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Protein

Interferon-inducible GTPase 1

Gene

Iigp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase with low activity. Has higher affinity for GDP than for GTP. Plays a role in resistance to intracellular pathogens. Required for disruption of the parasitophorous vacuole formed following T.gondii infection and subsequent killing of the parasite. Mediates resistance to C.trachomatis infection by targeting bacterial inclusions to autophagosomes for subsequent lysosomal destruction.4 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 848GTP1 Publication
Nucleotide bindingi102 – 1065GTP1 Publication
Nucleotide bindingi184 – 1863GTP1 Publication
Nucleotide bindingi231 – 2333GTP1 Publication

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • identical protein binding Source: MGI

GO - Biological processi

  • cellular response to interferon-beta Source: MGI
  • cytokine-mediated signaling pathway Source: MGI
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to protozoan Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • regulation of autophagy Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon-inducible GTPase 1 (EC:3.6.5.-)
Gene namesi
Name:Iigp1
Synonyms:Irga6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1926259. Iigp1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • nuclear membrane Source: UniProtKB-SubCell
  • symbiont-containing vacuole membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Protein is detected exclusively in the aqueous phase. 1 Publication
Mutagenesisi82 – 821K → A: Constitutively active. Binds GTP but fails to hydrolyze it. Does not localize to the parasitophorous vacuole membrane following T.gondii infection. 2 Publications
Mutagenesisi83 – 831S → N: Abrogates interaction with HOOK3. Greatly reduces binding affinity for GDP and GTP. Abolishes GTP-dependent oligomer formation. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 413412Interferon-inducible GTPase 1PRO_0000223527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineCurated

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

EPDiQ9QZ85.
PaxDbiQ9QZ85.
PRIDEiQ9QZ85.

PTM databases

iPTMnetiQ9QZ85.
PhosphoSiteiQ9QZ85.

Expressioni

Inductioni

Up-regulated by IFNG, IFNA1 and lipopolysaccharide (LPS) within 20 hours. Transiently up-regulated during the early stages of infection by Listeria monocytogenes. After 6 days expression is back to basal levels.2 Publications

Gene expression databases

BgeeiQ9QZ85.
CleanExiMM_IIGP1.
ExpressionAtlasiQ9QZ85. baseline and differential.
GenevisibleiQ9QZ85. MM.

Interactioni

Subunit structurei

Monomer, as apoenzyme and in the GDP-bound form. Homooligomer, upon GTP binding. Interacts with HOOK3.3 Publications

