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Protein

Gem-associated protein 5

Gene

GEMIN5

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

Functioni

Required for the assembly of the SMN complex that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:16857593, PubMed:18984161, PubMed:20513430). Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (PubMed:18984161). GEMIN5 acts as the snRNA-binding protein of the SMN complex (PubMed:11714716, PubMed:16857593, PubMed:19377484, PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600, PubMed:27881601). Binds to the 7-methylguanosine cap of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref. 25). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (PubMed:27507887).12 Publications

GO - Molecular functioni

GO - Biological processi

  • import into nucleus Source: Reactome
  • mRNA splicing, via spliceosome Source: UniProtKB
  • protein-containing complex assembly Source: UniProtKB
  • regulation of translation Source: UniProtKB
  • spliceosomal snRNP assembly Source: UniProtKB
  • translation Source: UniProtKB-KW

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, mRNA splicing, Protein biosynthesis, Translation regulation

Enzyme and pathway databases

ReactomeiR-HSA-191859 snRNP Assembly
SignaLinkiQ8TEQ6
SIGNORiQ8TEQ6

Names & Taxonomyi

Protein namesi
Recommended name:
Gem-associated protein 5
Short name:
Gemin5
Gene namesi
Name:GEMIN5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000082516.8
HGNCiHGNC:20043 GEMIN5
MIMi607005 gene
neXtProtiNX_Q8TEQ6

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14W → A: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes. 4 Publications1
Mutagenesisi15Y → A: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes. 4 Publications1
Mutagenesisi33R → A: Abolishes interaction with U4 snRNA. 1 Publication1
Mutagenesisi197E → A: Abolishes interaction with U4 snRNA. 1 Publication1
Mutagenesisi271 – 273KRR → AAA: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex. 1 Publication3
Mutagenesisi286W → A: Abolishes interaction with U4 snRNA. Abolishes interaction with the 7-methylguanosine cap of RNA molecules. No effect on interaction with SMN complex. 2 Publications1
Mutagenesisi290H → A: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex. 1 Publication1
Mutagenesisi335R → E: Abolishes interaction with U4 snRNA. 1 Publication1
Mutagenesisi359R → A: Abolishes interaction with U4 snRNA. 1 Publication1
Mutagenesisi381F → A: Strongly decreases interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. Abolishes interaction with 80S ribosomes. 3 Publications1
Mutagenesisi381F → D: Abolishes interaction with U4 snRNA. 1 Publication1
Mutagenesisi422W → E: Abolishes interaction with U4 snRNA. 1 Publication1
Mutagenesisi474Y → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 2 Publications1
Mutagenesisi641K → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 2 Publications1
Mutagenesisi660Y → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 1 Publication1
Mutagenesisi684R → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000082516
PharmGKBiPA134945791

Polymorphism and mutation databases

BioMutaiGEMIN5
DMDMi296439335

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000510041 – 1508Gem-associated protein 5Add BLAST1508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48PhosphoserineCombined sources1
Modified residuei51PhosphothreonineCombined sources1
Modified residuei624PhosphoserineCombined sources1
Modified residuei751PhosphothreonineCombined sources1
Cross-linki754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei757PhosphoserineCombined sources1
Modified residuei770PhosphoserineCombined sources1
Modified residuei778PhosphoserineCombined sources1
Modified residuei847PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8TEQ6
MaxQBiQ8TEQ6
PaxDbiQ8TEQ6
PeptideAtlasiQ8TEQ6
PRIDEiQ8TEQ6
ProteomicsDBi74478

PTM databases

iPTMnetiQ8TEQ6
PhosphoSitePlusiQ8TEQ6

Expressioni

Gene expression databases

BgeeiENSG00000082516 Expressed in 183 organ(s), highest expression level in oocyte
CleanExiHS_GEMIN5
GenevisibleiQ8TEQ6 HS

