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Protein

Ras-related protein Rab-6B

Gene

RAB6B

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

Functioni

Seems to have a role in retrograde membrane traffic at the level of the Golgi complex. May function in retrograde transport in neuronal cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451GTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 278GTP
Nucleotide bindingi68 – 725GTP
Nucleotide bindingi126 – 1294GTP

GO - Molecular functioni

  1. GDP binding Source: GO_Central
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: GO_Central
  4. myosin V binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: GO_Central
  2. intra-Golgi vesicle-mediated transport Source: GO_Central
  3. metabolic process Source: GOC
  4. Rab protein signal transduction Source: GO_Central
  5. retrograde transport, endosome to Golgi Source: GO_Central
  6. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-6B
Gene namesi
Name:RAB6B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:14902. RAB6B.

Subcellular locationi

Golgi apparatus membrane; Lipid-anchor. Cytoplasmic vesicle
Note: Colocalizes with BICD1 at vesicular structures that align along microtubules.

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  2. Golgi apparatus Source: UniProtKB
  3. Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271T → N: Loss of APBA1-binding. 1 Publication
Mutagenesisi72 – 721Q → L: Interacts with APBA1. 1 Publication

Organism-specific databases

PharmGKBiPA34147.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 208207Ras-related protein Rab-6BPRO_0000121115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei82 – 821O-AMP-tyrosine; by Legionella DrrA1 Publication
Lipidationi206 – 2061S-geranylgeranyl cysteineBy similarity
Modified residuei208 – 2081Cysteine methyl esterBy similarity
Lipidationi208 – 2081S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ9NRW1.
PaxDbiQ9NRW1.
PRIDEiQ9NRW1.

PTM databases

PhosphoSiteiQ9NRW1.

Expressioni

Tissue specificityi

Predominantly expressed in brain.

Gene expression databases

BgeeiQ9NRW1.
ExpressionAtlasiQ9NRW1. baseline and differential.
GenevestigatoriQ9NRW1.

Organism-specific databases

HPAiCAB017713.
HPA059131.

Interactioni

Subunit structurei

Interacts with CCDC64/BICDR1; leads to its accumulation in the pericentrosomal region (By similarity). Interacts with RAB6KIFL. Interacts (GTP-bound) with BICD1 (via C-terminus); the interaction is direct. Interacts (GDP-bound) with DYNLRB1. Interacts (GTP-bound) with APBA1/MINT1 isoform 2, also called Mint1_826, but not with isoform 1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APBA1Q02410-24EBI-1760079,EBI-9247455

Protein-protein interaction databases

BioGridi119610. 12 interactions.
IntActiQ9NRW1. 3 interactions.
STRINGi9606.ENSP00000285208.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 195Combined sources
Helixi26 – 3510Combined sources
Beta strandi47 – 5711Combined sources
Beta strandi60 – 6910Combined sources
Helixi73 – 786Combined sources
Helixi79 – 846Combined sources
Beta strandi87 – 948Combined sources
Helixi98 – 1025Combined sources
Helixi104 – 11512Combined sources
Beta strandi118 – 1269Combined sources
Helixi131 – 1333Combined sources
Helixi138 – 14710Combined sources
Beta strandi151 – 1544Combined sources
Turni157 – 1593Combined sources
Helixi163 – 17412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9SX-ray1.78A/B/C13-174[»]
2FE4X-ray2.30A13-174[»]
2FFQX-ray1.78A13-174[»]
ProteinModelPortaliQ9NRW1.
SMRiQ9NRW1. Positions 13-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRW1.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 509Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00730000110423.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9NRW1.
KOiK07894.
OMAiFQATIGI.
OrthoDBiEOG77DJ7M.
PhylomeDBiQ9NRW1.
TreeFamiTF300803.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRW1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF
60 70 80 90 100
LSKTMYLEDR TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS
110 120 130 140 150
FQQTSKWIDD VRTERGSDVI IMLVGNKTDL ADKRQITIEE GEQRAKELSV
160 170 180 190 200
MFIETSAKTG YNVKQLFRRV ASALPGMENV QEKSKEGMID IKLDKPQEPP

ASEGGCSC
Length:208
Mass (Da):23,462
Last modified:October 1, 2000 - v1
Checksum:iE81C831996E2446D
GO
Isoform 2 (identifier: Q9NRW1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MSAGGDFGNPLRKFKLVFLGEQSV → MWHMTRNWPLV

Note: No experimental confirmation available.

Show »
Length:195
Mass (Da):22,334
Checksum:iE772D44D7E9D2C2C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424MSAGG…GEQSV → MWHMTRNWPLV in isoform 2. 1 PublicationVSP_055831Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF166492 mRNA. Translation: AAF61637.1.
AF498940 mRNA. Translation: AAM21088.1.
BT007263 mRNA. Translation: AAP35927.1.
AK295451 mRNA. Translation: BAH12073.1.
AK312378 mRNA. Translation: BAG35296.1.
AC080128 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79158.1.
CH471052 Genomic DNA. Translation: EAW79159.1.
BC002510 mRNA. Translation: AAH02510.1.
U66623 mRNA. Translation: AAC51198.1.
CCDSiCCDS3082.1. [Q9NRW1-1]
RefSeqiNP_057661.3. NM_016577.3. [Q9NRW1-1]
UniGeneiHs.715344.

