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Protein

RalBP1-associated Eps domain-containing protein 2

Gene

REPS2

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

Functioni

Involved in growth factor signaling through its influence on the Ral signaling pathway.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi328 – 33912PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: ProtInc

GO - Biological processi

  • epidermal growth factor receptor signaling pathway Source: ProtInc
  • protein complex assembly Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RalBP1-associated Eps domain-containing protein 2
Alternative name(s):
Partner of RalBP1
RalBP1-interacting protein 2
Gene namesi
Name:REPS2
Synonyms:POB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9963. REPS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34330.

Polymorphism and mutation databases

BioMutaiREPS2.
DMDMi34098575.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660RalBP1-associated Eps domain-containing protein 2PRO_0000073831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei254 – 2541PhosphoserineCombined sources
Modified residuei479 – 4791PhosphothreonineCombined sources
Modified residuei493 – 4931PhosphoserineCombined sources

Post-translational modificationi

EGF stimulates phosphorylation on Tyr-residues and induces complex formation with EGF receptor through an adapter protein such as GRB2.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NFH8.
MaxQBiQ8NFH8.
PaxDbiQ8NFH8.
PRIDEiQ8NFH8.

PTM databases

iPTMnetiQ8NFH8.
PhosphoSiteiQ8NFH8.

Expressioni

Tissue specificityi

Expressed at high levels in the cerebrum, cerebellum, lung, kidney, and testis. Weakly expressed in the kidney. Relatively highly expressed in androgen-dependent as compared to androgen-independent prostate cancer cell lines and xenografts. Isoform 2 is down-regulated during progression of prostate cancer.

Gene expression databases

BgeeiQ8NFH8.
CleanExiHS_REPS2.
GenevisibleiQ8NFH8. HS.

Organism-specific databases

HPAiHPA000565.
HPA026073.

Interactioni

Subunit structurei

Interacts with ASAP1 and this complex can bind paxillin. May form a ternary complex with RALBP1 and ASAP1 (By similarity). Interacts with RALBP1 and GRB2. Binding to RALBP1 does not affect the Ral-binding activity of the latter. It can form a ternary complex with activated Ral and RALBP1. Binds EPN1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BIN1O004996EBI-8029141,EBI-719094
Eps15P4256710EBI-7067016,EBI-443923From a different organism.
GRB2P629938EBI-8029141,EBI-401755
SFNP319472EBI-8029141,EBI-476295
YWHAZP631042EBI-8029141,EBI-347088

Protein-protein interaction databases

BioGridi114622. 21 interactions.
IntActiQ8NFH8. 18 interactions.
MINTiMINT-110628.
STRINGi9606.ENSP00000349824.

Structurei

Secondary structure

1
660
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi279 – 2824Combined sources
Helixi283 – 29311Combined sources
Beta strandi296 – 3027Combined sources
Helixi303 – 3097Combined sources
Beta strandi312 – 3143Combined sources
Helixi320 – 3278Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi333 – 3364Combined sources
Helixi337 – 35216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IQ3NMR-A265-367[»]
ProteinModelPortaliQ8NFH8.
SMRiQ8NFH8. Positions 265-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NFH8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 147114EH 1PROSITE-ProRule annotationAdd
BLAST
Domaini282 – 37392EH 2PROSITE-ProRule annotationAdd
BLAST
Domaini315 – 35036EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni514 – 660147Interaction with RALBP1Add
BLAST
Regioni561 – 660100Interaction with ASAP1By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili601 – 65757Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 7674Ala-richAdd
BLAST
Compositional biasi477 – 52448Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 EH domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1955. Eukaryota.
ENOG410XTBP. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000231382.
HOVERGENiHBG056372.
InParanoidiQ8NFH8.
OMAiRPENQAT.
OrthoDBiEOG7B31MB.
PhylomeDBiQ8NFH8.
TreeFamiTF316546.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
[Graphical view]
PfamiPF12763. EF-hand_4. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NFH8-1) [UniParc]FASTAAdd to basket