Organism-specific databases

HPAiHPA037392
HPA037393

Interactioni

Subunit structurei

Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:20513430, PubMed:27507887). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:11714716, PubMed:20513430). Interacts directly with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE (PubMed:11714716). Identified in a SMN complex that contains GEMIN2/SIP1 (PubMed:19377484). Interacts with cytosolic DDX20/GEMIN3 and GEMIN4 (PubMed:19750007, PubMed:27507887). Interacts with SNRNP70 and HNRNPU (PubMed:27507887). Identified in a complex with 80S ribosomes; binds to the 60S large ribosomal subunit (PubMed:27507887). Interacts with the ribosomal subunits RPL3 and RPL4 (PubMed:27507887).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei33Interaction with U4 snRNACombined sources3 Publications1
Sitei284Interaction with U4 snRNACombined sources2 Publications1
Sitei335Interaction with U4 snRNACombined sources2 Publications1
Sitei359Interaction with U4 snRNACombined sources3 Publications1
Sitei381Interaction with U4 snRNACombined sources3 Publications1
Sitei422Interaction with U4 snRNACombined sources2 Publications1
Sitei426Interaction with U4 snRNACombined sources1 Publication1
Sitei470Interaction with U4 snRNACombined sources1 Publication1
Sitei474Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources3 Publications1
Sitei556Interaction with U4 snRNACombined sources1 Publication1
Sitei579Interaction with U4 snRNACombined sources1 Publication1
Sitei641Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources3 Publications1
Sitei660Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources3 Publications1
Sitei684Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources3 Publications1

Binary interactionsi

Protein-protein interaction databases

BioGridi117429, 87 interactors
CORUMiQ8TEQ6
ELMiQ8TEQ6
IntActiQ8TEQ6, 46 interactors
MINTiQ8TEQ6
STRINGi9606.ENSP00000285873

Structurei

Secondary structure

11508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8TEQ6
SMRiQ8TEQ6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati62 – 104WD 1Add BLAST43
Repeati107 – 148WD 2Add BLAST42
Repeati150 – 189WD 3Add BLAST40
Repeati193 – 264WD 4Add BLAST72
Repeati280 – 321WD 5Add BLAST42
Repeati333 – 374WD 6Add BLAST42
Repeati377 – 417WD 7Add BLAST41
Repeati424 – 464WD 8Add BLAST41
Repeati468 – 509WD 9Add BLAST42
Repeati533 – 573WD 10Add BLAST41
Repeati576 – 622WD 11Add BLAST47
Repeati637 – 677WD 12Add BLAST41
Repeati680 – 720WD 13Add BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 124Important for interaction with U1 snRNA1 PublicationAdd BLAST124
Regioni13 – 15Interaction with U4 snRNACombined sources3 Publications3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1362 – 1393Sequence analysisAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi738 – 746Poly-Lys9

Domaini

The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA (PubMed:19377484, PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601). The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref. 25). The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially (PubMed:27834343, PubMed:27881600, PubMed:27881601). Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit (PubMed:27507887).7 Publications

Sequence similaritiesi

Belongs to the WD repeat gemin-5 family.Curated

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiENOG410IJDN Eukaryota
ENOG410XTH3 LUCA
GeneTreeiENSGT00620000088064
HOGENOMiHOG000231391
HOVERGENiHBG051721
InParanoidiQ8TEQ6
KOiK13133
OMAiAKQLCFQ
OrthoDBiEOG091G03O1
PhylomeDBiQ8TEQ6
TreeFamiTF328886

Family and domain databases

Gene3Di2.130.10.10, 2 hits
InterProiView protein in InterPro
IPR024977 Apc4_WD40_dom
IPR020472 G-protein_beta_WD-40_rep
IPR011047 Quinoprotein_ADH-like_supfam
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PfamiView protein in Pfam
PF12894 ANAPC4_WD40, 2 hits
PF00400 WD40, 3 hits
PRINTSiPR00320 GPROTEINBRPT
SMARTiView protein in SMART
SM00320 WD40, 12 hits
SUPFAMiSSF50978 SSF50978, 2 hits
SSF50998 SSF50998, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 3 hits
PS50082 WD_REPEATS_2, 3 hits
PS50294 WD_REPEATS_REGION, 1 hit

Sequencei

Sequence statusi: Complete.

