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Protein

X-ray repair cross-complementing protein 5

Gene

XRCC5

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

Functioni

Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:20383123). The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.5 Publications

Miscellaneous

Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC6 and XRCC5.1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • damaged DNA binding Source: InterPro
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: ProtInc
  • enzyme activator activity Source: BHF-UCL
  • protein-containing complex binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • telomeric DNA binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA recombination, DNA repair, Immunity, Innate immunity, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-164843 2-LTR circle formation
R-HSA-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-3270619 IRF3-mediated induction of type I IFN
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-6798695 Neutrophil degranulation
SIGNORiP13010

Protein family/group databases

MoonDBiP13010 Curated

Names & Taxonomyi

Protein namesi
Recommended name:
X-ray repair cross-complementing protein 5 (EC:3.6.4.-)
Alternative name(s):
86 kDa subunit of Ku antigen
ATP-dependent DNA helicase 2 subunit 2
ATP-dependent DNA helicase II 80 kDa subunit
CTC box-binding factor 85 kDa subunit
Short name:
CTC85
Short name:
CTCBF
DNA repair protein XRCC5
Ku80
Ku86
Lupus Ku autoantigen protein p86
Nuclear factor IV
Thyroid-lupus autoantigen
Short name:
TLAA
X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining)
Gene namesi
Name:XRCC5
Synonyms:G22P2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000079246.15
HGNCiHGNC:12833 XRCC5
MIMi194364 gene
neXtProtiNX_P13010

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi720 – 721EE → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. 1 Publication2
Mutagenesisi726 – 727DD → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. 1 Publication2

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

DisGeNETi7520
OpenTargetsiENSG00000079246
PharmGKBiPA37425

Polymorphism and mutation databases

BioMutaiXRCC5
DMDMi125731

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000843402 – 732X-ray repair cross-complementing protein 5Add BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei144N6-acetyllysineCombined sources1
Cross-linki195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei255PhosphoserineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei265N6-acetyllysineCombined sources1
Modified residuei318PhosphoserineCombined sources1
Modified residuei332N6-acetyllysineCombined sources1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei535PhosphothreonineCombined sources1
Cross-linki566Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei577Phosphoserine; by PRKDCCombined sources1 Publication1
Modified residuei579Phosphoserine; by PRKDC1 Publication1
Modified residuei580Phosphoserine; by PRKDC1 Publication1
Modified residuei660N6-acetyllysineCombined sources1
Modified residuei665N6-acetyllysineCombined sources1
Cross-linki669Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki688Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei715Phosphothreonine; by PRKDC1 Publication1

Post-translational modificationi

Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity.1 Publication
Sumoylated.1 Publication
Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites (PubMed:22266820). Ubiquitinated by RNF138, leading to remove the Ku complex from DNA breaks (PubMed:26502055).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP13010
MaxQBiP13010
PaxDbiP13010
PeptideAtlasiP13010
PRIDEiP13010
ProteomicsDBi52890

2D gel databases

SWISS-2DPAGEiP13010

PTM databases

iPTMnetiP13010
PhosphoSitePlusiP13010
SwissPalmiP13010

Miscellaneous databases

PMAP-CutDBiP13010

Expressioni

Developmental stagei

Expression increases during promyelocyte differentiation.1 Publication

Inductioni

In osteoblasts, by FGF2.

Gene expression databases

BgeeiENSG00000079246 Expressed in 232 organ(s), highest expression level in kidney
CleanExiHS_XRCC5
ExpressionAtlasiP13010 baseline and differential
GenevisibleiP13010 HS

Organism-specific databases

HPAiCAB004468
HPA025813
HPA064685

Interactioni

Subunit structurei

Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex (PubMed:25941166, PubMed:25670504, PubMed:11493912, PubMed:22442688). Additional components of the NHEJ complex include NHEJ1/XLF and PAXX (PubMed:25574025, PubMed:25941166, PubMed:25670504). The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE) (PubMed:12145306). In addition, XRCC5 binds to the osteoblast-specific transcription factors MSX2 and RUNX2 (PubMed:12145306). Interacts with ELF3 (PubMed:15075319). May interact with APLF (PubMed:17353262, PubMed:17396150). The XRCC5/XRCC6 dimer associates in a DNA-dependent manner with APEX1 (PubMed:8621488). Identified in a complex with DEAF1 and XRCC6. Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation (PubMed:25852083). Interacts with RNF138 (PubMed:26502055). Interacts with CYREN isoform 1 (CYREN-1) and isoform 4 (CYREN-2) (PubMed:24610814, PubMed:28959974). Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction is direct and prevents XRCC5/XRCC6 heterodimeric binding and non-homologous end joining (NHEJ) repair activities induced by ionizing radiation (IR) (PubMed:26359349). Interacts with DHX9; this interaction occurs in a RNA-dependent manner (PubMed:14704337). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728).17 Publications
(Microbial infection) Interacts with human T-cell leukemia virus 1/HTLV-1 protein HBZ.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113353, 247 interactors
ComplexPortaliCPX-1993 Ku70:Ku80 complex
CORUMiP13010
DIPiDIP-31379N
ELMiP13010
IntActiP13010, 113 interactors
MINTiP13010
STRINGi9606.ENSP00000375977

