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Protein

N-chimaerin

Gene

CHN1

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

Functioni

GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri205 – 255Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

  • GTPase activator activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW
  • SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128656-MONOMER.
ReactomeiR-HSA-194840. Rho GTPase cycle.
SignaLinkiP15882.
SIGNORiP15882.

Names & Taxonomyi

Protein namesi
Recommended name:
N-chimaerin
Alternative name(s):
A-chimaerin
Alpha-chimerin
N-chimerin
Short name:
NC
Rho GTPase-activating protein 2
Gene namesi
Name:CHN1
Synonyms:ARHGAP2, CHN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1943. CHN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Duane retraction syndrome 2 (DURS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Duane retraction syndrome, a congenital eye movement disorder characterized by a failure of cranial nerve VI (the abducens nerve) to develop normally, resulting in restriction or absence of abduction, adduction or both, narrowing of the palpebral fissure, and retraction of the globe on attempted adduction. Undiagnosed in children, it can lead to amblyopia, a permanent uncorrectable loss of vision.
See also OMIM:604356
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04794020L → F in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912792dbSNPEnsembl.1
Natural variantiVAR_047941126I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. 1 PublicationCorresponds to variant rs121912793dbSNPEnsembl.1
Natural variantiVAR_047942143Y → H in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912794dbSNPEnsembl.1
Natural variantiVAR_047943223A → V in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912795dbSNPEnsembl.1
Natural variantiVAR_047944228G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 PublicationCorresponds to variant rs121912796dbSNPEnsembl.1
Natural variantiVAR_047945252P → Q in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912797dbSNPEnsembl.1
Natural variantiVAR_047946313E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 PublicationCorresponds to variant rs121912798dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1123.
MalaCardsiCHN1.
MIMi604356. phenotype.
OpenTargetsiENSG00000128656.
Orphaneti233. Duane retraction syndrome.
PharmGKBiPA26473.

Polymorphism and mutation databases

BioMutaiCHN1.
DMDMi21903393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000566942 – 459N-chimaerinAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei192PhosphothreonineCombined sources1
Modified residuei340PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP15882.
MaxQBiP15882.
PaxDbiP15882.
PeptideAtlasiP15882.
PRIDEiP15882.

PTM databases

iPTMnetiP15882.
PhosphoSitePlusiP15882.

Expressioni

Tissue specificityi

In neurons in brain regions that are involved in learning and memory processes.

Developmental stagei

Increases in amount during brain development coincident with synaptogenesis.

Gene expression databases

BgeeiENSG00000128656.
CleanExiHS_CHN1.
ExpressionAtlasiP15882. baseline and differential.
GenevisibleiP15882. HS.

Organism-specific databases

HPAiHPA036111.

Interactioni

Subunit structurei

Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HEMK1Q9Y5R43EBI-718947,EBI-10329202
NCK2O436398EBI-718947,EBI-713635

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: ProtInc

Protein-protein interaction databases

BioGridi107547. 10 interactors.
DIPiDIP-42177N.
IntActiP15882. 6 interactors.
MINTiMINT-1173390.
STRINGi9606.ENSP00000386741.

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 26Combined sources8
Helixi56 – 63Combined sources8
Beta strandi69 – 74Combined sources6
Beta strandi76 – 78Combined sources3
Beta strandi82 – 87Combined sources6
Beta strandi89 – 96Combined sources8
Beta strandi98 – 107Combined sources10
Helixi113 – 129Combined sources17
Helixi131 – 136Combined sources6
Turni143 – 145Combined sources3
Beta strandi146 – 148Combined sources3
Helixi164 – 166Combined sources3
Beta strandi208 – 211Combined sources4
Turni220 – 222Combined sources3
Beta strandi228 – 230Combined sources3
Beta strandi233 – 236Combined sources4
Turni237 – 239Combined sources3
Helixi245 – 248Combined sources4
Helixi257 – 261Combined sources5
Helixi270 – 277Combined sources8
Helixi283 – 295Combined sources13
Turni300 – 304Combined sources5
Helixi309 – 322Combined sources14
Helixi323 – 325Combined sources3
Turni330 – 332Combined sources3
Helixi336 – 348Combined sources13
Turni357 – 359Combined sources3
Helixi360 – 368Combined sources9
Helixi372 – 384Combined sources13
Helixi388 – 406Combined sources19
Helixi408 – 411Combined sources4
Helixi415 – 426Combined sources12
Helixi434 – 453Combined sources20
Helixi455 – 458Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OSAX-ray1.80A260-459[»]
3CXLX-ray2.60A15-459[»]
ProteinModelPortaliP15882.
SMRiP15882.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15882.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 135SH2PROSITE-ProRule annotationAdd BLAST87
Domaini268 – 459Rho-GAPPROSITE-ProRule annotationAdd BLAST192

