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Protein

Myotubularin-related protein 2

Gene

MTMR2

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

Functioni

Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate.3 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.2 Publications
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.1 Publication

Enzyme regulationi

Interaction with SBF1 increases phosphatase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei417Phosphocysteine intermediate1
Binding sitei463Substrate1

GO - Molecular functioni

  • phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
  • phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  • protein tyrosine/serine/threonine phosphatase activity Source: UniProtKB
  • protein tyrosine phosphatase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087053-MONOMER.
BRENDAi3.1.3.64. 2681.
3.1.3.95. 2681.
ReactomeiR-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.

Chemistry databases

SwissLipidsiSLP:000001135.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 2
Alternative name(s):
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.951 Publication)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.642 Publications)
Gene namesi
Name:MTMR2
Synonyms:KIAA1073
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7450. MTMR2.

Subcellular locationi

GO - Cellular componenti

  • axon Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite Source: BHF-UCL
  • dendritic spine Source: BHF-UCL
  • early endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
  • postsynaptic density Source: BHF-UCL
  • synaptic membrane Source: BHF-UCL
  • synaptic vesicle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 4B1 (CMT4B1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4.
See also OMIM:601382
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_047947283R → W in CMT4B1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi417C → S: Loss of activity. 2 Publications1
Mutagenesisi419D → A: No effect. 1 Publication1
Mutagenesisi422D → A: Loss of activity. 1 Publication1
Mutagenesisi607L → Y: Reduces homodimerization and interaction with SBF1. 1 Publication1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

DisGeNETi8898.
MalaCardsiMTMR2.
MIMi601382. phenotype.
OpenTargetsiENSG00000087053.
Orphaneti99955. Charcot-Marie-Tooth disease type 4B1.
PharmGKBiPA31253.

Polymorphism and mutation databases

BioMutaiMTMR2.
DMDMi212276520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000949341 – 643Myotubularin-related protein 2Add BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphoserineBy similarity1
Modified residuei9PhosphoserineBy similarity1
Modified residuei58PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13614.
MaxQBiQ13614.
PaxDbiQ13614.
PeptideAtlasiQ13614.
PRIDEiQ13614.

PTM databases

DEPODiQ13614.
iPTMnetiQ13614.
PhosphoSitePlusiQ13614.
SwissPalmiQ13614.

Expressioni

Gene expression databases

BgeeiENSG00000087053.
CleanExiHS_MTMR2.
ExpressionAtlasiQ13614. baseline and differential.
GenevisibleiQ13614. HS.

Organism-specific databases

HPAiHPA049831.

Interactioni

Subunit structurei

Homooligomer and heterooligomer. Interacts with SBF1 and SBF2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NEFLP071962EBI-475631,EBI-475646

Protein-protein interaction databases

BioGridi114415. 14 interactors.
IntActiQ13614. 5 interactors.
MINTiMINT-6774021.
STRINGi9606.ENSP00000345752.

Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi84 – 95Combined sources12
Turni96 – 98Combined sources3
Beta strandi99 – 121Combined sources23
Beta strandi123 – 128Combined sources6
Helixi129 – 131Combined sources3
Beta strandi132 – 138Combined sources7
Beta strandi145 – 147Combined sources3
Beta strandi149 – 155Combined sources7
Turni156 – 158Combined sources3
Beta strandi159 – 164Combined sources6
Helixi167 – 169Combined sources3
Helixi172 – 182Combined sources11
Turni185 – 189Combined sources5
Helixi193 – 195Combined sources3
Helixi205 – 207Combined sources3
Helixi211 – 217Combined sources7
Beta strandi223 – 228Combined sources6
Turni230 – 233Combined sources4
Beta strandi234 – 236Combined sources3
Beta strandi242 – 247Combined sources6
Helixi252 – 261Combined sources10
Helixi263 – 265Combined sources3
Beta strandi269 – 273Combined sources5
Turni275 – 277Combined sources3
Beta strandi280 – 284Combined sources5
Turni290 – 293Combined sources4
Helixi297 – 309Combined sources13
Beta strandi310 – 312Combined sources3
Beta strandi314 – 320Combined sources7
Helixi324 – 333Combined sources10
Turni340 – 342Combined sources3
Beta strandi346 – 350Combined sources5
Helixi356 – 370Combined sources15
Helixi376 – 378Combined sources3
Helixi379 – 386Combined sources8
Helixi388 – 407Combined sources20
Beta strandi413 – 416Combined sources4
Beta strandi418 – 422Combined sources5
Helixi423 – 435Combined sources13
Helixi437 – 440Combined sources4
Helixi442 – 452Combined sources11
Turni453 – 457Combined sources5
Helixi460 – 464Combined sources5
Turni465 – 467Combined sources3
Helixi479 – 493Combined sources15
Turni495 – 497Combined sources3
Helixi502 – 514Combined sources13
Beta strandi516 – 518Combined sources3
Beta strandi522 – 524Combined sources3
Helixi525 – 530Combined sources6
Helixi533 – 536Combined sources4
Helixi540 – 545Combined sources6
Helixi548 – 551Combined sources4
Turni554 – 557Combined sources4
Beta strandi560 – 562Combined sources3
Turni570 – 572Combined sources3
Helixi577 – 580Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LW3X-ray2.30A1-643[»]
1M7RX-ray2.60A/B1-643[»]
1ZSQX-ray1.82A73-586[»]
1ZVRX-ray1.98A73-586[»]
ProteinModelPortaliQ13614.
SMRiQ13614.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13614.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 139GRAMAdd BLAST72
Domaini205 – 580Myotubularin phosphatasePROSITE-ProRule annotationAdd BLAST376

