Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Collagen type IV alpha-3-binding protein

Gene

COL4A3BP

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

Functioni

Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei472Ceramide1
Binding sitei493Ceramide1
Binding sitei530Ceramide1
Binding sitei579Ceramide1

GO - Molecular functioni

  • ceramide binding Source: UniProtKB
  • ceramide transporter activity Source: UniProtKB
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • protein kinase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113163-MONOMER.
BRENDAi2.7.11.9. 2681.
ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.
SIGNORiQ9Y5P4.

Chemistry databases

SwissLipidsiSLP:000000407.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen type IV alpha-3-binding protein
Alternative name(s):
Ceramide transfer protein
Short name:
hCERT
Goodpasture antigen-binding protein
Short name:
GPBP
START domain-containing protein 11
Short name:
StARD11
StAR-related lipid transfer protein 11
Gene namesi
Name:COL4A3BP
Synonyms:CERT, STARD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:2205. COL4A3BP.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 34 (MRD34)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:616351
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073721132S → L in MRD34. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi132S → A: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity. 1 Publication1
Mutagenesisi324D → A: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA. 1 Publication1
Mutagenesisi472E → A: Reduces ceramide transfer. 1 Publication1
Mutagenesisi493Q → A: No effect on ceramide transfer activity. 1 Publication1
Mutagenesisi499W → A: Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588. 1 Publication1
Mutagenesisi530N → A: Reduces ceramide transfer. 1 Publication1
Mutagenesisi588W → A: Abolishes ceramide transfer; when associated with A-499. 1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi10087.
MIMi616351. phenotype.
OpenTargetsiENSG00000113163.
PharmGKBiPA26720.

Chemistry databases

ChEMBLiCHEMBL3399913.

Polymorphism and mutation databases

BioMutaiCOL4A3BP.
DMDMi20978413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002206651 – 624Collagen type IV alpha-3-binding proteinAdd BLAST624

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei126PhosphoserineCombined sources1
Modified residuei132Phosphoserine; by PKD1 Publication1
Modified residuei135PhosphoserineBy similarity1
Modified residuei315PhosphoserineCombined sources1
Modified residuei372PhosphotyrosineCombined sources1
Modified residuei373PhosphoserineCombined sources1
Modified residuei377PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-132 decreases the affinity toward phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity. Inactivated by hyperphosphorylation of serine residues by CSNK1G2/CK1 that triggers dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y5P4.
PaxDbiQ9Y5P4.
PeptideAtlasiQ9Y5P4.
PRIDEiQ9Y5P4.

PTM databases

iPTMnetiQ9Y5P4.
PhosphoSitePlusiQ9Y5P4.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000113163.
CleanExiHS_COL4A3BP.
ExpressionAtlasiQ9Y5P4. baseline and differential.
GenevisibleiQ9Y5P4. HS.

Organism-specific databases

HPAiHPA035645.

Interactioni

Subunit structurei

Interacts with COL4A3. Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTL8Q9H5683EBI-739994,EBI-10306917
ARL6IP1Q150413EBI-739994,EBI-714543
CSNK1G2P783684EBI-739994,EBI-748380
ITGB3BPQ133524EBI-739994,EBI-712105
STX2P32856-24EBI-11156432,EBI-11956649

Protein-protein interaction databases

BioGridi115396. 25 interactors.
IntActiQ9Y5P4. 20 interactors.
MINTiMINT-1441568.
STRINGi9606.ENSP00000369862.

Chemistry databases

BindingDBiQ9Y5P4.

