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Protein

Extended synaptotagmin-2

Gene

ESYT2

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

Functioni

Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi400Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi401Calcium 11 Publication1
Metal bindingi401Calcium 21 Publication1
Metal bindingi413Calcium 21 Publication1
Metal bindingi460Calcium 11 Publication1
Metal bindingi460Calcium 21 Publication1
Metal bindingi461Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi462Calcium 11 Publication1
Metal bindingi462Calcium 21 Publication1
Metal bindingi462Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi464Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi466Calcium 31 Publication1
Metal bindingi467Calcium 11 Publication1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • calcium-dependent phospholipid binding Source: FlyBase
  • calcium ion binding Source: UniProtKB
  • phosphatidylcholine binding Source: UniProtKB
  • phosphatidylethanolamine binding Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Lipid transport, Transport

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.

Protein family/group databases

TCDBi9.A.57.1.2. the extended-synaptotagmin (e-syt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Extended synaptotagmin-2
Short name:
E-Syt2
Alternative name(s):
Chr2Syt
Gene namesi
Name:ESYT2
Synonyms:FAM62B, KIAA1228
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:22211. ESYT2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 103CytoplasmicSequence analysisAdd BLAST103
Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Topological domaini125 – 127LumenalSequence analysis3
Transmembranei128 – 148HelicalSequence analysisAdd BLAST21
Topological domaini149 – 921CytoplasmicSequence analysisAdd BLAST773

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • integral component of plasma membrane Source: FlyBase
  • intrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • organelle membrane contact site Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi401D → A: Abolishes calcium binding; when associated with A-413. 1 Publication1
Mutagenesisi413D → A: Abolishes calcium binding; when associated with A-401. 1 Publication1
Mutagenesisi413D → N: Strongly reduces calcium binding. 1 Publication1
Mutagenesisi466D → A: Impairs binding of the third calcium ion, but has no effect on the binding of the other two calcium ions. 1 Publication1
Mutagenesisi833 – 840KRRSGRRK → AAASGAAA: Abolishes location at the cell membrane. 1 Publication8

Organism-specific databases

OpenTargetsiENSG00000117868.
PharmGKBiPA165617947.

Polymorphism and mutation databases

BioMutaiESYT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002782581 – 921Extended synaptotagmin-2Add BLAST921

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei691PhosphoserineCombined sources1
Modified residuei693PhosphoserineCombined sources1
Modified residuei705PhosphothreonineCombined sources1
Modified residuei736PhosphoserineCombined sources1
Modified residuei738PhosphoserineBy similarity1
Modified residuei739PhosphoserineCombined sources1
Modified residuei743PhosphoserineCombined sources1
Modified residuei748PhosphoserineCombined sources1
Modified residuei755PhosphoserineCombined sources1
Modified residuei758PhosphoserineCombined sources1
Modified residuei761PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiA0FGR8.
MaxQBiA0FGR8.
PaxDbiA0FGR8.
PRIDEiA0FGR8.

PTM databases

iPTMnetiA0FGR8.
PhosphoSitePlusiA0FGR8.
SwissPalmiA0FGR8.

Expressioni

Tissue specificityi

Widely expressed with high level in cerebellum.1 Publication

Gene expression databases

BgeeiENSG00000117868.
CleanExiHS_FAM62B.
ExpressionAtlasiA0FGR8. baseline and differential.
GenevisibleiA0FGR8. HS.

Organism-specific databases

HPAiHPA002132.

Interactioni

Subunit structurei

Homodimer. Interacts with ESYT1 and ESYT3. Interacts with FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2 complex; identified in a complex with the AP-2 complex and FGFR1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-3184170,EBI-3184170
ESYT1Q9BSJ84EBI-3184170,EBI-355956
ESYT3A0FGR93EBI-3184170,EBI-8771391

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi121556. 28 interactors.
DIPiDIP-61039N.
IntActiA0FGR8. 17 interactors.
MINTiMINT-4541681.
STRINGi9606.ENSP00000251527.