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri205 – 255Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

SH2 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG1453. Eukaryota.
ENOG410YM3I. LUCA.
GeneTreeiENSGT00840000129684.
HOGENOMiHOG000231926.
HOVERGENiHBG080489.
InParanoidiP15882.
KOiK20630.
OMAiNARDGSY.
OrthoDBiEOG091G0834.
PhylomeDBiP15882.
TreeFamiTF342052.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR017356. CHN1/CHN2.
IPR020454. DAG/PE-bd.
IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF038015. N-chimaerin. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform Alpha-2 (identifier: P15882-1) [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
MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRITCTCEVE NRPKYYGREF
60 70 80 90 100
HGMISREAAD QLLIVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD
110 120 130 140 150
GKHFVGEKRF ESIHDLVTDG LITLYIETKA AEYIAKMTIN PIYEHVGYTT
160 170 180 190 200
LNREPAYKKH MPVLKETHDE RDSTGQDGVS EKRLTSLVRR ATLKENEQIP
210 220 230 240 250
KYEKIHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG LNVHKQCSKM
260 270 280 290 300
VPNDCKPDLK HVKKVYSCDL TTLVKAHTTK RPMVVDMCIR EIESRGLNSE
310 320 330 340 350
GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL
360 370 380 390 400
PIPLITYDAY PKFIESAKIM DPDEQLETLH EALKLLPPAH CETLRYLMAH
410 420 430 440 450
LKRVTLHEKE NLMNAENLGI VFGPTLMRSP ELDAMAALND IRYQRLVVEL

LIKNEDILF
Length:459
Mass (Da):53,172
Last modified:July 11, 2002 - v3
Checksum:i04C4CC9BCC611389
GO
Isoform Alpha-1 (identifier: P15882-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: MALTLFDTDE...TGQDGVSEKR → MPSKESWSGR...QPLKLFAYSQ

Show »
Length:334
Mass (Da):38,196
Checksum:i2E5BF139A231D13C
GO
Isoform 3 (identifier: P15882-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-209: Missing.

Note: No experimental confirmation available.
Show »
Length:433
Mass (Da):50,034
Checksum:iEB3E22E1C704D1BF
GO

Sequence cautioni

The sequence CAA35769 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04794020L → F in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912792dbSNPEnsembl.1
Natural variantiVAR_047941126I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. 1 PublicationCorresponds to variant rs121912793dbSNPEnsembl.1
Natural variantiVAR_047942143Y → H in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912794dbSNPEnsembl.1
Natural variantiVAR_047943223A → V in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912795dbSNPEnsembl.1
Natural variantiVAR_047944228G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 PublicationCorresponds to variant rs121912796dbSNPEnsembl.1
Natural variantiVAR_047945252P → Q in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 PublicationCorresponds to variant rs121912797dbSNPEnsembl.1
Natural variantiVAR_047946313E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 PublicationCorresponds to variant rs121912798dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0016361 – 183MALTL…VSEKR → MPSKESWSGRKTNRAAVHKS KQEGRQQDLLIAALGMKLGS PKSSVTIWQPLKLFAYSQ in isoform Alpha-1. 2 PublicationsAdd BLAST183
Alternative sequenceiVSP_043297184 – 209Missing in isoform 3. 1 PublicationAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51408 mRNA. Translation: CAA35769.1. Different initiation.
Z22641 mRNA. Translation: CAA80354.1.
AK055060 mRNA. Translation: BAG51458.1.
AK289941 mRNA. Translation: BAF82630.1.
AK300890 mRNA. Translation: BAG62531.1.
AC007435 Genomic DNA. No translation available.
AC018890 Genomic DNA. Translation: AAY14688.1.
AC020596 Genomic DNA. Translation: AAY14940.1.
CH471058 Genomic DNA. Translation: EAX11117.1.
CH471058 Genomic DNA. Translation: EAX11118.1.
CH471058 Genomic DNA. Translation: EAX11119.1.
BC011393 mRNA. Translation: AAH11393.1.
S75654 Genomic DNA. Translation: AAB33506.1.
CCDSiCCDS46454.1. [P15882-3]
CCDS46455.1. [P15882-1]
CCDS56147.1. [P15882-2]
PIRiA48090.
I53329.
RefSeqiNP_001020372.2. NM_001025201.3. [P15882-3]
NP_001193531.1. NM_001206602.1. [P15882-2]
NP_001813.1. NM_001822.5. [P15882-1]
UniGeneiHs.380138.