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni330 – 333Substrate binding1 Publication4
Regioni355 – 356Substrate binding1 Publication2
Regioni417 – 423Substrate binding1 Publication7

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili593 – 6271 PublicationAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 53Ser-richAdd BLAST50

Domaini

The coiled-coil domain mediates interaction with SBF2.

Sequence similaritiesi

Contains 1 GRAM domain.Curated
Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1089. Eukaryota.
ENOG410XPTU. LUCA.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiQ13614.
KOiK18081.
OMAiNDMWRAT.
OrthoDBiEOG091G04DS.
PhylomeDBiQ13614.
TreeFamiTF315197.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PfamiPF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 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: Q13614-1) [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
MEKSSSCESL GSQPAAARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI
60 70 80 90 100
STSADNFSPD LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA
110 120 130 140 150
VRGTLTVTNY RLYFKSMERD PPFVLDASLG VINRVEKIGG ASSRGENSYG
160 170 180 190 200
LETVCKDIRN LRFAHKPEGR TRRSIFENLM KYAFPVSNNL PLFAFEYKEV
210 220 230 240 250
FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY PALLVVPANI
260 270 280 290 300
PDEELKRVAS FRSRGRIPVL SWIHPESQAT ITRCSQPMVG VSGKRSKEDE
310 320 330 340 350
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF
360 370 380 390 400
LDIHNIHVMR ESLRKLKEIV YPNIEETHWL SNLESTHWLE HIKLILAGAL
410 420 430 440 450
RIADKVESGK TSVVVHCSDG WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE
460 470 480 490 500
KEWLSFGHRF QLRVGHGDKN HADADRSPVF LQFIDCVWQM TRQFPTAFEF
510 520 530 540 550
NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKRTVSL WSYINSQLED
560 570 580 590 600
FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHNRYKEL
610 620 630 640
LAKRAELQKK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV
Length:643
Mass (Da):73,381
Last modified:November 4, 2008 - v4
Checksum:i10FD6508D0CDA719
GO
Isoform 2 (identifier: Q13614-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.
Show »
Length:571
Mass (Da):65,959
Checksum:iDBC304269CEFC843
GO

Sequence cautioni

The sequence BAA83025 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0472553K → T.2 PublicationsCorresponds to variant rs3824874dbSNPEnsembl.1
Natural variantiVAR_047947283R → W in CMT4B1. 1 Publication1
Natural variantiVAR_047256545N → S.Corresponds to variant rs558018dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0449331 – 72Missing in isoform 2. 1 PublicationAdd BLAST72

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028996 mRNA. Translation: BAA83025.2. Different initiation.
AK302940 mRNA. Translation: BAG64098.1.
AP000870 Genomic DNA. No translation available.
AP001877 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66971.1.
BC052990 mRNA. Translation: AAH52990.1.
U58033 mRNA. Translation: AAC79118.1.
CCDSiCCDS8305.1. [Q13614-1]
CCDS8306.1. [Q13614-2]
PIRiT09497.
RefSeqiNP_001230500.1. NM_001243571.1. [Q13614-2]
NP_057240.3. NM_016156.5. [Q13614-1]
NP_958435.1. NM_201278.2. [Q13614-2]
NP_958438.1. NM_201281.2. [Q13614-2]
XP_005274431.1. XM_005274374.2. [Q13614-2]
XP_005274432.1. XM_005274375.2. [Q13614-2]
XP_006718997.1. XM_006718934.2. [Q13614-2]
XP_006718998.1. XM_006718935.2. [Q13614-2]
XP_006718999.1. XM_006718936.3. [Q13614-2]
XP_016874006.1. XM_017018517.1. [Q13614-2]
XP_016874007.1. XM_017018518.1. [Q13614-2]
UniGeneiHs.181326.