Structurei

Secondary structure

1921
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi196 – 219Combined sources24
Helixi221 – 226Combined sources6
Helixi230 – 232Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi248 – 255Combined sources8
Beta strandi264 – 282Combined sources19
Turni283 – 286Combined sources4
Beta strandi287 – 304Combined sources18
Beta strandi316 – 323Combined sources8
Beta strandi326 – 333Combined sources8
Helixi334 – 337Combined sources4
Turni341 – 345Combined sources5
Helixi348 – 358Combined sources11
Beta strandi365 – 370Combined sources6
Helixi372 – 379Combined sources8
Beta strandi384 – 396Combined sources13
Turni405 – 407Combined sources3
Beta strandi414 – 420Combined sources7
Beta strandi423 – 426Combined sources4
Beta strandi437 – 446Combined sources10
Beta strandi453 – 460Combined sources8
Beta strandi463 – 465Combined sources3
Beta strandi467 – 475Combined sources9
Helixi476 – 482Combined sources7
Beta strandi483 – 490Combined sources8
Beta strandi494 – 496Combined sources3
Beta strandi498 – 512Combined sources15
Helixi515 – 524Combined sources10
Beta strandi535 – 547Combined sources13
Beta strandi552 – 554Combined sources3
Beta strandi560 – 566Combined sources7
Beta strandi569 – 572Combined sources4
Beta strandi583 – 593Combined sources11
Turni595 – 597Combined sources3
Beta strandi599 – 606Combined sources8
Turni607 – 609Combined sources3
Beta strandi612 – 619Combined sources8
Helixi621 – 624Combined sources4
Helixi627 – 629Combined sources3
Beta strandi630 – 636Combined sources7
Beta strandi638 – 640Combined sources3
Beta strandi645 – 656Combined sources12
Beta strandi789 – 797Combined sources9
Turni798 – 801Combined sources4
Beta strandi802 – 811Combined sources10
Beta strandi823 – 831Combined sources9
Beta strandi835 – 837Combined sources3
Beta strandi851 – 858Combined sources8
Helixi862 – 867Combined sources6
Beta strandi869 – 876Combined sources8
Beta strandi889 – 894Combined sources6
Turni899 – 902Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DMGNMR-A785-913[»]
4NPJX-ray2.10A/B363-660[»]
4NPKX-ray2.55A363-660[»]
4P42X-ray2.44A/B191-662[»]
ProteinModelPortaliA0FGR8.
SMRiA0FGR8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0FGR8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini372 – 473C2 1PROSITE-ProRule annotationAdd BLAST102
Domaini523 – 617C2 2PROSITE-ProRule annotationAdd BLAST95
Domaini788 – 892C2 3PROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni195 – 370Glycerophospholipid-binding barrel-like domainAdd BLAST176
Regioni833 – 840Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi736 – 739Poly-Ser4

Domaini

Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic.1 Publication
The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium (PubMed:24373768). The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for location at the cell membrane (PubMed:23791178).2 Publications
Contains a barrel-like domain that binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol (PubMed:24847877).1 Publication

Sequence similaritiesi

Belongs to the extended synaptotagmin family.Curated
Contains 3 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410ISCC. Eukaryota.
ENOG410XPR4. LUCA.
GeneTreeiENSGT00550000074417.
HOVERGENiHBG055795.
InParanoidiA0FGR8.
PhylomeDBiA0FGR8.
TreeFamiTF324255.

