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Protein

Oligophrenin-1

Gene

OPHN1

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

Functioni

Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at presynaptic terminals. Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation (By similarity).By similarity

GO - Molecular functioni

  • GTPase activator activity Source: ProtInc
  • phospholipid binding Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Endocytosis, Neurogenesis

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Oligophrenin-1
Gene namesi
Name:OPHN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8148. OPHN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, OPHN1-related (MRXSO)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSO patients manifest mental retardation associated with cerebellar hypoplasia and distinctive facial dysmorphism.
See also OMIM:300486
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991P → PEFSLLMNGLKIFIKCL in MRXSO. 1 Publication
VAR_066746

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiOPHN1.
MIMi300486. phenotype.
Orphaneti137831. X-linked intellectual disability - cerebellar hypoplasia.
PharmGKBiPA31934.

Polymorphism and mutation databases

BioMutaiOPHN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802Oligophrenin-1PRO_0000056760Add
BLAST

Proteomic databases

MaxQBiO60890.
PaxDbiO60890.
PRIDEiO60890.

PTM databases

iPTMnetiO60890.
PhosphoSiteiO60890.
SwissPalmiO60890.

Expressioni

Tissue specificityi

Expressed in brain.

Gene expression databases

BgeeiO60890.
CleanExiHS_OPHN1.

Organism-specific databases

HPAiHPA002919.

Interactioni

Subunit structurei

Interacts with HOMER1. Interacts with AMPA receptor complexes. Interacts with SH3GL2 (endophilin-A1) (By similarity). Interacts (via C-terminus) with NR1D1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi111029. 5 interactions.
IntActiO60890. 1 interaction.
STRINGi9606.ENSP00000347710.

Structurei

3D structure databases

ProteinModelPortaliO60890.
SMRiO60890. Positions 6-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini265 – 368104PHPROSITE-ProRule annotationAdd
BLAST
Domaini380 – 564185Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi629 – 761133Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1451. Eukaryota.
ENOG410YJPS. LUCA.
GeneTreeiENSGT00840000129684.
HOGENOMiHOG000018767.
HOVERGENiHBG067993.
InParanoidiO60890.
OMAiNVCEHSR.
OrthoDBiEOG71VSS5.
PhylomeDBiO60890.
TreeFamiTF316851.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 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: O60890-1) [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
MGHPPLEFSD CYLDSPDFRE RLKCYEQELE RTNKFIKDVI KDGNALISAM
60 70 80 90 100
RNYSSAVQKF SQTLQSFQFD FIGDTLTDDE INIAESFKEF AELLNEVENE
110 120 130 140 150
RMMMVHNASD LLIKPLENFR KEQIGFTKER KKKFEKDGER FYSLLDRHLH
160 170 180 190 200
LSSKKKESQL QEADLQVDKE RHNFFESSLD YVYQIQEVQE SKKFNIVEPV
210 220 230 240 250
LAFLHSLFIS NSLTVELTQD FLPYKQQLQL SLQNTRNHFS STREEMEELK
260 270 280 290 300
KRMKEAPQTC KLPGQPTIEG YLYTQEKWAL GISWVKYYCQ YEKETKTLTM
310 320 330 340 350
TPMEQKPGAK QGPLDLTLKY CVRRKTESID KRFCFDIETN ERPGTITLQA
360 370 380 390 400
LSEANRRLWM EAMDGKEPIY HSPITKQQEM ELNEVGFKFV RKCINIIETK
410 420 430 440 450
GIKTEGLYRT VGSNIQVQKL LNAFFDPKCP GDVDFHNSDW DIKTITSSLK
460 470 480 490 500
FYLRNLSEPV MTYRLHKELV SAAKSDNLDY RLGAIHSLVY KLPEKNREML
510 520 530 540 550
ELLIRHLVNV CEHSKENLMT PSNMGVIFGP TLMRAQEDTV AAMMNIKFQN
560 570 580 590 600
IVVEILIEHF GKIYLGPPEE SAAPPVPPPR VTARRHKPIT ISKRLLRERT
610 620 630 640 650
VFYTSSLDES EDEIQHQTPN GTITSSIEPP KPPQHPKLPI QRSGETDPGR
660 670 680 690 700
KSPSRPILDG KLEPCPEVDV GKLVSRLQDG GTKITPKATN GPMPGSGPTK
710 720 730 740 750
TPSFHIKRPA PRPLAHHKEG DADSFSKVRP PGEKPTIIRP PVRPPDPPCR
760 770 780 790 800
AATPQKPEPK PDIVAGNAGE ITSSVVASRT RFFETASRKT GSSQGRLPGD