Structurei

Secondary structure

1624
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 33Combined sources8
Turni36 – 38Combined sources3
Beta strandi40 – 48Combined sources9
Beta strandi51 – 56Combined sources6
Beta strandi58 – 62Combined sources5
Beta strandi64 – 71Combined sources8
Beta strandi75 – 78Combined sources4
Beta strandi85 – 90Combined sources6
Beta strandi93 – 98Combined sources6
Helixi102 – 119Combined sources18
Helixi397 – 407Combined sources11
Beta strandi413 – 415Combined sources3
Beta strandi418 – 424Combined sources7
Beta strandi427 – 432Combined sources6
Beta strandi444 – 451Combined sources8
Helixi455 – 463Combined sources9
Helixi465 – 467Combined sources3
Helixi468 – 471Combined sources4
Beta strandi474 – 485Combined sources12
Beta strandi488 – 495Combined sources8
Beta strandi499 – 502Combined sources4
Beta strandi504 – 515Combined sources12
Beta strandi518 – 522Combined sources5
Beta strandi525 – 532Combined sources8
Beta strandi542 – 546Combined sources5
Beta strandi548 – 559Combined sources12
Beta strandi563 – 565Combined sources3
Helixi570 – 572Combined sources3
Beta strandi573 – 584Combined sources12
Helixi591 – 617Combined sources27
Beta strandi618 – 620Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E3MX-ray2.20A347-624[»]
2E3NX-ray1.40A347-624[»]
2E3OX-ray1.55A347-624[»]
2E3PX-ray1.40A/B347-624[»]
2E3QX-ray2.08A347-624[»]
2E3RX-ray1.65A/B347-624[»]
2E3SX-ray1.94A347-624[»]
2RSGNMR-A24-117[»]
2Z9YX-ray1.80A347-624[»]
2Z9ZX-ray1.74A347-624[»]
3H3QX-ray2.00A/B347-624[»]
3H3RX-ray1.85A/B347-624[»]
3H3SX-ray1.66A/B347-624[»]
3H3TX-ray2.40A/B347-624[»]
4HHVX-ray1.75A/B20-121[»]
ProteinModelPortaliQ9Y5P4.
SMRiQ9Y5P4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5P4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 117PHPROSITE-ProRule annotationAdd BLAST95
Domaini389 – 618STARTPROSITE-ProRule annotationAdd BLAST230

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili263 – 303Sequence analysisAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi321 – 327FFAT7

Domaini

The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids.1 Publication
The PH domain targets the Golgi apparatus.1 Publication
The FFAT motif is required for interaction with VAPA and VAPB.1 Publication

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 START domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1739. Eukaryota.
ENOG410XQTB. LUCA.
GeneTreeiENSGT00650000093230.
HOVERGENiHBG050753.
InParanoidiQ9Y5P4.
KOiK08283.
OMAiSHALWPE.
OrthoDBiEOG091G063Z.
PhylomeDBiQ9Y5P4.
TreeFamiTF106160.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9Y5P4-1) [UniParc]FASTAAdd to basket
Also known as: CERTL

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
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN
60 70 80 90 100
ALSYYKSEDE TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ
110 120 130 140 150
DPDHRQQWID AIEQHKTESG YGSESSLRRH GSMVSLVSGA SGYSATSTSS
160 170 180 190 200
FKKGHSLREK LAEMETFRDI LCRQVDTLQK YFDACADAVS KDELQRDKVV
210 220 230 240 250
EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID FKGEAITFKA
260 270 280 290 300
TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK
310 320 330 340 350
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP
360 370 380 390 400
TSLPSGDAFS SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM
410 420 430 440 450
VQNHMTYSLQ DVGGDANWQL VVEEGEMKVY RREVEENGIV LDPLKATHAV
460 470 480 490 500
KGVTGHEVCN YFWNVDVRND WETTIENFHV VETLADNAII IYQTHKRVWP
510 520 530 540 550
ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL NNRCVRAKIN
560 570 580 590 600
VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
610 620
EYPKFLKRFT SYVQEKTAGK PILF
Length:624
Mass (Da):70,835
Last modified:November 1, 1999 - v1
Checksum:iA125162492AC5A0E
GO
Isoform 2 (identifier: Q9Y5P4-2) [UniParc]FASTAAdd to basket
Also known as: Delta26, GPBPD26

The sequence of this isoform differs from the canonical sequence as follows:
     371-396: Missing.