Also known as: REPS2a, Long

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
MEAAAAAAAA AAAAAAAGGG CGSGPPPLLL SEGEQQCYSE LFARCAGAAG
60 70 80 90 100
GGPGSGPPEA ARVAPGTATA AAGPVADLFR ASQLPAETLH QITELCGAKR
110 120 130 140 150
VGYFGPTQFY IALKLIAAAQ SGLPVRIESI KCELPLPRFM MSKNDGEIRF
160 170 180 190 200
GNPAELHGTK VQIPYLTTEK NSFKRMDDED KQQETQSPTM SPLASPPSSP
210 220 230 240 250
PHYQRVPLSH GYSKLRSSAE QMHPAPYEAR QPLVQPEGSS SGGPGTKPLR
260 270 280 290 300
HQASLIRSFS VERELQDNSS YPDEPWRITE EQREYYVNQF RSLQPDPSSF
310 320 330 340 350
ISGSVAKNFF TKSKLSIPEL SYIWELSDAD CDGALTLPEF CAAFHLIVAR
360 370 380 390 400
KNGYPLPEGL PPTLQPEYLQ AAFPKPKWDC QLFDSYSESL PANQQPRDLN
410 420 430 440 450
RMEKTSVKDM ADLPVPNQDV TSDDKQALKS TINEALPKDV SEDPATPKDS
460 470 480 490 500
NSLKARPRSR SYSSTSIEEA MKRGEDPPTP PPRPQKTHSR ASSLDLNKVF
510 520 530 540 550
QPSVPATKSG LLPPPPALPP RPCPSQSEQV SEAELLPQLS RAPSQAAESS
560 570 580 590 600
PAKKDVLYSQ PPSKPIRRKF RPENQATENQ EPSTAASGPA SAATMKPHPT
610 620 630 640 650
VQKQSSKQKK AIQTAIRKNK EANAVLARLN SELQQQLKEV HQERIALENQ
660
LEQLRPVTVL
Length:660
Mass (Da):71,534
Last modified:August 15, 2003 - v2
Checksum:iAACB3B8B8A9C2E3A
GO
Isoform 2 (identifier: Q8NFH8-2) [UniParc]FASTAAdd to basket

Also known as: REPS2b, Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Show »
Length:521
Mass (Da):57,902
Checksum:iF5FCF51B56961026
GO
Isoform 3 (identifier: Q8NFH8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.
     182-182: Missing.

Show »
Length:520
Mass (Da):57,774
Checksum:iC5B4F557D58A444D
GO
Isoform 4 (identifier: Q8NFH8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     182-182: Missing.

Show »
Length:659
Mass (Da):71,405
Checksum:i527A658BDFB4582B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti321 – 3211S → C.1 Publication
VAR_069419

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 139139Missing in isoform 2 and isoform 3. 2 PublicationsVSP_007958Add
BLAST
Alternative sequencei182 – 1821Missing in isoform 3 and isoform 4. 1 PublicationVSP_040086

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010233 mRNA. Translation: AAC02901.1.
AF511533 mRNA. Translation: AAM43933.1.
AF512951 mRNA. Translation: AAM43953.1.
AL732371, AL929302 Genomic DNA. Translation: CAI40017.1.
AL929302, AL732371 Genomic DNA. Translation: CAI41286.1.
AL929302, AL732371 Genomic DNA. Translation: CAO03550.1.
AL732371, AL929302 Genomic DNA. Translation: CAO03570.1.
CCDSiCCDS14180.2. [Q8NFH8-1]
CCDS43919.1. [Q8NFH8-4]
RefSeqiNP_001074444.1. NM_001080975.1. [Q8NFH8-4]
NP_004717.2. NM_004726.2. [Q8NFH8-1]
UniGeneiHs.186810.