GO - Molecular functioni

  • identical protein binding Source: MGI

Protein-protein interaction databases

BioGridi208563. 2 interactions.
DIPiDIP-58958N.
IntActiQ9QZ85. 4 interactions.
MINTiMINT-1857405.
STRINGi10090.ENSMUSP00000032473.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2510Combined sources
Helixi29 – 313Combined sources
Helixi36 – 4712Combined sources
Helixi51 – 6616Combined sources
Beta strandi70 – 756Combined sources
Helixi82 – 909Combined sources
Beta strandi94 – 963Combined sources
Helixi104 – 1085Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi122 – 1265Combined sources
Helixi130 – 1323Combined sources
Helixi137 – 1437Combined sources
Helixi146 – 1483Combined sources
Beta strandi150 – 15910Combined sources
Helixi162 – 17312Combined sources
Beta strandi179 – 1835Combined sources
Helixi185 – 19511Combined sources
Turni197 – 1993Combined sources
Helixi202 – 21918Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi227 – 2293Combined sources
Turni233 – 2364Combined sources
Beta strandi237 – 2393Combined sources
Helixi240 – 24910Combined sources
Helixi253 – 2553Combined sources
Helixi256 – 2627Combined sources
Helixi268 – 28821Combined sources
Beta strandi292 – 2943Combined sources
Helixi296 – 2983Combined sources
Helixi303 – 31917Combined sources
Helixi324 – 33310Combined sources
Helixi338 – 3425Combined sources
Helixi347 – 3493Combined sources
Beta strandi355 – 3573Combined sources
Helixi359 – 37416Combined sources
Beta strandi377 – 3793Combined sources
Helixi386 – 40924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TPZX-ray2.00A/B1-411[»]
1TQ2X-ray2.70A/B1-411[»]
1TQ4X-ray1.95A1-413[»]
1TQ6X-ray2.70A1-413[»]
1TQDX-ray2.30A/B1-413[»]
4LV5X-ray1.70B1-413[»]
4LV8X-ray1.72B1-413[»]
5FPHX-ray3.20A/B/C/D/E/F/G1-413[»]
ProteinModelPortaliQ9QZ85.
SMRiQ9QZ85. Positions 14-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZ85.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 250183IRG-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410J4GH. Eukaryota.
ENOG41125KF. LUCA.
GeneTreeiENSGT00390000014733.
HOGENOMiHOG000220822.
HOVERGENiHBG054304.
InParanoidiQ9QZ85.
OMAiVELNIAI.
OrthoDBiEOG779NX6.
PhylomeDBiQ9QZ85.
TreeFamiTF331897.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030385. G_IRG_dom.
IPR007743. Immunity-related_GTPase-like.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05049. IIGP. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51716. G_IRG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QZ85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQLFSSPKS DENNDLPSSF TGYFKKFNTG RKIISQEILN LIELRMRKGN
60 70 80 90 100
IQLTNSAISD ALKEIDSSVL NVAVTGETGS GKSSFINTLR GIGNEEEGAA
110 120 130 140 150
KTGVVEVTME RHPYKHPNIP NVVFWDLPGI GSTNFPPNTY LEKMKFYEYD
160 170 180 190 200
FFIIISATRF KKNDIDIAKA ISMMKKEFYF VRTKVDSDIT NEADGKPQTF
210 220 230 240 250
DKEKVLQDIR LNCVNTFREN GIAEPPIFLL SNKNVCHYDF PVLMDKLISD
260 270 280 290 300
LPIYKRHNFM VSLPNITDSV IEKKRQFLKQ RIWLEGFAAD LVNIIPSLTF
310 320 330 340 350
LLDSDLETLK KSMKFYRTVF GVDETSLQRL ARDWEIEVDQ VEAMIKSPAV
360 370 380 390 400
FKPTDEETIQ ERLSRYIQEF CLANGYLLPK NSFLKEIFYL KYYFLDMVTE
410
DAKTLLKEIC LRN
Length:413
Mass (Da):47,572
Last modified:February 21, 2006 - v2
Checksum:i44B5A95FCA58A37A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381N → D in AAF07195 (PubMed:11907101).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007971 mRNA. Translation: CAA07798.1.
AF194871 mRNA. Translation: AAF07195.1.
AK153060 mRNA. Translation: BAE31686.1.
CT010300 mRNA. Translation: CAJ18508.1.
BC004649 mRNA. Translation: AAH04649.1.
CCDSiCCDS29270.1.
RefSeqiNP_001139747.1. NM_001146275.1.
NP_068564.4. NM_021792.4.
XP_011245278.1. XM_011246976.1.
XP_011245279.1. XM_011246977.1.
XP_011245280.1. XM_011246978.1.
XP_011245281.1. XM_011246979.1.
XP_011245282.1. XM_011246980.1.
UniGeneiMm.261140.

Genome annotation databases

EnsembliENSMUST00000032473; ENSMUSP00000032473; ENSMUSG00000054072.
ENSMUST00000066912; ENSMUSP00000063390; ENSMUSG00000054072.
GeneIDi60440.
KEGGimmu:60440.
UCSCiuc008fac.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007971 mRNA. Translation: CAA07798.1.
AF194871 mRNA. Translation: AAF07195.1.
AK153060 mRNA. Translation: BAE31686.1.
CT010300 mRNA. Translation: CAJ18508.1.
BC004649 mRNA. Translation: AAH04649.1.
CCDSiCCDS29270.1.
RefSeqiNP_001139747.1. NM_001146275.1.
NP_068564.4. NM_021792.4.
XP_011245278.1. XM_011246976.1.
XP_011245279.1. XM_011246977.1.
XP_011245280.1. XM_011246978.1.
XP_011245281.1. XM_011246979.1.
XP_011245282.1. XM_011246980.1.
UniGeneiMm.261140.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TPZX-ray2.00A/B1-411[»]
1TQ2X-ray2.70A/B1-411[»]
1TQ4X-ray1.95A1-413[»]
1TQ6X-ray2.70A1-413[»]
1TQDX-ray2.30A/B1-413[»]
4LV5X-ray1.70B1-413[»]
4LV8X-ray1.72B1-413[»]
5FPHX-ray3.20A/B/C/D/E/F/G1-413[»]
ProteinModelPortaliQ9QZ85.
SMRiQ9QZ85. Positions 14-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208563. 2 interactions.
DIPiDIP-58958N.
IntActiQ9QZ85. 4 interactions.
MINTiMINT-1857405.
STRINGi10090.ENSMUSP00000032473.