Genome annotation databases

EnsembliENST00000346299; ENSP00000345752; ENSG00000087053. [Q13614-1]
ENST00000352297; ENSP00000343737; ENSG00000087053. [Q13614-2]
ENST00000393223; ENSP00000376915; ENSG00000087053. [Q13614-2]
ENST00000409459; ENSP00000386882; ENSG00000087053. [Q13614-2]
GeneIDi8898.
KEGGihsa:8898.
UCSCiuc001pft.4. human. [Q13614-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Inherited peripheral neuropathies mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028996 mRNA. Translation: BAA83025.2. Different initiation.
AK302940 mRNA. Translation: BAG64098.1.
AP000870 Genomic DNA. No translation available.
AP001877 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66971.1.
BC052990 mRNA. Translation: AAH52990.1.
U58033 mRNA. Translation: AAC79118.1.
CCDSiCCDS8305.1. [Q13614-1]
CCDS8306.1. [Q13614-2]
PIRiT09497.
RefSeqiNP_001230500.1. NM_001243571.1. [Q13614-2]
NP_057240.3. NM_016156.5. [Q13614-1]
NP_958435.1. NM_201278.2. [Q13614-2]
NP_958438.1. NM_201281.2. [Q13614-2]
XP_005274431.1. XM_005274374.2. [Q13614-2]
XP_005274432.1. XM_005274375.2. [Q13614-2]
XP_006718997.1. XM_006718934.2. [Q13614-2]
XP_006718998.1. XM_006718935.2. [Q13614-2]
XP_006718999.1. XM_006718936.3. [Q13614-2]
XP_016874006.1. XM_017018517.1. [Q13614-2]
XP_016874007.1. XM_017018518.1. [Q13614-2]
UniGeneiHs.181326.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LW3X-ray2.30A1-643[»]
1M7RX-ray2.60A/B1-643[»]
1ZSQX-ray1.82A73-586[»]
1ZVRX-ray1.98A73-586[»]
ProteinModelPortaliQ13614.
SMRiQ13614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114415. 14 interactors.
IntActiQ13614. 5 interactors.
MINTiMINT-6774021.
STRINGi9606.ENSP00000345752.

Chemistry databases

SwissLipidsiSLP:000001135.

PTM databases

DEPODiQ13614.
iPTMnetiQ13614.
PhosphoSitePlusiQ13614.
SwissPalmiQ13614.

Polymorphism and mutation databases

BioMutaiMTMR2.
DMDMi212276520.

Proteomic databases

EPDiQ13614.
MaxQBiQ13614.
PaxDbiQ13614.
PeptideAtlasiQ13614.
PRIDEiQ13614.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346299; ENSP00000345752; ENSG00000087053. [Q13614-1]
ENST00000352297; ENSP00000343737; ENSG00000087053. [Q13614-2]
ENST00000393223; ENSP00000376915; ENSG00000087053. [Q13614-2]
ENST00000409459; ENSP00000386882; ENSG00000087053. [Q13614-2]
GeneIDi8898.
KEGGihsa:8898.
UCSCiuc001pft.4. human. [Q13614-1]

Organism-specific databases

CTDi8898.
DisGeNETi8898.
GeneCardsiMTMR2.
GeneReviewsiMTMR2.
HGNCiHGNC:7450. MTMR2.
HPAiHPA049831.
MalaCardsiMTMR2.
MIMi601382. phenotype.
603557. gene.
neXtProtiNX_Q13614.
OpenTargetsiENSG00000087053.
Orphaneti99955. Charcot-Marie-Tooth disease type 4B1.
PharmGKBiPA31253.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1089. Eukaryota.
ENOG410XPTU. LUCA.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiQ13614.
KOiK18081.
OMAiNDMWRAT.
OrthoDBiEOG091G04DS.
PhylomeDBiQ13614.
TreeFamiTF315197.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087053-MONOMER.
BRENDAi3.1.3.64. 2681.
3.1.3.95. 2681.
ReactomeiR-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

ChiTaRSiMTMR2. human.
EvolutionaryTraceiQ13614.
GeneWikiiMTMR2.
GenomeRNAii8898.
PROiQ13614.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087053.
CleanExiHS_MTMR2.
ExpressionAtlasiQ13614. baseline and differential.
GenevisibleiQ13614. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PfamiPF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTMR2_HUMAN
AccessioniPrimary (citable) accession number: Q13614
Secondary accession number(s): A6NN98, Q9UPS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 4, 2008
Last modified: November 30, 2016
This is version 174 of the entry and version 4 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 11
    Human chromosome 11: 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.