Genome annotation databases

EnsembliENST00000303843; ENSP00000306033; ENSG00000169891. [Q8NFH8-4]
ENST00000357277; ENSP00000349824; ENSG00000169891. [Q8NFH8-1]
GeneIDi9185.
KEGGihsa:9185.
UCSCiuc004cxv.1. human. [Q8NFH8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010233 mRNA. Translation: AAC02901.1.
AF511533 mRNA. Translation: AAM43933.1.
AF512951 mRNA. Translation: AAM43953.1.
AL732371, AL929302 Genomic DNA. Translation: CAI40017.1.
AL929302, AL732371 Genomic DNA. Translation: CAI41286.1.
AL929302, AL732371 Genomic DNA. Translation: CAO03550.1.
AL732371, AL929302 Genomic DNA. Translation: CAO03570.1.
CCDSiCCDS14180.2. [Q8NFH8-1]
CCDS43919.1. [Q8NFH8-4]
RefSeqiNP_001074444.1. NM_001080975.1. [Q8NFH8-4]
NP_004717.2. NM_004726.2. [Q8NFH8-1]
UniGeneiHs.186810.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IQ3NMR-A265-367[»]
ProteinModelPortaliQ8NFH8.
SMRiQ8NFH8. Positions 265-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114622. 21 interactions.
IntActiQ8NFH8. 18 interactions.
MINTiMINT-110628.
STRINGi9606.ENSP00000349824.

PTM databases

iPTMnetiQ8NFH8.
PhosphoSiteiQ8NFH8.

Polymorphism and mutation databases

BioMutaiREPS2.
DMDMi34098575.

Proteomic databases

EPDiQ8NFH8.
MaxQBiQ8NFH8.
PaxDbiQ8NFH8.
PRIDEiQ8NFH8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303843; ENSP00000306033; ENSG00000169891. [Q8NFH8-4]
ENST00000357277; ENSP00000349824; ENSG00000169891. [Q8NFH8-1]
GeneIDi9185.
KEGGihsa:9185.
UCSCiuc004cxv.1. human. [Q8NFH8-1]

Organism-specific databases

CTDi9185.
GeneCardsiREPS2.
HGNCiHGNC:9963. REPS2.
HPAiHPA000565.
HPA026073.
MIMi300317. gene.
neXtProtiNX_Q8NFH8.
PharmGKBiPA34330.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1955. Eukaryota.
ENOG410XTBP. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000231382.
HOVERGENiHBG056372.
InParanoidiQ8NFH8.
OMAiRPENQAT.
OrthoDBiEOG7B31MB.
PhylomeDBiQ8NFH8.
TreeFamiTF316546.

Miscellaneous databases

ChiTaRSiREPS2. human.
EvolutionaryTraceiQ8NFH8.
GeneWikiiREPS2.
GenomeRNAii9185.
NextBioi34439.
PROiQ8NFH8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NFH8.
CleanExiHS_REPS2.
GenevisibleiQ8NFH8. HS.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
[Graphical view]
PfamiPF12763. EF-hand_4. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral."
    Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.
    J. Biol. Chem. 273:814-821(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
    Tissue: Brain.
  2. "REPS2/POB1 is downregulated during human prostate cancer progression and inhibits growth factor signalling in prostate cancer cells."
    Oosterhoff J.K., Penninkhof F., Brinkmann A.O., Anton Grootegoed J., Blok L.J.
    Oncogene 22:2920-2925(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    Tissue: Hypothalamus.
  3. "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].
  4. "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis."
    Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A., Kikuchi A.
    Oncogene 18:5915-5922(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPN1.
  5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-479 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)."
    Koshiba S., Kigawa T., Iwahara J., Kikuchi A., Yokoyama S.
    FEBS Lett. 442:138-142(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 265-367.
  7. Cited for: VARIANT CYS-321.

Entry informationi

Entry nameiREPS2_HUMAN
AccessioniPrimary (citable) accession number: Q8NFH8
Secondary accession number(s): A6PWZ6
, O43428, Q5JNZ8, Q8NFI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: May 11, 2016
This is version 131 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

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.