PTM databases

iPTMnetiQ9QZ85.
PhosphoSiteiQ9QZ85.

Proteomic databases

EPDiQ9QZ85.
PaxDbiQ9QZ85.
PRIDEiQ9QZ85.

Protocols and materials databases

DNASUi60440.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032473; ENSMUSP00000032473; ENSMUSG00000054072.
ENSMUST00000066912; ENSMUSP00000063390; ENSMUSG00000054072.
GeneIDi60440.
KEGGimmu:60440.
UCSCiuc008fac.2. mouse.

Organism-specific databases

CTDi60440.
MGIiMGI:1926259. Iigp1.

Phylogenomic databases

eggNOGiENOG410J4GH. Eukaryota.
ENOG41125KF. LUCA.
GeneTreeiENSGT00390000014733.
HOGENOMiHOG000220822.
HOVERGENiHBG054304.
InParanoidiQ9QZ85.
OMAiVELNIAI.
OrthoDBiEOG779NX6.
PhylomeDBiQ9QZ85.
TreeFamiTF331897.

Miscellaneous databases

EvolutionaryTraceiQ9QZ85.
NextBioi314867.
PROiQ9QZ85.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZ85.
CleanExiMM_IIGP1.
ExpressionAtlasiQ9QZ85. baseline and differential.
GenevisibleiQ9QZ85. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030385. G_IRG_dom.
IPR007743. Immunity-related_GTPase-like.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05049. IIGP. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51716. G_IRG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two families of GTPases dominate the complex cellular response to IFN-gamma."
    Boehm U., Guethlein L., Klamp T., Ozbek K., Schaub A., Fuetterer A., Pfeffer K., Howard J.C.
    J. Immunol. 161:6715-6723(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: C57BL/6J.
    Tissue: Embryonic fibroblast and Macrophage.
  2. "The IFN-inducible Golgi- and endoplasmic reticulum- associated 47-kDa GTPase IIGP is transiently expressed during listeriosis."
    Zerrahn J., Schaible U.E., Brinkmann V., Guhlich U., Kaufmann S.H.E.
    J. Immunol. 168:3428-3436(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Splenocyte.
  3. "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].
    Strain: C57BL/6J.
  4. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. "IIGP, a member of the IFN inducible and microbial defense mediating 47 kDa GTPase family, interacts with the microtubule binding protein hook3."
    Kaiser F., Kaufmann S.H.E., Zerrahn J.
    J. Cell Sci. 117:1747-1756(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOOK3, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-83.
  7. "Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced by phagocytosis."
    Martens S., Sabel K., Lange R., Uthaiah R., Wolf E., Howard J.C.
    J. Immunol. 173:2594-2606(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROBABLE MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
    Strain: C57BL/6J.
  8. "Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases."
    Martens S., Parvanova I., Zerrahn J., Griffiths G., Schell G., Reichmann G., Howard J.C.
    PLoS Pathog. 1:E24-E24(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82.
    Strain: C57BL/6J.
  9. "Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii."
    Hunn J.P., Koenen-Waisman S., Papic N., Schroeder N., Pawlowski N., Lange R., Kaiser F., Zerrahn J., Martens S., Howard J.C.
    EMBO J. 27:2495-2509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82 AND SER-83.
    Strain: C57BL/6J.
  10. "Inactive and active states of the interferon-inducible resistance GTPase, Irga6, in vivo."
    Papic N., Hunn J.P., Pawlowski N., Zerrahn J., Howard J.C.
    J. Biol. Chem. 283:32143-32151(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  11. "IFN-gamma-inducible Irga6 mediates host resistance against Chlamydia trachomatis via autophagy."
    Al-Zeer M.A., Al-Younes H.M., Braun P.R., Zerrahn J., Meyer T.F.
    PLoS ONE 4:E4588-E4588(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Spleen.
  13. "IIGP1, an interferon-gamma-inducible 47-kDa GTPase of the mouse, showing cooperative enzymatic activity and GTP-dependent multimerization."
    Uthaiah R.C., Praefcke G.J.K., Howard J.C., Herrmann C.
    J. Biol. Chem. 278:29336-29343(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-411 IN COMPLEX WITH GTP, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiIIGP1_MOUSE
AccessioniPrimary (citable) accession number: Q9QZ85
Secondary accession number(s): Q9Z1M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: February 21, 2006
Last modified: May 11, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.