ES
Length:802
Mass (Da):91,641
Last modified:August 1, 1998 - v1
Checksum:iA24D150048071608
GO
Isoform 2 (identifier: O60890-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: WALGISWVKYYCQYEKETKTLTMTPMEQKPGAKQ → CVWGHRGIHWVSISQELLPLVGCEFWAPLLFIDP
     312-802: Missing.

Note: No experimental confirmation available.
Show »
Length:311
Mass (Da):36,673
Checksum:i48A3897FB3B8BDCB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391V → I.1 Publication
Corresponds to variant rs41303733 [ dbSNP | Ensembl ].
VAR_061184
Natural varianti45 – 451A → T.1 Publication
VAR_013638
Natural varianti199 – 1991P → PEFSLLMNGLKIFIKCL in MRXSO. 1 Publication
VAR_066746
Natural varianti301 – 3011T → M.1 Publication
Corresponds to variant rs138108344 [ dbSNP | Ensembl ].
VAR_013639
Natural varianti693 – 6931M → I.
Corresponds to variant rs36095561 [ dbSNP | Ensembl ].
VAR_033452

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 31134WALGI…PGAKQ → CVWGHRGIHWVSISQELLPL VGCEFWAPLLFIDP in isoform 2. 1 PublicationVSP_055336Add
BLAST
Alternative sequencei312 – 802491Missing in isoform 2. 1 PublicationVSP_055337Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001189 mRNA. Translation: CAA04579.1.
AJ248245
, AJ248246, AJ248247, AJ248248, AJ248249, AJ248250, AJ248251, AJ248252, AJ248253, AJ248254, AJ248255, AJ248256, AJ248257, AJ248258, AJ248259, AJ248260, AJ248261, AJ248262, AJ248263, AJ248264, AJ248265, AJ248266, AJ248267 Genomic DNA. Translation: CAB96181.1.
AB102656 mRNA. Translation: BAC81125.1.
AL157700
, AL158201, AL672138, Z82203 Genomic DNA. Translation: CAD18899.2.
AL158201
, AL157700, AL672138, Z82203 Genomic DNA. Translation: CAI40982.1.
AL672138
, AL157700, AL158201, Z82203 Genomic DNA. Translation: CAI41508.1.
Z82203
, AL157700, AL158201, AL672138 Genomic DNA. Translation: CAI42695.1.
BC059393 mRNA. Translation: AAH59393.1.
BC140763 mRNA. Translation: AAI40764.1.
CCDSiCCDS14388.1. [O60890-1]
PIRiH59434.
RefSeqiNP_002538.1. NM_002547.2. [O60890-1]
XP_011529263.1. XM_011530961.1. [O60890-1]
UniGeneiHs.128824.

Genome annotation databases

EnsembliENST00000355520; ENSP00000347710; ENSG00000079482. [O60890-1]
GeneIDi4983.
KEGGihsa:4983.
UCSCiuc004dww.5. human. [O60890-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001189 mRNA. Translation: CAA04579.1.
AJ248245
, AJ248246, AJ248247, AJ248248, AJ248249, AJ248250, AJ248251, AJ248252, AJ248253, AJ248254, AJ248255, AJ248256, AJ248257, AJ248258, AJ248259, AJ248260, AJ248261, AJ248262, AJ248263, AJ248264, AJ248265, AJ248266, AJ248267 Genomic DNA. Translation: CAB96181.1.
AB102656 mRNA. Translation: BAC81125.1.
AL157700
, AL158201, AL672138, Z82203 Genomic DNA. Translation: CAD18899.2.
AL158201
, AL157700, AL672138, Z82203 Genomic DNA. Translation: CAI40982.1.
AL672138
, AL157700, AL158201, Z82203 Genomic DNA. Translation: CAI41508.1.
Z82203
, AL157700, AL158201, AL672138 Genomic DNA. Translation: CAI42695.1.
BC059393 mRNA. Translation: AAH59393.1.
BC140763 mRNA. Translation: AAI40764.1.
CCDSiCCDS14388.1. [O60890-1]
PIRiH59434.
RefSeqiNP_002538.1. NM_002547.2. [O60890-1]
XP_011529263.1. XM_011530961.1. [O60890-1]
UniGeneiHs.128824.