Family and domain databases

Gene3Di2.60.40.150. 3 hits.
InterProiIPR000008. C2_dom.
IPR031468. SMP_LBD.
[Graphical view]
PfamiPF00168. C2. 3 hits.
PF17047. SMP_LBD. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 3 hits.
PROSITEiPS50004. C2. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A0FGR8-1) [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
MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS
60 70 80 90 100
HAPGSRLGAR RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN
110 120 130 140 150
PGGVLSVELP GLLAQLARSF ALLLPVYALG YLGLSFSWVL LALALLAWCR
160 170 180 190 200
RSRGLKALRL CRALALLEDE ERVVRLGVRA CDLPAWVHFP DTERAEWLNK
210 220 230 240 250
TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV DVGQQPLRIN
260 270 280 290 300
GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM
310 320 330 340 350
RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI
360 370 380 390 400
ILDIISNYLV LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK
410 420 430 440 450
DTYLKGLVKG KSDPYGIIRV GNQIFQSRVI KENLSPKWNE VYEALVYEHP
460 470 480 490 500
GQELEIELFD EDPDKDDFLG SLMIDLIEVE KERLLDEWFT LDEVPKGKLH
510 520 530 540 550
LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL YLDSARNLPS
560 570 580 590 600
GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL
610 620 630 640 650
EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI
660 670 680 690 700
ALRVLHLEKR ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN
710 720 730 740 750
TAPSTPVIGG SDKPGMEEKA QPPEAGPQGL HDLGRSSSSL LASPGHISVK
760 770 780 790 800
EPTPSIASDI SLPIATQELR QRLRQLENGT TLGQSPLGQI QLTIRHSSQR
810 820 830 840 850
NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK THVSKKTLNP
860 870 880 890 900
VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL
910 920
AKGWTQWYDL TEDGTRPQAM T
Length:921
Mass (Da):102,357
Last modified:November 28, 2006 - v1
Checksum:iD57F1BD9BB0A0C8A
GO
Isoform 2 (identifier: A0FGR8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: MTANRDAALS...RAPSPPRPGG → MTPPSRAEAG...GAGGAGGRAA

Note: No experimental confirmation available.
Show »
Length:893
Mass (Da):98,902
Checksum:i9C059B137A2F1EFB
GO
Isoform 4 (identifier: A0FGR8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.
     706-731: PVIGGSDKPGMEEKAQPPEAGPQGLH → SQSRSRPPASPRTSRCPSPPRSCGKG
     732-921: Missing.

Note: No experimental confirmation available.
Show »
Length:527
Mass (Da):59,403
Checksum:iE4257349511C9C28
GO
Isoform 5 (identifier: A0FGR8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-593: Missing.
     594-603: NPKRQDLEVE → MPVLPPCVLQ

Note: No experimental confirmation available.
Show »
Length:328
Mass (Da):35,846
Checksum:iEF531CFF2A35D17C
GO
Isoform 6 (identifier: A0FGR8-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: S → SNPLEFNPDVLKKTAVQRALKS

Note: No experimental confirmation available.
Show »
Length:942
Mass (Da):104,708
Checksum:i207D6C010DB58248
GO

Sequence cautioni

The sequence BAA91539 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC85769 differs from that shown. Reason: Frameshift at position 800.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti141L → V in CAH10642 (PubMed:17974005).Curated1
Sequence conflicti612S → P in BAC85769 (PubMed:14702039).Curated1
Sequence conflicti615N → S in BAC86489 (PubMed:14702039).Curated1
Sequence conflicti795R → Q in BAC85769 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030725210C → S.Corresponds to variant rs13233513dbSNPEnsembl.1
Natural variantiVAR_030726638S → G.1 PublicationCorresponds to variant rs2305473dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0232361 – 593Missing in isoform 5. 1 PublicationAdd BLAST593
Alternative sequenceiVSP_0232381 – 204Missing in isoform 4. 1 PublicationAdd BLAST204
Alternative sequenceiVSP_0232391 – 97MTANR…PRPGG → MTPPSRAEAGVRRSRVPSEG RWRGAEPPGISASTQPASAG RAARHCGAMSGARGEGPEAG AGGAGGRAA in isoform 2. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_038324550S → SNPLEFNPDVLKKTAVQRAL KS in isoform 6. 1 Publication1
Alternative sequenceiVSP_023240594 – 603NPKRQDLEVE → MPVLPPCVLQ in isoform 5. 1 Publication10
Alternative sequenceiVSP_023241706 – 731PVIGG…PQGLH → SQSRSRPPASPRTSRCPSPP RSCGKG in isoform 4. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_023242732 – 921Missing in isoform 4. 1 PublicationAdd BLAST190

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ993201 mRNA. Translation: ABJ97706.1.
AY368150 mRNA. Translation: AAR89381.1.
AK001181 mRNA. Translation: BAA91539.1. Different initiation.
AK124091 mRNA. Translation: BAC85769.1. Frameshift.
AK126214 mRNA. Translation: BAC86489.1.
CH236954 Genomic DNA. Translation: EAL23931.1.
AB033054 mRNA. Translation: BAA86542.2.
AL833233 mRNA. Translation: CAH10642.1.
BC013957 mRNA. Translation: AAH13957.2.
AJ303365 mRNA. Translation: CAC33887.1.
CCDSiCCDS34791.1. [A0FGR8-2]
RefSeqiNP_065779.1. NM_020728.2. [A0FGR8-2]
UniGeneiHs.490795.

