
YKVRSRLLAC KNLELIQTRS SSRDRWISEN QDSADVDPQE HSFTRTIDEE
1360 1370 1380 1390 1400
AEMEEQAERD REEGHPEPED EEEEREHEVM TAGKIFQCFL SAREVARSRD
1410 1420 1430 1440 1450
RDRMNSGAGS GARADDPPPQ SQQERRVSTD LPEGQDVYTA ACNSVIHRCA
1460 1470 1480 1490 1500
LLILGVSPVI DELQKRREEG QLQQPSTSAS EGGGLMTRSE SLTAESRLVH
1510 1520 1530 1540 1550
TSPNYRLIKS RSESDLSQPE SDEEGYALSG RRNVDLDLAA SHRKRGPMHS
1560 1570 1580 1590 1600
QLESLSDSWA RLKHSRDWLC NSSYSFESDF DLTKSLGVHT LIENVVSFVS
1610 1620 1630 1640 1650
GDVGNAPGFK EPEESMSTSP QASIIAMEQQ QLRAELRLEA LHQILVLLSG
1660 1670 1680 1690 1700
MEEKGSISLA GSRLSSGFQS STLLTSVRLQ FLAGCFGLGT VGHTGGKGES
1710 1720 1730 1740 1750
GRLHHYQDGI RAAKRNIQIE IQVAVHKIYQ QLSATLERAL QANKHHIEAQ
1760 1770 1780 1790 1800
QRLLLVTVFA LSVHYQPVDV SLAISTGLLN VLSQLCGTDT MLGQPLQLLP
1810 1820 1830 1840 1850
KTGVSQLSTA LKVASTRLLQ ILAITTGTYA DKLSPKVVQS LLDLLCSQLK
1860 1870 1880 1890 1900
NLLSQTGVLH MASFGEGEQE DGEEEEKKVD SSGETEKKDF RAALRKQHAA
1910 1920 1930 1940 1950
ELHLGDFLVF LRRVVSSKAI QSKMASPKWT EVLLNIASQK CSSGIPLVGN
1960 1970 1980 1990 2000
LRTRLLALHV LEAVLPACES GVEDDQMAQI VERLFSLLSD CMWETPIAQA
2010 2020 2030 2040 2050
KHAIQIKEKE QEIKLQKQGE LEEEDENLPI QEVSFDPEKA QCCLVENGQI
2060 2070 2080 2090 2100
LTHGSGGKGY GLASTGVTSG CYQWKFYIVK ENRGNEGTCV GVSRWPVHDF
2110 2120 2130 2140 2150
NHRTTSDMWL YRAYSGNLYH NGEQTLTLSS FTQGDFITCV LDMEARTISF
2160 2170 2180 2190 2200
GKNGEEPKLA FEDVDAAELY PCVMFYSSNP GEKVKICDMQ MRGTPRDLLP
2210 2220 2230 2240 2250
GDPICSPVAA VLAEATIQLI RILHRTDRWT YCINKKMMER LHKIKICIKE
2260 2270 2280 2290 2300
SGQKLKKSRS VQSREENEMR EEKESKEEEK GKHTRHGLAD LSELQLRTLC
2310 2320 2330 2340 2350
IEVWPVLAVI GGVDAGLRVG GRCVHKQTGR HATLLGVVKE GSTSAKVQWD
2360 2370 2380 2390 2400
EAEITISFPT FWSPSDTPLY NLEPCEPLPF DVARFRGLTA SVLLDLTYLT
2410 2420 2430 2440 2450
GVHEDMGKQS TKRHEKKHRH ESEEKGDVEQ KPESESALDM RTGLTSDDVK
2460 2470 2480 2490 2500
SQSTTSSKSE NEIASFSLDP TLPSVESQHQ ITEGKRKNHE HMSKNHDVAQ
2510 2520 2530 2540 2550
SEIRAVQLSY LYLGAMKSLS ALLGCSKYAE LLLIPKVLAE NGHNSDCASS
2560 2570 2580 2590 2600
PVVHEDVEMR AALQFLMRHM VKRAVMRSPI KRALGLADLE RAQAMIYKLV
2610 2620 2630 2640 2650
VHGLLEDQFG GKIKQEIDQQ AEESDPAQQA QTPVTTSPSA SSTTSFMSSS
2660 2670 2680 2690 2700
LEDTTTATTP VTDTETVPAS ESPGVMPLSL LRQMFSSYPT TTVLPTRRAQ
2710 2720 2730 2740 2750
TPPISSLPTS PSDEVGRRQS LTSPDSQSAR PANRTALSDP SSRLSTSPPP
2760 2770 2780 2790 2800
PAIAVPLLEM GFSLRQIAKA MEATGARGEA DAQNITVLAM WMIEHPGHED
2810 2820 2830 2840 2850