Genome annotation databases

EnsembliENST00000295497; ENSP00000295497; ENSG00000128656. [P15882-2]
ENST00000409156; ENSP00000386470; ENSG00000128656. [P15882-3]
ENST00000409900; ENSP00000386741; ENSG00000128656. [P15882-1]
GeneIDi1123.
KEGGihsa:1123.
UCSCiuc002ujg.4. human. [P15882-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51408 mRNA. Translation: CAA35769.1. Different initiation.
Z22641 mRNA. Translation: CAA80354.1.
AK055060 mRNA. Translation: BAG51458.1.
AK289941 mRNA. Translation: BAF82630.1.
AK300890 mRNA. Translation: BAG62531.1.
AC007435 Genomic DNA. No translation available.
AC018890 Genomic DNA. Translation: AAY14688.1.
AC020596 Genomic DNA. Translation: AAY14940.1.
CH471058 Genomic DNA. Translation: EAX11117.1.
CH471058 Genomic DNA. Translation: EAX11118.1.
CH471058 Genomic DNA. Translation: EAX11119.1.
BC011393 mRNA. Translation: AAH11393.1.
S75654 Genomic DNA. Translation: AAB33506.1.
CCDSiCCDS46454.1. [P15882-3]
CCDS46455.1. [P15882-1]
CCDS56147.1. [P15882-2]
PIRiA48090.
I53329.
RefSeqiNP_001020372.2. NM_001025201.3. [P15882-3]
NP_001193531.1. NM_001206602.1. [P15882-2]
NP_001813.1. NM_001822.5. [P15882-1]
UniGeneiHs.380138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OSAX-ray1.80A260-459[»]
3CXLX-ray2.60A15-459[»]
ProteinModelPortaliP15882.
SMRiP15882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107547. 10 interactors.
DIPiDIP-42177N.
IntActiP15882. 6 interactors.
MINTiMINT-1173390.
STRINGi9606.ENSP00000386741.

PTM databases

iPTMnetiP15882.
PhosphoSitePlusiP15882.

Polymorphism and mutation databases

BioMutaiCHN1.
DMDMi21903393.

Proteomic databases

EPDiP15882.
MaxQBiP15882.
PaxDbiP15882.
PeptideAtlasiP15882.
PRIDEiP15882.

Protocols and materials databases

DNASUi1123.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295497; ENSP00000295497; ENSG00000128656. [P15882-2]
ENST00000409156; ENSP00000386470; ENSG00000128656. [P15882-3]
ENST00000409900; ENSP00000386741; ENSG00000128656. [P15882-1]
GeneIDi1123.
KEGGihsa:1123.
UCSCiuc002ujg.4. human. [P15882-1]

Organism-specific databases

CTDi1123.
DisGeNETi1123.
GeneCardsiCHN1.
GeneReviewsiCHN1.
HGNCiHGNC:1943. CHN1.
HPAiHPA036111.
MalaCardsiCHN1.
MIMi118423. gene.
604356. phenotype.
neXtProtiNX_P15882.
OpenTargetsiENSG00000128656.
Orphaneti233. Duane retraction syndrome.
PharmGKBiPA26473.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1453. Eukaryota.
ENOG410YM3I. LUCA.
GeneTreeiENSGT00840000129684.
HOGENOMiHOG000231926.
HOVERGENiHBG080489.
InParanoidiP15882.
KOiK20630.
OMAiNARDGSY.
OrthoDBiEOG091G0834.
PhylomeDBiP15882.
TreeFamiTF342052.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128656-MONOMER.
ReactomeiR-HSA-194840. Rho GTPase cycle.
SignaLinkiP15882.
SIGNORiP15882.

Miscellaneous databases

ChiTaRSiCHN1. human.
EvolutionaryTraceiP15882.
GenomeRNAii1123.
PROiP15882.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128656.
CleanExiHS_CHN1.
ExpressionAtlasiP15882. baseline and differential.
GenevisibleiP15882. HS.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR017356. CHN1/CHN2.
IPR020454. DAG/PE-bd.
IPR002219. PE/DAG-bd.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF038015. N-chimaerin. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHIN_HUMAN
AccessioniPrimary (citable) accession number: P15882
Secondary accession number(s): A8K1M6
, B3KNU6, B4DV19, Q53SD6, Q53SH5, Q96FB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 11, 2002
Last modified: November 30, 2016
This is version 181 of the entry and version 3 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 2
    Human chromosome 2: 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.