Q8TEQ6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQEPRTLPP SPNWYCARCS DAVPGGLFGF AARTSVFLVR VGPGAGESPG
60 70 80 90 100
TPPFRVIGEL VGHTERVSGF TFSHHPGQYN LCATSSDDGT VKIWDVETKT
110 120 130 140 150
VVTEHALHQH TISTLHWSPR VKDLIVSGDE KGVVFCYWFN RNDSQHLFIE
160 170 180 190 200
PRTIFCLTCS PHHEDLVAIG YKDGIVVIID ISKKGEVIHR LRGHDDEIHS
210 220 230 240 250
IAWCPLPGED CLSINQEETS EEAEITNGNA VAQAPVTKGC YLATGSKDQT
260 270 280 290 300
IRIWSCSRGR GVMILKLPFL KRRGGGIDPT VKERLWLTLH WPSNQPTQLV
310 320 330 340 350
SSCFGGELLQ WDLTQSWRRK YTLFSASSEG QNHSRIVFNL CPLQTEDDKQ
360 370 380 390 400
LLLSTSMDRD VKCWDIATLE CSWTLPSLGG FAYSLAFSSV DIGSLAIGVG
410 420 430 440 450
DGMIRVWNTL SIKNNYDVKN FWQGVKSKVT ALCWHPTKEG CLAFGTDDGK
460 470 480 490 500
VGLYDTYSNK PPQISSTYHK KTVYTLAWGP PVPPMSLGGE GDRPSLALYS
510 520 530 540 550
CGGEGIVLQH NPWKLSGEAF DINKLIRDTN SIKYKLPVHT EISWKADGKI
560 570 580 590 600
MALGNEDGSI EIFQIPNLKL ICTIQQHHKL VNTISWHHEH GSQPELSYLM
610 620 630 640 650
ASGSNNAVIY VHNLKTVIES SPESPVTITE PYRTLSGHTA KITSVAWSPH
660 670 680 690 700
HDGRLVSASY DGTAQVWDAL REEPLCNFRG HRGRLLCVAW SPLDPDCIYS
710 720 730 740 750
GADDFCVHKW LTSMQDHSRP PQGKKSIELE KKRLSQPKAK PKKKKKPTLR
760 770 780 790 800
TPVKLESIDG NEEESMKENS GPVENGVSDQ EGEEQAREPE LPCGLAPAVS
810 820 830 840 850
REPVICTPVS SGFEKSKVTI NNKVILLKKE PPKEKPETLI KKRKARSLLP
860 870 880 890 900
LSTSLDHRSK EELHQDCLVL ATAKHSRELN EDVSADVEER FHLGLFTDRA
910 920 930 940 950
TLYRMIDIEG KGHLENGHPE LFHQLMLWKG DLKGVLQTAA ERGELTDNLV
960 970 980 990 1000
AMAPAAGYHV WLWAVEAFAK QLCFQDQYVK AASHLLSIHK VYEAVELLKS
1010 1020 1030 1040 1050
NHFYREAIAI AKARLRPEDP VLKDLYLSWG TVLERDGHYA VAAKCYLGAT
1060 1070 1080 1090 1100
CAYDAAKVLA KKGDAASLRT AAELAAIVGE DELSASLALR CAQELLLANN
1110 1120 1130 1140 1150
WVGAQEALQL HESLQGQRLV FCLLELLSRH LEEKQLSEGK SSSSYHTWNT
1160 1170 1180 1190 1200
GTEGPFVERV TAVWKSIFSL DTPEQYQEAF QKLQNIKYPS ATNNTPAKQL
1210 1220 1230 1240 1250
LLHICHDLTL AVLSQQMASW DEAVQALLRA VVRSYDSGSF TIMQEVYSAF
1260 1270 1280 1290 1300
LPDGCDHLRD KLGDHQSPAT PAFKSLEAFF LYGRLYEFWW SLSRPCPNSS
1310 1320 1330 1340 1350
VWVRAGHRTL SVEPSQQLDT ASTEETDPET SQPEPNRPSE LDLRLTEEGE
1360 1370 1380 1390 1400
RMLSTFKELF SEKHASLQNS QRTVAEVQET LAEMIRQHQK SQLCKSTANG
1410 1420 1430 1440 1450
PDKNEPEVEA EQPLCSSQSQ CKEEKNEPLS LPELTKRLTE ANQRMAKFPE
1460 1470 1480 1490 1500
SIKAWPFPDV LECCLVLLLI RSHFPGCLAQ EMQQQAQELL QKYGNTKTYR

RHCQTFCM
Length:1,508
Mass (Da):168,589
Last modified:May 18, 2010 - v3
Checksum:iEA5293F395BBF14E
GO

Sequence cautioni

The sequence BAB84892 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti299L → P in BAB14222 (PubMed:14702039).Curated1
Sequence conflicti456T → A in BAB14222 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033807682R → Q5 PublicationsCorresponds to variant dbSNP:rs1974777Ensembl.1
Natural variantiVAR_0576041155P → S. Corresponds to variant dbSNP:rs6865950Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY063750 mRNA Translation: AAL38980.1
AK074066 mRNA Translation: BAB84892.2 Different initiation.
AC008421 Genomic DNA No translation available.
BC008776 mRNA Translation: AAH08776.2
BC014147 mRNA Translation: AAH14147.2
BC113614 mRNA Translation: AAI13615.1
AK022748 mRNA Translation: BAB14222.1
AL117665 mRNA Translation: CAB56035.2
CCDSiCCDS4330.1
PIRiT17345
RefSeqiNP_001239085.1, NM_001252156.1
NP_056280.2, NM_015465.4
UniGeneiHs.483921