EEEPQSGSTA DSRPGAAVLG SGGKSNDPCY LQSPGDIPSA DAAEMEEGFS
2860 2870 2880 2890 2900
ESPDNLDHTE NAASGSGPSA RGRSAVTRRH KFDLAARTLL ARAAGLYRSV
2910 2920 2930 2940 2950
QAHRNQSRRE GISLQQDPGA LYDFNLDEEL EIDLDDEAME AMFGQDLTSD
2960 2970 2980 2990 3000
NDILGMWIPE VLDWPTWHVC ESEDREEVVV CELCECSVVS FNQHMKRNHP
3010 3020 3030 3040 3050
GCGRSANRQG YRSNGSYVDG WFGGECGSGN PYYLLCGTCR EKYLAMKTKS
3060 3070 3080 3090 3100
KSTSSERYKG QAPDLIGKQD SVYEEDWDML DVDEDEKLTG EEEFELLAGP
3110 3120 3130 3140 3150
LGLNDRRIVP EPVQFPDSDP LGASVAMVTA TNSMEETLMQ IGCHGSVEKS
3160 3170 3180 3190 3200
SSGRITLGEQ AAALANPHDR VVALRRVTAA AQVLLARTMV MRALSLLSVS
3210 3220 3230 3240 3250
GSSCSLAAGL ESLGLTDIRT LVRLMCLAAA GRAGLSTSPS AMASTSERSR
3260 3270 3280 3290 3300
GGHSKANKPI SCLAYLSTAV GCLASNAPSA AKLLVQLCTQ NLISAATGVN
3310 3320 3330 3340 3350
LTTVDDSIQR KFLPSFLRGI AEENKLVTSP NFVVTQALVA LLADKGAKLR
3360 3370 3380 3390 3400
PNYDKSEVEK KGPLELANAL AACCLSSRLS SQHRQWAAQQ LVRTLAAHDR
3410 3420 3430 3440 3450
DNQTTLQTLA DMGGDLRKCS FIKLEAHQNR VMTCVWCNKK GLLATSGNDG
3460 3470 3480 3490 3500
TIRVWNVTKK QYSLQQTCVF NRLEGDAEES LGSPSDPSFS PVSWSISGKY
3510 3520 3530 3540 3550
LAGALEKMVN IWQVNGGKGL VDIQPHWVSA LAWPEEGPAT AWSGESPELL
3560 3570 3580 3590 3600
LVGRMDGSLG LIEVVDVSTM HRRELEHCYR KDVSVTCIAW FSEDRPFAVG
3610 3620 3630 3640 3650
YFDGKLLLGT KEPLEKGGIV LIDAHKDTLI SMKWDPTGHI LMTCAKEDSV
3660 3670 3680 3690 3700
KLWGSISGCW CCLHSLCHPS IVNGIAWCRL PGKGSKLQLL MATGCQSGLV
3710 3720 3730 3740 3750
CVWRIPQDTT QTNVTSAEGW WEQESNCQDG YRKSSGAKCV YQLRGHITPV
3760 3770 3780 3790 3800
RTVAFSSDGL ALVSGGLGGL MNIWSLRDGS VLQTVVIGSG AIQTTVWIPE
3810 3820 3830 3840 3850
VGVAACSNRS KDVLVVNCTA EWAAANHVLA TCRTALKQQG VLGLNMAPCM
3860 3870 3880 3890 3900
RAFLERLPMM LQEQYAYEKP HVVCGDQLVH SPYMQCLASL AVGLHLDQLL
3910 3920 3930 3940 3950
CNPPVPPHHQ NCLPDPASWN PNEWAWLECF STTIKAAEAL TNGAQFPESF
3960 3970 3980 3990 4000
TVPDLEPVPE DELVFLMDNS KWINGMDEQI MSWATSRPED WHLGGKCDVY
4010 4020 4030 4040 4050
LWGAGRHGQL AEAGRNVMVP AAAPSFSQAQ QVICGQNCTF VIQANGTVLA
4060 4070 4080 4090 4100
CGEGSYGRLG QGNSDDLHVL TVISALQGFV VTQLVTSCGS DGHSMALTES
4110 4120 4130 4140 4150
GEVFSWGDGD YGKLGHGNSD RQRRPRQIEA LQGEEVVQMS CGFKHSAVVT
4160 4170 4180 4190 4200
SDGKLFTFGN GDYGRLGLGN TSNKKLPERV TALEGYQIGQ VACGLNHTLA
4210 4220 4230 4240 4250
VSADGSMVWA FGDGDYGKLG LGNSTAKSSP QKIDVLCGIG IKKVACGTQF
4260 4270 4280 4290 4300
SVALTKDGHV YTFGQDRLIG LPEGRARNHN RPQQIPVLAG VIIEDVAVGA
4310 4320 4330 4340 4350
EHTLALASNG DVYAWGSNSE GQLGLGHTNH VREPTLVTGL QGKNVRQISA