Genome annotation databases

EnsembliENST00000285208; ENSP00000285208; ENSG00000154917. [Q9NRW1-1]
ENST00000486858; ENSP00000419381; ENSG00000154917. [Q9NRW1-2]
ENST00000543906; ENSP00000437797; ENSG00000154917. [Q9NRW1-1]
GeneIDi51560.
KEGGihsa:51560.
UCSCiuc003epy.3. human. [Q9NRW1-1]

Polymorphism databases

DMDMi13633595.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF166492 mRNA. Translation: AAF61637.1.
AF498940 mRNA. Translation: AAM21088.1.
BT007263 mRNA. Translation: AAP35927.1.
AK295451 mRNA. Translation: BAH12073.1.
AK312378 mRNA. Translation: BAG35296.1.
AC080128 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79158.1.
CH471052 Genomic DNA. Translation: EAW79159.1.
BC002510 mRNA. Translation: AAH02510.1.
U66623 mRNA. Translation: AAC51198.1.
CCDSiCCDS3082.1. [Q9NRW1-1]
RefSeqiNP_057661.3. NM_016577.3. [Q9NRW1-1]
UniGeneiHs.715344.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9SX-ray1.78A/B/C13-174[»]
2FE4X-ray2.30A13-174[»]
2FFQX-ray1.78A13-174[»]
ProteinModelPortaliQ9NRW1.
SMRiQ9NRW1. Positions 13-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119610. 12 interactions.
IntActiQ9NRW1. 3 interactions.
STRINGi9606.ENSP00000285208.

PTM databases

PhosphoSiteiQ9NRW1.

Polymorphism databases

DMDMi13633595.

Proteomic databases

MaxQBiQ9NRW1.
PaxDbiQ9NRW1.
PRIDEiQ9NRW1.

Protocols and materials databases

DNASUi51560.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285208; ENSP00000285208; ENSG00000154917. [Q9NRW1-1]
ENST00000486858; ENSP00000419381; ENSG00000154917. [Q9NRW1-2]
ENST00000543906; ENSP00000437797; ENSG00000154917. [Q9NRW1-1]
GeneIDi51560.
KEGGihsa:51560.
UCSCiuc003epy.3. human. [Q9NRW1-1]

Organism-specific databases

CTDi51560.
GeneCardsiGC03M133543.
HGNCiHGNC:14902. RAB6B.
HPAiCAB017713.
HPA059131.
MIMi615852. gene.
neXtProtiNX_Q9NRW1.
PharmGKBiPA34147.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00730000110423.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9NRW1.
KOiK07894.
OMAiFQATIGI.
OrthoDBiEOG77DJ7M.
PhylomeDBiQ9NRW1.
TreeFamiTF300803.

Miscellaneous databases

ChiTaRSiRAB6B. human.
EvolutionaryTraceiQ9NRW1.
GeneWikiiRAB6B.
GenomeRNAii51560.
NextBioi35479141.
PROiQ9NRW1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRW1.
ExpressionAtlasiQ9NRW1. baseline and differential.
GenevestigatoriQ9NRW1.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus."
    Opdam F.J.M., Echard A., Croes H.J.E., van den Hurk J.A.J.M., van de Vorstenbosch R.A., Ginsel L.A., Goud B., Fransen J.A.M.
    J. Cell Sci. 113:2725-2735(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Amygdala and Hippocampus.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  8. "RAB GTPases expressed in human melanoma cells."
    Chen D., Guo J., Gahl W.A.
    Biochim. Biophys. Acta 1355:1-6(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-124 (ISOFORM 1/2).
  9. Cited for: FUNCTION, INTERACTION WITH BICD1, SUBCELLULAR LOCATION.
  10. "Rab6 family proteins interact with the dynein light chain protein DYNLRB1."
    Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B., King S.M., Fransen J.
    Cell Motil. Cytoskeleton 65:183-196(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DYNLRB1, SUBCELLULAR LOCATION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Modulation of Rab GTPase function by a protein phosphocholine transferase."
    Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
    Nature 477:103-106(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: AMPYLATION AT TYR-82.
  13. Cited for: INTERACTION WITH APBA1, MUTAGENESIS OF THR-27 AND GLN-72.
  14. "The structure of human neuronal Rab6B in the active and inactive form."
    Garcia-Saez I., Tcherniuk S., Kozielski F.
    Acta Crystallogr. D 62:725-733(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 13-174.

Entry informationi

Entry nameiRAB6B_HUMAN
AccessioniPrimary (citable) accession number: Q9NRW1
Secondary accession number(s): B2R5Z9
, B7Z337, D3DND3, Q92929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 147 of the entry and version 1 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.