Structurei

Secondary structure

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP13010
SMRiP13010
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13010

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini251 – 460KuAdd BLAST210

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni138 – 165Leucine-zipperAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi720 – 728EEXXXDL motif9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi478 – 519Pro-richAdd BLAST42

Domaini

The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.1 Publication

Sequence similaritiesi

Belongs to the ku80 family.Curated

Phylogenomic databases

eggNOGiKOG2326 Eukaryota
ENOG410YKH9 LUCA
GeneTreeiENSGT00390000015674
HOVERGENiHBG006237
InParanoidiP13010
KOiK10885
OMAiYRFPPLD
OrthoDBiEOG091G11VD
PhylomeDBiP13010
TreeFamiTF101205

Family and domain databases

Gene3Di1.25.40.240, 1 hit
2.40.290.10, 1 hit
3.40.50.410, 1 hit
InterProiView protein in InterPro
IPR006164 Ku70/Ku80_beta-barrel_dom
IPR024193 Ku80
IPR005160 Ku_C
IPR036494 Ku_C_sf
IPR005161 Ku_N
IPR014893 Ku_PK_bind
IPR016194 SPOC-like_C_dom_sf
IPR002035 VWF_A
IPR036465 vWFA_dom_sf
PANTHERiPTHR12604:SF4 PTHR12604:SF4, 1 hit
PfamiView protein in Pfam
PF02735 Ku, 1 hit
PF03730 Ku_C, 1 hit
PF03731 Ku_N, 1 hit
PF08785 Ku_PK_bind, 1 hit
PIRSFiPIRSF016570 Ku80, 1 hit
SMARTiView protein in SMART
SM00559 Ku78, 1 hit
SM00327 VWA, 1 hit
SUPFAMiSSF100939 SSF100939, 1 hit
SSF101420 SSF101420, 1 hit
SSF53300 SSF53300, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P13010-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN
60 70 80 90 100
KDEIALVLFG TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP
110 120 130 140 150
GSQQADFLDA LIVSMDVIQH ETIGKKFEKR HIEIFTDLSS RFSKSQLDII
160 170 180 190 200
IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD GPFRLGGHGP SFPLKGITEQ
210 220 230 240 250
QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI ERHSIHWPCR
260 270 280 290 300
LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD
310 320 330 340 350
DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ
360 370 380 390 400
VQRRFFMGNQ VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR
410 420 430 440 450
ANPQVGVAFP HIKHNYECLV YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ
460 470 480 490 500
LNAVDALIDS MSLAKKDEKT DTLEDLFPTT KIPNPRFQRL FQCLLHRALH
510 520 530 540 550
PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI EAKKKDQVTA
560 570 580 590 600
QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV
610 620 630 640 650
LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS
660 670 680 690 700
EEQRFNNFLK ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE
710 720 730
AKKFLAPKDK PSGDTAAVFE EGGDVDDLLD MI
Length:732
Mass (Da):82,705
Last modified:January 23, 2007 - v3
Checksum:i2363CA84834E74A3
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JZ81C9JZ81_HUMAN
X-ray repair cross-complementing pr...
XRCC5
131Annotation score:
H7C0H9H7C0H9_HUMAN
X-ray repair cross-complementing pr...
XRCC5
19Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 16MDV → YSY AA sequence (PubMed:8605992).Curated3
Sequence conflicti117V → A in BAF83429 (PubMed:14702039).Curated1
Sequence conflicti134I → V in BAD96323 (Ref. 4) Curated1
Sequence conflicti178R → S in BAD96323 (Ref. 4) Curated1
Sequence conflicti315R → L in CAA40736 (PubMed:2212941).Curated1
Sequence conflicti461M → R AA sequence (PubMed:8605992).Curated1
Sequence conflicti479T → G AA sequence (PubMed:8605992).Curated1
Sequence conflicti540I → T in BAF83429 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014724463L → F. Corresponds to variant dbSNP:rs1805380Ensembl.1
Natural variantiVAR_053784508I → V. Corresponds to variant dbSNP:rs2287558Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04977 mRNA Translation: AAA59475.1
M30938 mRNA Translation: AAA36154.1
AK290740 mRNA Translation: BAF83429.1
AK222603 mRNA Translation: BAD96323.1
DQ787434 Genomic DNA Translation: ABG46942.1
CH471063 Genomic DNA Translation: EAW70562.1
BC019027 mRNA Translation: AAH19027.1
BC095442 mRNA Translation: AAH95442.1
X57500 mRNA Translation: CAA40736.1
CCDSiCCDS2402.1
PIRiA35051 A32626
D42397
S62889
RefSeqiNP_066964.1, NM_021141.3
UniGeneiHs.388739

