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Protein

Rho GTPase-activating protein 4

Gene

ARHGAP4

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

Functioni

Inhibitory effect on stress fiber organization. May down-regulate Rho-like GTPase in hematopoietic cells.

GO - Molecular functioni

  • GTPase activator activity Source: ProtInc
  • Rac GTPase binding Source: GO_Central
  • SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 4
Alternative name(s):
Rho-GAP hematopoietic protein C1
Rho-type GTPase-activating protein 4
p115
Gene namesi
Name:ARHGAP4
Synonyms:KIAA0131, RGC1, RHOGAP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:674. ARHGAP4.

Subcellular locationi

  • Cytoplasm

  • Note: Just below the plasma membrane.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24958.

Polymorphism and mutation databases

BioMutaiARHGAP4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 946946Rho GTPase-activating protein 4PRO_0000056701Add
BLAST

Proteomic databases

MaxQBiP98171.
PaxDbiP98171.
PRIDEiP98171.

PTM databases

PhosphoSiteiP98171.

Miscellaneous databases

PMAP-CutDBP98171.

Expressioni

Tissue specificityi

Predominantly in hematopoietic cells (spleen, thymus and leukocytes); low levels in placenta, lung and various fetal tissues.

Gene expression databases

BgeeiP98171.
CleanExiHS_ARHGAP4.
ExpressionAtlasiP98171. baseline and differential.
GenevestigatoriP98171.

Organism-specific databases

HPAiHPA001012.
HPA001083.

Interactioni

Protein-protein interaction databases

BioGridi106886. 4 interactions.
IntActiP98171. 3 interactions.
MINTiMINT-4717773.
STRINGi9606.ENSP00000203786.

Structurei

Secondary structure

1
946
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi749 – 7557Combined sources
Beta strandi772 – 7809Combined sources
Beta strandi783 – 7886Combined sources
Beta strandi791 – 80111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EPDNMR-A746-814[»]
ProteinModelPortaliP98171.
SMRiP98171. Positions 502-695, 751-814.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98171.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 317299F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini507 – 695189Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini746 – 80560SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili128 – 19568Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG264793.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiP98171.
OMAiWTQYTQR.
PhylomeDBiP98171.
TreeFamiTF315892.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P98171-1) [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
MAAHGKLRRE RGLQAEYETQ VKEMRWQLSE QLRCLELQGE LRRELLQELA
60 70 80 90 100
EFMRRRAEVE LEYSRGLEKL AERFSSRGGR LGSSREHQSF RKEPSLLSPL
110 120 130 140 150
HCWAVLLQHT RQQSRESAAL SEVLAGPLAQ RLSHIAEDVG RLVKKSRDLE
160 170 180 190 200
QQLQDELLEV VSELQTAKKT YQAYHMESVN AEAKLREAER QEEKRAGRSV
210 220 230 240 250
PTTTAGATEA GPLRKSSLKK GGRLVEKRQA KFMEHKLKCT KARNEYLLSL
260 270 280 290 300
ASVNAAVSNY YLHDVLDLMD CCDTGFHLAL GQVLRSYTAA ESRTQASQVQ
310 320 330 340 350
GLGSLEEAVE ALDPPGDKAK VLEVHATVFC PPLRFDYHPH DGDEVAEICV
360 370 380 390 400
EMELRDEILP RAQNIQSRLD RQTIETEEVN KTLKATLQAL LEVVASDDGD
410 420 430 440 450
VLDSFQTSPS TESLKSTSSD PGSRQAGRRR GQQQETETFY LTKLQEYLSG
460 470 480 490 500
RSILAKLQAK HEKLQEALQR GDKEEQEVSW TQYTQRKFQK SRQPRPSSQY
510 520 530 540 550
NQRLFGGDME KFIQSSGQPV PLVVESCIRF INLNGLQHEG IFRVSGAQLR
560 570 580 590 600
VSEIRDAFER GEDPLVEGCT AHDLDSVAGV LKLYFRSLEP PLFPPDLFGE
610 620 630 640 650
LLASSELEAT AERVEHVSRL LWRLPAPVLV VLRYLFTFLN HLAQYSDENM
660 670 680 690 700
MDPYNLAVCF GPTLLPVPAG QDPVALQGRV NQLVQTLIVQ PDRVFPPLTS
710 720 730 740 750
LPGPVYEKCM APPSASCLGD AQLESLGADN EPELEAEMPA QEDDLEGVVE
760 770 780 790 800
AVACFAYTGR TAQELSFRRG DVLRLHERAS SDWWRGEHNG MRGLIPHKYI
810 820 830 840 850
TLPAGTEKQV VGAGLQTAGE SGSSPEGLLA SELVHRPEPC TSPEAMGPSG
860 870 880 890 900
HRRRCLVPAS PEQHVEVDKA VAQNMDSVFK ELLGKTSVRQ GLGPASTTSP
910 920 930 940
SPGPRSPKAP PSSRLGRNKG FSRGPGAPAS PSASHPQGLD TTPKPH
Length:946
Mass (Da):105,026
Last modified:October 17, 2006 - v2
Checksum:iED3D48C5DAA24969
GO
Isoform 2 (identifier: P98171-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-227: K → KLWPPQRPVAASSCAPVCWLQAGFLVHPPWWGAMCAPSTHQ

Note: No experimental confirmation available.