Genome annotation databases

EnsembliENST00000251527; ENSP00000251527; ENSG00000117868. [A0FGR8-2]
GeneIDi57488.
KEGGihsa:57488.
UCSCiuc003wob.2. human. [A0FGR8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ993201 mRNA. Translation: ABJ97706.1.
AY368150 mRNA. Translation: AAR89381.1.
AK001181 mRNA. Translation: BAA91539.1. Different initiation.
AK124091 mRNA. Translation: BAC85769.1. Frameshift.
AK126214 mRNA. Translation: BAC86489.1.
CH236954 Genomic DNA. Translation: EAL23931.1.
AB033054 mRNA. Translation: BAA86542.2.
AL833233 mRNA. Translation: CAH10642.1.
BC013957 mRNA. Translation: AAH13957.2.
AJ303365 mRNA. Translation: CAC33887.1.
CCDSiCCDS34791.1. [A0FGR8-2]
RefSeqiNP_065779.1. NM_020728.2. [A0FGR8-2]
UniGeneiHs.490795.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DMGNMR-A785-913[»]
4NPJX-ray2.10A/B363-660[»]
4NPKX-ray2.55A363-660[»]
4P42X-ray2.44A/B191-662[»]
ProteinModelPortaliA0FGR8.
SMRiA0FGR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121556. 28 interactors.
DIPiDIP-61039N.
IntActiA0FGR8. 17 interactors.
MINTiMINT-4541681.
STRINGi9606.ENSP00000251527.

Protein family/group databases

TCDBi9.A.57.1.2. the extended-synaptotagmin (e-syt) family.

PTM databases

iPTMnetiA0FGR8.
PhosphoSitePlusiA0FGR8.
SwissPalmiA0FGR8.

Polymorphism and mutation databases

BioMutaiESYT2.

Proteomic databases

EPDiA0FGR8.
MaxQBiA0FGR8.
PaxDbiA0FGR8.
PRIDEiA0FGR8.

Protocols and materials databases

DNASUi57488.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251527; ENSP00000251527; ENSG00000117868. [A0FGR8-2]
GeneIDi57488.
KEGGihsa:57488.
UCSCiuc003wob.2. human. [A0FGR8-1]

Organism-specific databases

CTDi57488.
GeneCardsiESYT2.
H-InvDBHIX0007266.
HGNCiHGNC:22211. ESYT2.
HPAiHPA002132.
neXtProtiNX_A0FGR8.
OpenTargetsiENSG00000117868.
PharmGKBiPA165617947.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ISCC. Eukaryota.
ENOG410XPR4. LUCA.
GeneTreeiENSGT00550000074417.
HOVERGENiHBG055795.
InParanoidiA0FGR8.
PhylomeDBiA0FGR8.
TreeFamiTF324255.

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSiESYT2. human.
EvolutionaryTraceiA0FGR8.
GeneWikiiFAM62B.
GenomeRNAii57488.
PROiA0FGR8.

Gene expression databases

BgeeiENSG00000117868.
CleanExiHS_FAM62B.
ExpressionAtlasiA0FGR8. baseline and differential.
GenevisibleiA0FGR8. HS.

Family and domain databases

Gene3Di2.60.40.150. 3 hits.
InterProiIPR000008. C2_dom.
IPR031468. SMP_LBD.
[Graphical view]
PfamiPF00168. C2. 3 hits.
PF17047. SMP_LBD. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 3 hits.
PROSITEiPS50004. C2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiESYT2_HUMAN
AccessioniPrimary (citable) accession number: A0FGR8
Secondary accession number(s): A4D229
, Q69YJ2, Q6UKI4, Q6ZTU0, Q6ZVU1, Q9BQS0, Q9NW47, Q9ULJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: November 28, 2006
Last modified: November 2, 2016
This is version 102 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.