4360 4370 4380 4390 4400
GRCHSAAWTA PPVPPRAPGV SVPLQLGLPD TVPPQYGALR EVSIHTVRAR
4410 4420 4430 4440 4450
LRLLYHFSDL MYSSWRLLNL SPNNQNSTSH YNAGTWGIVQ GQLRPLLAPR
4460 4470 4480 4490 4500
VYTLPMVRSI GKTMVQGKNY GPQITVKRIS TRGRKCKPIF VQIARQVVKL
4510 4520 4530 4540 4550
NASDLRLPSR AWKVKLVGEG ADDAGGVFDD TITEMCQELE TGIVDLLIPS
4560 4570 4580 4590 4600
PNATAEVGYN RDRFLFNPSA CLDEHLMQFK FLGILMGVAI RTKKPLDLHL
4610 4620 4630 4640 4650
APLVWKQLCC VPLTLEDLEE VDLLYVQTLN SILHIEDSGI TEESFHEMIP
4660 4670 4680 4690 4700
LDSFVGQSAD GKMVPIIPGG NSIPLTFSNR KEYVERAIEY RLHEMDRQVA
4710 4720 4730 4740 4750
AVREGMSWIV PVPLLSLLTA KQLEQMVCGM PEISVEVLKK VVRYREVDEQ
4760 4770 4780 4790 4800
HQLVQWFWHT LEEFSNEERV LFMRFVSGRS RLPANTADIS QRFQIMKVDR
4810 4820 4830 4840 4850
PYDSLPTSQT CFFQLRLPPY SSQLVMAERL RYAINNCRSI DMDNYMLSRN
4860
VDNAEGSDTD Y
Length:4,861
Mass (Da):532,228
Last modified:May 18, 2010 - v2
Checksum:i31B2C1A1430B9622
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1532 – 15321R → Q in AAD12586 (PubMed:8861955).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1088 – 10881L → F.
Corresponds to variant rs1063423 [ dbSNP | Ensembl ].
VAR_042556
Natural varianti1278 – 12781L → F.
Corresponds to variant rs3764187 [ dbSNP | Ensembl ].
VAR_042557
Natural varianti1411 – 14111G → V.
Corresponds to variant rs36089909 [ dbSNP | Ensembl ].
VAR_042558
Natural varianti1447 – 14471H → N.
Corresponds to variant rs7162519 [ dbSNP | Ensembl ].
VAR_042559
Natural varianti1572 – 15721S → A.
Corresponds to variant rs16947363 [ dbSNP | Ensembl ].
VAR_042560
Natural varianti1696 – 16961G → A.1 Publication
Corresponds to variant rs2255243 [ dbSNP | Ensembl ].
VAR_042561
Natural varianti1995 – 19951T → A.
Corresponds to variant rs2228512 [ dbSNP | Ensembl ].
VAR_042562
Natural varianti2220 – 22201I → V.1 Publication
Corresponds to variant rs2228510 [ dbSNP | Ensembl ].
VAR_042563
Natural varianti2816 – 28161A → T.
Corresponds to variant rs35122568 [ dbSNP | Ensembl ].
VAR_042564
Natural varianti3152 – 31521S → F.
Corresponds to variant rs2228513 [ dbSNP | Ensembl ].
VAR_042565
Natural varianti3517 – 35171G → R.
Corresponds to variant rs7182782 [ dbSNP | Ensembl ].
VAR_042566
Natural varianti3722 – 37221E → D.1 Publication
Corresponds to variant rs2229749 [ dbSNP | Ensembl ].
VAR_042567
Natural varianti4394 – 43941I → V.
Corresponds to variant rs2228516 [ dbSNP | Ensembl ].
VAR_057122