Show »
Length:986
Mass (Da):109,393
Checksum:i7098B225673075FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti609 – 6091A → D in CAA55394 (PubMed:8570618).Curated
Sequence conflicti731 – 7311E → D in CAA55394 (PubMed:8570618).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041A → V.
Corresponds to variant rs5987182 [ dbSNP | Ensembl ].
VAR_028413

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei227 – 2271K → KLWPPQRPVAASSCAPVCWL QAGFLVHPPWWGAMCAPSTH Q in isoform 2. 1 PublicationVSP_042902

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78817 mRNA. Translation: CAA55394.1.
U52112 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72778.1.
BC052303 mRNA. Translation: AAH52303.1.
D50921 mRNA. Translation: BAA09480.1.
CCDSiCCDS14736.1. [P98171-1]
CCDS55540.1. [P98171-2]
PIRiI38100.
RefSeqiNP_001158213.1. NM_001164741.1. [P98171-2]
NP_001657.3. NM_001666.4. [P98171-1]
UniGeneiHs.701324.

Genome annotation databases

EnsembliENST00000350060; ENSP00000203786; ENSG00000089820. [P98171-1]
ENST00000370028; ENSP00000359045; ENSG00000089820. [P98171-2]
GeneIDi393.
KEGGihsa:393.
UCSCiuc004fjk.2. human. [P98171-1]
uc004fjl.2. human. [P98171-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78817 mRNA. Translation: CAA55394.1.
U52112 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72778.1.
BC052303 mRNA. Translation: AAH52303.1.
D50921 mRNA. Translation: BAA09480.1.
CCDSiCCDS14736.1. [P98171-1]
CCDS55540.1. [P98171-2]
PIRiI38100.
RefSeqiNP_001158213.1. NM_001164741.1. [P98171-2]
NP_001657.3. NM_001666.4. [P98171-1]
UniGeneiHs.701324.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EPDNMR-A746-814[»]
ProteinModelPortaliP98171.
SMRiP98171. Positions 502-695, 751-814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106886. 4 interactions.
IntActiP98171. 3 interactions.
MINTiMINT-4717773.
STRINGi9606.ENSP00000203786.

PTM databases

PhosphoSiteiP98171.

Polymorphism and mutation databases

BioMutaiARHGAP4.

Proteomic databases

MaxQBiP98171.
PaxDbiP98171.
PRIDEiP98171.

Protocols and materials databases

DNASUi393.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350060; ENSP00000203786; ENSG00000089820. [P98171-1]
ENST00000370028; ENSP00000359045; ENSG00000089820. [P98171-2]
GeneIDi393.
KEGGihsa:393.
UCSCiuc004fjk.2. human. [P98171-1]
uc004fjl.2. human. [P98171-2]

Organism-specific databases

CTDi393.
GeneCardsiGC0XM153172.
HGNCiHGNC:674. ARHGAP4.
HPAiHPA001012.
HPA001083.
MIMi300023. gene.
neXtProtiNX_P98171.
PharmGKBiPA24958.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264793.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiP98171.
OMAiWTQYTQR.
PhylomeDBiP98171.
TreeFamiTF315892.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiARHGAP4. human.
EvolutionaryTraceiP98171.
GeneWikiiARHGAP4.
GenomeRNAii393.
NextBioi1639.
PMAP-CutDBP98171.
PROiP98171.
SOURCEiSearch...

Gene expression databases

BgeeiP98171.
CleanExiHS_ARHGAP4.
ExpressionAtlasiP98171. baseline and differential.
GenevestigatoriP98171.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An X chromosome-linked gene encoding a protein with characteristics of a rhoGAP predominantly expressed in hematopoietic cells."
    Tribioli C., Droetto S., Bione S., Cesareni G., Torrisi M.R., Lotti L.V., Lanfrancone L., Toniolo D., Pelicci P.-G.
    Proc. Natl. Acad. Sci. U.S.A. 93:695-699(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Embryo.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] (ISOFORM 2).
    Tissue: Pancreas.
  5. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-946 (ISOFORM 1).
    Tissue: Bone marrow.
  6. "Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae."
    Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C., Torri G., Toniolo D.
    Hum. Mol. Genet. 3:1061-1068(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM 1).
    Tissue: Embryo.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Solution structure of SH3 domain in Rho-GTPase-activating protein 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 746-814.

Entry informationi

Entry nameiRHG04_HUMAN
AccessioniPrimary (citable) accession number: P98171
Secondary accession number(s): Q14144, Q86UY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 147 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 X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.