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Protein

Suppressor of fused homolog

Gene

SUFU

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

Functioni

Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes (PubMed:15367681, PubMed:24311597, PubMed:24217340). Down-regulates GLI2-mediated transactivation of target genes (PubMed:24311597, PubMed:24217340). Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein (PubMed:10806483, PubMed:24217340). Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). Required for normal embryonic development. Required for the proper formation of hair follicles and the control of epidermal differentiation (By similarity).By similarity9 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • signal transducer activity Source: ProtInc
  • transcription corepressor activity Source: UniProtKB
  • transcription factor binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiR-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-5632684. Hedgehog 'on' state.
SignaLinkiQ9UMX1.
SIGNORiQ9UMX1.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of fused homolog
Short name:
SUFUH
Gene namesi
Name:SUFU
ORF Names:UNQ650/PRO1280
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:16466. SUFU.

Subcellular locationi

GO - Cellular componenti

  • ciliary base Source: Reactome
  • ciliary tip Source: Reactome
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Medulloblastoma (MDB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionMalignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.
See also OMIM:155255

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106E → A: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi111D → A: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi128T → A or D: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi147Y → R: Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-159 and R-380. 1 Publication1
Mutagenesisi152E → A: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi159D → A: Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding. 1 Publication1
Mutagenesisi159D → R: Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-380. 1 Publication1
Mutagenesisi181E → A: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi221E → A: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi262D → A: No effect on down-regulation of GLI1 activity. 1 Publication1
Mutagenesisi380L → R: Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-159. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi51684.
MalaCardsiSUFU.
MIMi155255. phenotype.
OpenTargetsiENSG00000107882.
Orphaneti251863. Desmoplastic/nodular medulloblastoma.
263662. Familial multiple meningioma.
251858. Medulloblastoma with extensive nodularity.
PharmGKBiPA38146.

Chemistry databases

ChEMBLiCHEMBL5390.

Polymorphism and mutation databases

BioMutaiSUFU.
DMDMi62511179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000723021 – 484Suppressor of fused homologAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei301PhosphoserineCombined sources1
Modified residuei303N6-acetyllysineCombined sources1
Modified residuei342PhosphoserineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei481PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UMX1.
PaxDbiQ9UMX1.
PeptideAtlasiQ9UMX1.
PRIDEiQ9UMX1.

PTM databases

iPTMnetiQ9UMX1.
PhosphoSitePlusiQ9UMX1.

Expressioni

Tissue specificityi

Ubiquitous in adult tissues. Detected in osteoblasts of the perichondrium in the developing limb of 12-week old embryos. Isoform 1 is detected in fetal brain, lung, kidney and testis. Isoform 2 is detected in fetal testis, and at much lower levels in fetal brain, lung and kidney.2 Publications

Gene expression databases

BgeeiENSG00000107882.
CleanExiHS_SUFU.
GenevisibleiQ9UMX1. HS.

Organism-specific databases

HPAiHPA008700.

Interactioni

Subunit structurei

May form homodimers. Part of a DNA-bound corepressor complex containing SAP18, GLI1 and SIN3. Part of a complex containing CTNNB1. Binds BTRC, GLI2, GLI3, SAP18 and STK36. Binds both free and DNA-bound GLI1. Interacts with KIF7. Interacts with GLI3FL and this interaction regulates the formation of either repressor or activator forms of GLI3. Its association with GLI3FL is regulated by Hh signaling and dissociation of the SUFU-GLI3 interaction requires the presence of the ciliary motor KIF3A (By similarity). Interacts with ULK3; inactivating the protein kinase activity of ULK3 (PubMed:20643644). Interacts with RAB23 (PubMed:22365972).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GLI1P0815125EBI-740595,EBI-308084
Gli2Q0VGT23EBI-740595,EBI-9344284From a different organism.
GLI3P100713EBI-740595,EBI-308055
PEX26Q7Z4122EBI-740595,EBI-752057
RCN3Q96D154EBI-740595,EBI-746283
STK36Q9NRP73EBI-740595,EBI-863797
ZNF747Q9BV973EBI-740595,EBI-4395497
ZNF764Q96H863EBI-740595,EBI-745775