Genome annotation databases

EnsembliENST00000392132; ENSP00000375977; ENSG00000079246
ENST00000392133; ENSP00000375978; ENSG00000079246
GeneIDi7520
KEGGihsa:7520
UCSCiuc002vfy.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

NIEHS SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04977 mRNA Translation: AAA59475.1
M30938 mRNA Translation: AAA36154.1
AK290740 mRNA Translation: BAF83429.1
AK222603 mRNA Translation: BAD96323.1
DQ787434 Genomic DNA Translation: ABG46942.1
CH471063 Genomic DNA Translation: EAW70562.1
BC019027 mRNA Translation: AAH19027.1
BC095442 mRNA Translation: AAH95442.1
X57500 mRNA Translation: CAA40736.1
CCDSiCCDS2402.1
PIRiA35051 A32626
D42397
S62889
RefSeqiNP_066964.1, NM_021141.3
UniGeneiHs.388739

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70B1-565[»]
1JEYX-ray2.50B1-565[»]
1Q2ZNMR-A590-709[»]
1RW2NMR-A566-710[»]
3RZ9X-ray2.29B559-571[»]
5Y3Relectron microscopy6.60B6-541[»]
ProteinModelPortaliP13010
SMRiP13010
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113353, 247 interactors
ComplexPortaliCPX-1993 Ku70:Ku80 complex
CORUMiP13010
DIPiDIP-31379N
ELMiP13010
IntActiP13010, 113 interactors
MINTiP13010
STRINGi9606.ENSP00000375977

Protein family/group databases

MoonDBiP13010 Curated

PTM databases

iPTMnetiP13010
PhosphoSitePlusiP13010
SwissPalmiP13010

Polymorphism and mutation databases

BioMutaiXRCC5
DMDMi125731

2D gel databases

SWISS-2DPAGEiP13010

Proteomic databases

EPDiP13010
MaxQBiP13010
PaxDbiP13010
PeptideAtlasiP13010
PRIDEiP13010
ProteomicsDBi52890

Protocols and materials databases

DNASUi7520
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392132; ENSP00000375977; ENSG00000079246
ENST00000392133; ENSP00000375978; ENSG00000079246
GeneIDi7520
KEGGihsa:7520
UCSCiuc002vfy.4 human

Organism-specific databases

CTDi7520
DisGeNETi7520
EuPathDBiHostDB:ENSG00000079246.15
GeneCardsiXRCC5
HGNCiHGNC:12833 XRCC5
HPAiCAB004468
HPA025813
HPA064685
MIMi194364 gene
neXtProtiNX_P13010
OpenTargetsiENSG00000079246
PharmGKBiPA37425
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2326 Eukaryota
ENOG410YKH9 LUCA
GeneTreeiENSGT00390000015674
HOVERGENiHBG006237
InParanoidiP13010
KOiK10885
OMAiYRFPPLD
OrthoDBiEOG091G11VD
PhylomeDBiP13010
TreeFamiTF101205

Enzyme and pathway databases

ReactomeiR-HSA-164843 2-LTR circle formation
R-HSA-1834949 Cytosolic sensors of pathogen-associated DNA
R-HSA-3270619 IRF3-mediated induction of type I IFN
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-6798695 Neutrophil degranulation
SIGNORiP13010

Miscellaneous databases

ChiTaRSiXRCC5 human
EvolutionaryTraceiP13010
GeneWikiiKu80
GenomeRNAii7520
PMAP-CutDBiP13010
PROiPR:P13010
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000079246 Expressed in 232 organ(s), highest expression level in kidney
CleanExiHS_XRCC5
ExpressionAtlasiP13010 baseline and differential
GenevisibleiP13010 HS

Family and domain databases

Gene3Di1.25.40.240, 1 hit
2.40.290.10, 1 hit
3.40.50.410, 1 hit
InterProiView protein in InterPro
IPR006164 Ku70/Ku80_beta-barrel_dom
IPR024193 Ku80
IPR005160 Ku_C
IPR036494 Ku_C_sf
IPR005161 Ku_N
IPR014893 Ku_PK_bind
IPR016194 SPOC-like_C_dom_sf
IPR002035 VWF_A
IPR036465 vWFA_dom_sf
PANTHERiPTHR12604:SF4 PTHR12604:SF4, 1 hit
PfamiView protein in Pfam
PF02735 Ku, 1 hit
PF03730 Ku_C, 1 hit
PF03731 Ku_N, 1 hit
PF08785 Ku_PK_bind, 1 hit
PIRSFiPIRSF016570 Ku80, 1 hit
SMARTiView protein in SMART
SM00559 Ku78, 1 hit
SM00327 VWA, 1 hit
SUPFAMiSSF100939 SSF100939, 1 hit
SSF101420 SSF101420, 1 hit
SSF53300 SSF53300, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXRCC5_HUMAN
AccessioniPrimary (citable) accession number: P13010
Secondary accession number(s): A8K3X5
, Q0Z7V0, Q4VBQ5, Q53HH7, Q7M4N0, Q9UCQ0, Q9UCQ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 215 of the entry and version 3 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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