Show »
Length:598
Mass (Da):68,007
Checksum:iFC52E241DE7C5D85
GO
Isoform 3 (identifier: Q9Y5P4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQHSCIPTPP...GLLLGCRASM

Show »
Length:752
Mass (Da):83,708
Checksum:i277A14A581D94EDF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073721132S → L in MRD34. 1 Publication1
Natural variantiVAR_069403138S → C Found in a patient with mental retardation. 1 Publication1
Natural variantiVAR_061815599K → R.Corresponds to variant rs55882089dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0410221M → MQHSCIPTPPSPFSAPPAFL PVVTRESRRGLSSGGSAGRN AGVTATAAAADGWKGRLPSP LVLLPRSARCQARRRRGGRT SSLLLLPPTPERALFASPSP DPSPRGLGASSGAAEGAGAG LLLGCRASM in isoform 3. 1 Publication1
Alternative sequenceiVSP_006276371 – 396Missing in isoform 2. 4 PublicationsAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136450 mRNA. Translation: AAD30288.1.
AF232930 mRNA. Translation: AAG42046.1.
AF232935 Genomic DNA. Translation: AAG42051.1.
AY453385 mRNA. Translation: AAR26717.1.
AY453386 mRNA. Translation: AAR26718.1.
AK091851 mRNA. Translation: BAC03762.1.
AK096854 mRNA. Translation: BAG53379.1.
AK292087 mRNA. Translation: BAF84776.1.
AC008897 Genomic DNA. No translation available.
AC112183 Genomic DNA. No translation available.
AC116341 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95757.1.
CH471084 Genomic DNA. Translation: EAW95760.1.
BC000102 mRNA. Translation: AAH00102.1.
AB036934 Genomic DNA. Translation: BAB58974.1.
AB036936 Genomic DNA. Translation: BAB58977.1.
CCDSiCCDS4028.1. [Q9Y5P4-1]
CCDS4029.1. [Q9Y5P4-2]
CCDS47235.1. [Q9Y5P4-3]
RefSeqiNP_001123577.1. NM_001130105.1. [Q9Y5P4-3]
NP_005704.1. NM_005713.2. [Q9Y5P4-1]
NP_112729.1. NM_031361.2. [Q9Y5P4-2]
XP_006714576.1. XM_006714513.2. [Q9Y5P4-1]
XP_016864408.1. XM_017008919.1. [Q9Y5P4-2]
UniGeneiHs.270437.