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi119676. 40 interactors.
IntActiQ9UMX1. 38 interactors.
MINTiMINT-1441707.
STRINGi9606.ENSP00000358918.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 29Combined sources3
Helixi32 – 44Combined sources13
Beta strandi52 – 55Combined sources4
Helixi60 – 62Combined sources3
Beta strandi69 – 76Combined sources8
Helixi80 – 82Combined sources3
Beta strandi87 – 96Combined sources10
Beta strandi101 – 105Combined sources5
Beta strandi110 – 125Combined sources16
Helixi136 – 151Combined sources16
Beta strandi160 – 162Combined sources3
Beta strandi169 – 171Combined sources3
Beta strandi176 – 181Combined sources6
Beta strandi188 – 190Combined sources3
Beta strandi193 – 203Combined sources11
Helixi205 – 213Combined sources9
Helixi216 – 224Combined sources9
Helixi227 – 229Combined sources3
Turni230 – 234Combined sources5
Helixi244 – 247Combined sources4
Helixi250 – 262Combined sources13
Beta strandi266 – 276Combined sources11
Beta strandi363 – 367Combined sources5
Beta strandi369 – 373Combined sources5
Helixi375 – 378Combined sources4
Helixi381 – 387Combined sources7
Helixi389 – 391Combined sources3
Beta strandi395 – 403Combined sources9
Beta strandi405 – 409Combined sources5
Beta strandi420 – 422Combined sources3
Beta strandi424 – 427Combined sources4
Beta strandi430 – 434Combined sources5
Helixi437 – 446Combined sources10
Turni447 – 449Combined sources3
Beta strandi460 – 464Combined sources5
Helixi465 – 467Combined sources3
Beta strandi469 – 473Combined sources5
Helixi476 – 479Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M1LX-ray2.65A/B/C/D27-262[»]
4BL8X-ray3.04A/B32-483[»]
4BL9X-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLAX-ray3.50A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLBX-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLDX-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4KM8X-ray2.26A1-484[»]
4KM9X-ray3.19A1-484[»]
4KMDX-ray1.70A1-484[»]
4KMHX-ray3.04A/B1-484[»]
ProteinModelPortaliQ9UMX1.
SMRiQ9UMX1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UMX1.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni279 – 360Intrinsically disordered1 PublicationAdd BLAST82

Sequence similaritiesi

Belongs to the SUFU family.Curated

Phylogenomic databases

eggNOGiENOG410IFRJ. Eukaryota.
ENOG410XRUC. LUCA.
GeneTreeiENSGT00390000009747.
HOVERGENiHBG061539.
InParanoidiQ9UMX1.
KOiK06229.
OMAiGDNIPWR.
OrthoDBiEOG091G132G.
PhylomeDBiQ9UMX1.
TreeFamiTF324548.

Family and domain databases

InterProiIPR020941. SUFU-like_domain.
IPR024314. SUFU_C.
IPR007768. Suppressor_of_fused.
IPR016591. Suppressor_of_fused_euk.
[Graphical view]
PANTHERiPTHR10928. PTHR10928. 1 hit.
PfamiPF05076. SUFU. 1 hit.
PF12470. SUFU_C. 1 hit.
[Graphical view]
PIRSFiPIRSF011844. Suppressor_of_fused_protein. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UMX1-1) [UniParc]FASTAAdd to basket
Also known as: Su(fu)484

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
MAELRPSGAP GPTAPPAPGP TAPPAFASLF PPGLHAIYGE CRRLYPDQPN
60 70 80 90 100
PLQVTAIVKY WLGGPDPLDY VSMYRNVGSP SANIPEHWHY ISFGLSDLYG
110 120 130 140 150
DNRVHEFTGT DGPSGFGFEL TFRLKRETGE SAPPTWPAEL MQGLARYVFQ
160 170 180 190 200
SENTFCSGDH VSWHSPLDNS ESRIQHMLLT EDPQMQPVQT PFGVVTFLQI
210 220 230 240 250
VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR GETIFEIDPH
260 270 280 290 300
LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDDEDSRS ICIGTQPRRL
310 320 330 340 350
SGKDTEQIRE TLRRGLEINS KPVLPPINPQ RQNGLAHDRA PSRKDSLESD
360 370 380 390 400
SSTAIIPHEL IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI
410 420 430 440 450
TGDMAITFVS TGVEGAFATE EHPYAAHGPW LQILLTEEFV EKMLEDLEDL
460 470 480
TSPEEFKLPK EYSWPEKKLK VSILPDVVFD SPLH
Note: Major isoform.
Length:484
Mass (Da):53,947
Last modified:April 12, 2005 - v2
Checksum:i4A9CD1CF75FC179A
GO
Isoform 2 (identifier: Q9UMX1-2) [UniParc]FASTAAdd to basket
Also known as: Su(fu)433

The sequence of this isoform differs from the canonical sequence as follows:
     433-433: I → L
     434-484: Missing.