Genome annotation databases

EnsembliENST00000285873; ENSP00000285873; ENSG00000082516
GeneIDi25929
KEGGihsa:25929
UCSCiuc003lvx.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY063750 mRNA Translation: AAL38980.1
AK074066 mRNA Translation: BAB84892.2 Different initiation.
AC008421 Genomic DNA No translation available.
BC008776 mRNA Translation: AAH08776.2
BC014147 mRNA Translation: AAH14147.2
BC113614 mRNA Translation: AAI13615.1
AK022748 mRNA Translation: BAB14222.1
AL117665 mRNA Translation: CAB56035.2
CCDSiCCDS4330.1
PIRiT17345
RefSeqiNP_001239085.1, NM_001252156.1
NP_056280.2, NM_015465.4
UniGeneiHs.483921

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GXHX-ray1.80A1-739[»]
5GXIX-ray1.85A1-739[»]
5H1JX-ray2.00A1-726[»]
5H1KX-ray1.90A/B1-726[»]
5H1LX-ray2.10A1-726[»]
5H1MX-ray2.49A1-726[»]
5H3SX-ray3.00A/B1-740[»]
5H3TX-ray2.57A/B/C/D1-740[»]
5H3UX-ray2.50A/B1-740[»]
5TEEX-ray1.65A1-739[»]
5TEFX-ray1.95A1-739[»]
5THAX-ray1.80A1-739[»]
ProteinModelPortaliQ8TEQ6
SMRiQ8TEQ6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117429, 87 interactors
CORUMiQ8TEQ6
ELMiQ8TEQ6
IntActiQ8TEQ6, 46 interactors
MINTiQ8TEQ6
STRINGi9606.ENSP00000285873

PTM databases

iPTMnetiQ8TEQ6
PhosphoSitePlusiQ8TEQ6

Polymorphism and mutation databases

BioMutaiGEMIN5
DMDMi296439335

Proteomic databases

EPDiQ8TEQ6
MaxQBiQ8TEQ6
PaxDbiQ8TEQ6
PeptideAtlasiQ8TEQ6
PRIDEiQ8TEQ6
ProteomicsDBi74478

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285873; ENSP00000285873; ENSG00000082516
GeneIDi25929
KEGGihsa:25929
UCSCiuc003lvx.4 human

Organism-specific databases

CTDi25929
EuPathDBiHostDB:ENSG00000082516.8
GeneCardsiGEMIN5
H-InvDBiHIX0005347
HGNCiHGNC:20043 GEMIN5
HPAiHPA037392
HPA037393
MIMi607005 gene
neXtProtiNX_Q8TEQ6
OpenTargetsiENSG00000082516
PharmGKBiPA134945791
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJDN Eukaryota
ENOG410XTH3 LUCA
GeneTreeiENSGT00620000088064
HOGENOMiHOG000231391
HOVERGENiHBG051721
InParanoidiQ8TEQ6
KOiK13133
OMAiAKQLCFQ
OrthoDBiEOG091G03O1
PhylomeDBiQ8TEQ6
TreeFamiTF328886

Enzyme and pathway databases

ReactomeiR-HSA-191859 snRNP Assembly
SignaLinkiQ8TEQ6
SIGNORiQ8TEQ6

Miscellaneous databases

ChiTaRSiGEMIN5 human
GeneWikiiGEMIN5
GenomeRNAii25929
PROiPR:Q8TEQ6
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000082516 Expressed in 183 organ(s), highest expression level in oocyte
CleanExiHS_GEMIN5
GenevisibleiQ8TEQ6 HS

Family and domain databases

Gene3Di2.130.10.10, 2 hits
InterProiView protein in InterPro
IPR024977 Apc4_WD40_dom
IPR020472 G-protein_beta_WD-40_rep
IPR011047 Quinoprotein_ADH-like_supfam
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PfamiView protein in Pfam
PF12894 ANAPC4_WD40, 2 hits
PF00400 WD40, 3 hits
PRINTSiPR00320 GPROTEINBRPT
SMARTiView protein in SMART
SM00320 WD40, 12 hits
SUPFAMiSSF50978 SSF50978, 2 hits
SSF50998 SSF50998, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 3 hits
PS50082 WD_REPEATS_2, 3 hits
PS50294 WD_REPEATS_REGION, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGEMI5_HUMAN
AccessioniPrimary (citable) accession number: Q8TEQ6
Secondary accession number(s): Q14CV0
, Q8WWV4, Q969W4, Q9H9K3, Q9UFI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 18, 2010
Last modified: October 10, 2018
This is version 164 of the entry and version 3 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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