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50078 mRNA. Translation: AAD12586.1.
AC073167 Genomic DNA. No translation available.
AC118274 Genomic DNA. No translation available.
BC040929 mRNA. Translation: AAH40929.1.
CCDSiCCDS45277.1.
PIRiS71752.
RefSeqiNP_003913.3. NM_003922.3.
UniGeneiHs.210385.

Genome annotation databases

EnsembliENST00000443617; ENSP00000390158; ENSG00000103657.
GeneIDi8925.
KEGGihsa:8925.
UCSCiuc002amp.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50078 mRNA. Translation: AAD12586.1.
AC073167 Genomic DNA. No translation available.
AC118274 Genomic DNA. No translation available.
BC040929 mRNA. Translation: AAH40929.1.
CCDSiCCDS45277.1.
PIRiS71752.
RefSeqiNP_003913.3. NM_003922.3.
UniGeneiHs.210385.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O2WX-ray2.00A/B/C/D3975-4360[»]
4QT6X-ray1.64A2035-2192[»]
ProteinModelPortaliQ15751.
SMRiQ15751. Positions 2035-2192, 3996-4360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114439. 27 interactions.
IntActiQ15751. 6 interactions.
MINTiMINT-8330052.
STRINGi9606.ENSP00000390158.

PTM databases

PhosphoSiteiQ15751.

Polymorphism and mutation databases

BioMutaiHERC1.
DMDMi296434522.

Proteomic databases

MaxQBiQ15751.
PaxDbiQ15751.
PRIDEiQ15751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000443617; ENSP00000390158; ENSG00000103657.
GeneIDi8925.
KEGGihsa:8925.
UCSCiuc002amp.3. human.

Organism-specific databases

CTDi8925.
GeneCardsiGC15M063900.
HGNCiHGNC:4867. HERC1.
HPAiHPA049749.
MIMi605109. gene.
neXtProtiNX_Q15751.
PharmGKBiPA29242.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00790000122949.
HOGENOMiHOG000168589.
HOVERGENiHBG053919.
InParanoidiQ15751.
KOiK10594.
OMAiHHYQDGI.
OrthoDBiEOG70KGNN.
PhylomeDBiQ15751.
TreeFamiTF106426.

Enzyme and pathway databases

UniPathwayiUPA00143.
SignaLinkiQ15751.

Miscellaneous databases

ChiTaRSiHERC1. human.
GeneWikiiHERC1.
GenomeRNAii8925.
NextBioi33556.
PROiQ15751.
SOURCEiSearch...

Gene expression databases

BgeeiQ15751.
CleanExiHS_HERC1.
ExpressionAtlasiQ15751. baseline and differential.
GenevisibleiQ15751. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
2.130.10.30. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR000569. HECT.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR003877. SPRY_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
PF00415. RCC1. 12 hits.
PF00622. SPRY. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SMARTiSM00119. HECTc. 1 hit.
SM00449. SPRY. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50978. SSF50978. 2 hits.
SSF50985. SSF50985. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50237. HECT. 1 hit.
PS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 14 hits.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins."
    Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.
    EMBO J. 15:4262-4273(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ARF1, VARIANTS ALA-1696; VAL-2220 AND ASP-3722.
  2. Erratum
    Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.
    EMBO J. 15:5738-5738(1996)
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 4211-4861.
    Tissue: Liver.
  5. "A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70."
    Rosa J.L., Barbacid M.
    Oncogene 15:1-6(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLTC.
  6. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PKM.
  7. "The giant protein HERC1 is recruited to aluminum fluoride-induced actin-rich surface protrusions in HeLa cells."
    Garcia-Gonzalo F.R., Munoz P., Gonzalez E., Casaroli-Marano R.P., Vilaro S., Bartrons R., Ventura F., Rosa J.L.
    FEBS Lett. 559:77-83(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated guanine nucleotide release from ARF proteins."
    Garcia-Gonzalo F.R., Bartrons R., Ventura F., Rosa J.L.
    FEBS Lett. 579:343-348(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARF6.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase."
    Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R., Rosa J.L., Guan K.-L.
    J. Biol. Chem. 281:8313-8316(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSC2.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1517; SER-1521; THR-2701; SER-2706 AND SER-2710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1521 AND THR-2701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-1406 AND SER-1512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHERC1_HUMAN
AccessioniPrimary (citable) accession number: Q15751
Secondary accession number(s): Q8IW65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 18, 2010
Last modified: July 22, 2015
This is version 133 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.