Show »
Length:433
Mass (Da):47,932
Checksum:i40CF1CDD5F526102
GO
Isoform 3 (identifier: Q9UMX1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     433-484: ILLTEEFVEK...PDVVFDSPLH → VRRPFFFSLL...LMDSGPGACV

Show »
Length:481
Mass (Da):52,977
Checksum:i7B312507FF653923
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti336A → P in AAD50501 (PubMed:10559945).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02156615P → L.1 PublicationCorresponds to variant rs28942088dbSNPEnsembl.1
Natural variantiVAR_021567340A → S.1 PublicationCorresponds to variant rs34135067dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_013280433 – 484ILLTE…DSPLH → VRRPFFFSLLPFIDFLAHPS SSPLAALDGTPSWGAGHECL MDSGPGACV in isoform 3. 1 PublicationAdd BLAST52
Alternative sequenceiVSP_013278433I → L in isoform 2. 2 Publications1
Alternative sequenceiVSP_013279434 – 484Missing in isoform 2. 2 PublicationsAdd BLAST51

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144231 mRNA. Translation: AAF23890.1.
AF159447 mRNA. Translation: AAF23893.1.
AF222345 mRNA. Translation: AAF35866.1.
AF175770 mRNA. Translation: AAD50501.1.
AY081829
, AY081818, AY081819, AY081820, AY081822, AY081824, AY081825, AY081821, AY081823, AY081826, AY081828, AY081827 Genomic DNA. Translation: AAM08947.1.
AY358550 mRNA. Translation: AAQ88914.1.
AL121928, AL391121, AL157386 Genomic DNA. Translation: CAI12525.1.
AL121928, AL157386, AL391121 Genomic DNA. Translation: CAI12526.1.
AL157386, AL391121, AL121928 Genomic DNA. Translation: CAI39614.1.
AL157386, AL121928, AL391121 Genomic DNA. Translation: CAI39615.1.
AL391121, AL121928, AL157386 Genomic DNA. Translation: CAI40864.1.
AL391121, AL121928, AL157386 Genomic DNA. Translation: CAI40865.1.
BC013291 mRNA. Translation: AAH13291.1.
AF172319 mRNA. Translation: AAD51655.1.
AL137465 mRNA. Translation: CAB70752.1.
CCDSiCCDS53571.1. [Q9UMX1-2]
CCDS7537.1. [Q9UMX1-1]
PIRiT46409.
RefSeqiNP_001171604.1. NM_001178133.1. [Q9UMX1-2]
NP_057253.2. NM_016169.3. [Q9UMX1-1]
UniGeneiHs.404089.

Genome annotation databases

EnsembliENST00000369899; ENSP00000358915; ENSG00000107882. [Q9UMX1-2]
ENST00000369902; ENSP00000358918; ENSG00000107882. [Q9UMX1-1]
ENST00000423559; ENSP00000411597; ENSG00000107882. [Q9UMX1-3]
GeneIDi51684.
KEGGihsa:51684.
UCSCiuc001kvw.3. human. [Q9UMX1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144231 mRNA. Translation: AAF23890.1.
AF159447 mRNA. Translation: AAF23893.1.
AF222345 mRNA. Translation: AAF35866.1.
AF175770 mRNA. Translation: AAD50501.1.
AY081829
, AY081818, AY081819, AY081820, AY081822, AY081824, AY081825, AY081821, AY081823, AY081826, AY081828, AY081827 Genomic DNA. Translation: AAM08947.1.
AY358550 mRNA. Translation: AAQ88914.1.
AL121928, AL391121, AL157386 Genomic DNA. Translation: CAI12525.1.
AL121928, AL157386, AL391121 Genomic DNA. Translation: CAI12526.1.
AL157386, AL391121, AL121928 Genomic DNA. Translation: CAI39614.1.
AL157386, AL121928, AL391121 Genomic DNA. Translation: CAI39615.1.
AL391121, AL121928, AL157386 Genomic DNA. Translation: CAI40864.1.
AL391121, AL121928, AL157386 Genomic DNA. Translation: CAI40865.1.
BC013291 mRNA. Translation: AAH13291.1.
AF172319 mRNA. Translation: AAD51655.1.
AL137465 mRNA. Translation: CAB70752.1.
CCDSiCCDS53571.1. [Q9UMX1-2]
CCDS7537.1. [Q9UMX1-1]
PIRiT46409.
RefSeqiNP_001171604.1. NM_001178133.1. [Q9UMX1-2]
NP_057253.2. NM_016169.3. [Q9UMX1-1]
UniGeneiHs.404089.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M1LX-ray2.65A/B/C/D27-262[»]
4BL8X-ray3.04A/B32-483[»]
4BL9X-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLAX-ray3.50A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLBX-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLDX-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4KM8X-ray2.26A1-484[»]
4KM9X-ray3.19A1-484[»]
4KMDX-ray1.70A1-484[»]
4KMHX-ray3.04A/B1-484[»]
ProteinModelPortaliQ9UMX1.
SMRiQ9UMX1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119676. 40 interactors.
IntActiQ9UMX1. 38 interactors.
MINTiMINT-1441707.
STRINGi9606.ENSP00000358918.