Genome annotation databases

EnsembliENST00000261415; ENSP00000261415; ENSG00000113163. [Q9Y5P4-2]
ENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
ENST00000405807; ENSP00000383996; ENSG00000113163. [Q9Y5P4-1]
GeneIDi10087.
KEGGihsa:10087.
UCSCiuc003kds.4. human. [Q9Y5P4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136450 mRNA. Translation: AAD30288.1.
AF232930 mRNA. Translation: AAG42046.1.
AF232935 Genomic DNA. Translation: AAG42051.1.
AY453385 mRNA. Translation: AAR26717.1.
AY453386 mRNA. Translation: AAR26718.1.
AK091851 mRNA. Translation: BAC03762.1.
AK096854 mRNA. Translation: BAG53379.1.
AK292087 mRNA. Translation: BAF84776.1.
AC008897 Genomic DNA. No translation available.
AC112183 Genomic DNA. No translation available.
AC116341 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95757.1.
CH471084 Genomic DNA. Translation: EAW95760.1.
BC000102 mRNA. Translation: AAH00102.1.
AB036934 Genomic DNA. Translation: BAB58974.1.
AB036936 Genomic DNA. Translation: BAB58977.1.
CCDSiCCDS4028.1. [Q9Y5P4-1]
CCDS4029.1. [Q9Y5P4-2]
CCDS47235.1. [Q9Y5P4-3]
RefSeqiNP_001123577.1. NM_001130105.1. [Q9Y5P4-3]
NP_005704.1. NM_005713.2. [Q9Y5P4-1]
NP_112729.1. NM_031361.2. [Q9Y5P4-2]
XP_006714576.1. XM_006714513.2. [Q9Y5P4-1]
XP_016864408.1. XM_017008919.1. [Q9Y5P4-2]
UniGeneiHs.270437.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E3MX-ray2.20A347-624[»]
2E3NX-ray1.40A347-624[»]
2E3OX-ray1.55A347-624[»]
2E3PX-ray1.40A/B347-624[»]
2E3QX-ray2.08A347-624[»]
2E3RX-ray1.65A/B347-624[»]
2E3SX-ray1.94A347-624[»]
2RSGNMR-A24-117[»]
2Z9YX-ray1.80A347-624[»]
2Z9ZX-ray1.74A347-624[»]
3H3QX-ray2.00A/B347-624[»]
3H3RX-ray1.85A/B347-624[»]
3H3SX-ray1.66A/B347-624[»]
3H3TX-ray2.40A/B347-624[»]
4HHVX-ray1.75A/B20-121[»]
ProteinModelPortaliQ9Y5P4.
SMRiQ9Y5P4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115396. 25 interactors.
IntActiQ9Y5P4. 20 interactors.
MINTiMINT-1441568.
STRINGi9606.ENSP00000369862.

Chemistry databases

BindingDBiQ9Y5P4.
ChEMBLiCHEMBL3399913.
SwissLipidsiSLP:000000407.

PTM databases

iPTMnetiQ9Y5P4.
PhosphoSitePlusiQ9Y5P4.

Polymorphism and mutation databases

BioMutaiCOL4A3BP.
DMDMi20978413.

Proteomic databases

EPDiQ9Y5P4.
PaxDbiQ9Y5P4.
PeptideAtlasiQ9Y5P4.
PRIDEiQ9Y5P4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261415; ENSP00000261415; ENSG00000113163. [Q9Y5P4-2]
ENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
ENST00000405807; ENSP00000383996; ENSG00000113163. [Q9Y5P4-1]
GeneIDi10087.
KEGGihsa:10087.
UCSCiuc003kds.4. human. [Q9Y5P4-1]

Organism-specific databases

CTDi10087.
DisGeNETi10087.
GeneCardsiCOL4A3BP.
HGNCiHGNC:2205. COL4A3BP.
HPAiHPA035645.
MIMi604677. gene.
616351. phenotype.
neXtProtiNX_Q9Y5P4.
OpenTargetsiENSG00000113163.
PharmGKBiPA26720.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1739. Eukaryota.
ENOG410XQTB. LUCA.
GeneTreeiENSGT00650000093230.
HOVERGENiHBG050753.
InParanoidiQ9Y5P4.
KOiK08283.
OMAiSHALWPE.
OrthoDBiEOG091G063Z.
PhylomeDBiQ9Y5P4.
TreeFamiTF106160.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113163-MONOMER.
BRENDAi2.7.11.9. 2681.
ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.
SIGNORiQ9Y5P4.

Miscellaneous databases

EvolutionaryTraceiQ9Y5P4.
GeneWikiiCOL4A3BP.
GenomeRNAii10087.
PROiQ9Y5P4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113163.
CleanExiHS_COL4A3BP.
ExpressionAtlasiQ9Y5P4. baseline and differential.
GenevisibleiQ9Y5P4. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiC43BP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5P4
Secondary accession number(s): A8K7S2
, B3KUB7, Q53YV1, Q53YV2, Q96Q85, Q96Q88, Q9H2S7, Q9H2S8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 151 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

Caution

Was originally reported to have a protein kinase activity and to phosphorylate on Ser and Thr residues the Goodpasture autoantigen (in vitro).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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.