3D structure databases

ProteinModelPortaliO60890.
SMRiO60890. Positions 6-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111029. 5 interactions.
IntActiO60890. 1 interaction.
STRINGi9606.ENSP00000347710.

PTM databases

iPTMnetiO60890.
PhosphoSiteiO60890.
SwissPalmiO60890.

Polymorphism and mutation databases

BioMutaiOPHN1.

Proteomic databases

MaxQBiO60890.
PaxDbiO60890.
PRIDEiO60890.

Protocols and materials databases

DNASUi4983.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355520; ENSP00000347710; ENSG00000079482. [O60890-1]
GeneIDi4983.
KEGGihsa:4983.
UCSCiuc004dww.5. human. [O60890-1]

Organism-specific databases

CTDi4983.
GeneCardsiOPHN1.
HGNCiHGNC:8148. OPHN1.
HPAiHPA002919.
MalaCardsiOPHN1.
MIMi300127. gene.
300486. phenotype.
neXtProtiNX_O60890.
Orphaneti137831. X-linked intellectual disability - cerebellar hypoplasia.
PharmGKBiPA31934.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1451. Eukaryota.
ENOG410YJPS. LUCA.
GeneTreeiENSGT00840000129684.
HOGENOMiHOG000018767.
HOVERGENiHBG067993.
InParanoidiO60890.
OMAiNVCEHSR.
OrthoDBiEOG71VSS5.
PhylomeDBiO60890.
TreeFamiTF316851.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiOPHN1. human.
GeneWikiiOPHN1.
GenomeRNAii4983.
NextBioi19186.
PROiO60890.
SOURCEiSearch...

Gene expression databases

BgeeiO60890.
CleanExiHS_OPHN1.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MRXSO.
    Tissue: Fetal brain.
  2. "Deletion including the oligophrenin-1 gene associated with enlarged cerebral ventricles, cerebellar hypoplasia, seizures and ataxia."
    Tentler D., Gustavsson P., Leisti J., Schueler M., Chelly J., Timonen E., Anneren G., Willard H.F., Dahl N.
    Eur. J. Hum. Genet. 7:541-548(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN MRXSO.
  3. "Determination of the gene structure of human oligophrenin-1 and identification of three novel polymorphisms by screening of DNA from 164 patients with non-specific X-linked mental retardation."
    Billuart P., Chelly J., Carrie A., Vinet M.C., Couvert P., McDonell N., Zemni R., Kahn A., Moraine C., Beldjord C., Bienvenu T.
    Ann. Genet. 43:5-9(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-45 AND MET-301.
  4. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
    Kitano T., Schwarz C., Nickel B., Paeaebo S.
    Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "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].
  6. "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] (ISOFORMS 1 AND 2), VARIANT ILE-39.
    Tissue: Lung and Placenta.
  7. "Insertion of 16 amino acids in the BAR domain of the oligophrenin 1 protein causes mental retardation and cerebellar hypoplasia in an Italian family."
    Pirozzi F., Di Raimo F.R., Zanni G., Bertini E., Billuart P., Tartaglione T., Tabolacci E., Brancaccio A., Neri G., Chiurazzi P.
    Hum. Mutat. 32:E2294-E2307(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MRXSO GLU-PHE-SER-LEU-LEU-MET-ASN-GLY-LEU-LYS-ILE-PHE-ILE-LYS-CYS-LEU-199 INS.

Entry informationi

Entry nameiOPHN1_HUMAN
AccessioniPrimary (citable) accession number: O60890
Secondary accession number(s): B9EIP8
, Q5JQ81, Q6PCC1, Q8WX47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 132 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

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. 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.