Chemistry databases

ChEMBLiCHEMBL5390.

PTM databases

iPTMnetiQ9UMX1.
PhosphoSitePlusiQ9UMX1.

Polymorphism and mutation databases

BioMutaiSUFU.
DMDMi62511179.

Proteomic databases

EPDiQ9UMX1.
PaxDbiQ9UMX1.
PeptideAtlasiQ9UMX1.
PRIDEiQ9UMX1.

Protocols and materials databases

DNASUi51684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369899; ENSP00000358915; ENSG00000107882. [Q9UMX1-2]
ENST00000369902; ENSP00000358918; ENSG00000107882. [Q9UMX1-1]
ENST00000423559; ENSP00000411597; ENSG00000107882. [Q9UMX1-3]
GeneIDi51684.
KEGGihsa:51684.
UCSCiuc001kvw.3. human. [Q9UMX1-1]

Organism-specific databases

CTDi51684.
DisGeNETi51684.
GeneCardsiSUFU.
HGNCiHGNC:16466. SUFU.
HPAiHPA008700.
MalaCardsiSUFU.
MIMi155255. phenotype.
607035. gene.
neXtProtiNX_Q9UMX1.
OpenTargetsiENSG00000107882.
Orphaneti251863. Desmoplastic/nodular medulloblastoma.
263662. Familial multiple meningioma.
251858. Medulloblastoma with extensive nodularity.
PharmGKBiPA38146.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFRJ. Eukaryota.
ENOG410XRUC. LUCA.
GeneTreeiENSGT00390000009747.
HOVERGENiHBG061539.
InParanoidiQ9UMX1.
KOiK06229.
OMAiGDNIPWR.
OrthoDBiEOG091G132G.
PhylomeDBiQ9UMX1.
TreeFamiTF324548.

Enzyme and pathway databases

ReactomeiR-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-5632684. Hedgehog 'on' state.
SignaLinkiQ9UMX1.
SIGNORiQ9UMX1.

Miscellaneous databases

ChiTaRSiSUFU. human.
EvolutionaryTraceiQ9UMX1.
GeneWikiiSUFU.
GenomeRNAii51684.
PROiQ9UMX1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107882.
CleanExiHS_SUFU.
GenevisibleiQ9UMX1. HS.

Family and domain databases

InterProiIPR020941. SUFU-like_domain.
IPR024314. SUFU_C.
IPR007768. Suppressor_of_fused.
IPR016591. Suppressor_of_fused_euk.
[Graphical view]
PANTHERiPTHR10928. PTHR10928. 1 hit.
PfamiPF05076. SUFU. 1 hit.
PF12470. SUFU_C. 1 hit.
[Graphical view]
PIRSFiPIRSF011844. Suppressor_of_fused_protein. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSUFU_HUMAN
AccessioniPrimary (citable) accession number: Q9UMX1
Secondary accession number(s): Q7LCP7
, Q9NT90, Q9NZ07, Q9UHK2, Q9UHM8, Q9UMY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: November 30, 2016
This is version 143 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 10
    Human chromosome 10: 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.