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Protein

WD repeat-containing protein 5

Gene

WDR5

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

Functioni

Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei107Important for interaction with histone H31
Sitei133Important for interaction with histone H31
Sitei263Important for interaction with histone H31
Sitei322Important for interaction with histone H31

GO - Molecular functioni

  • histone-lysine N-methyltransferase activity Source: Reactome
  • methylated histone binding Source: GO_Central

GO - Biological processi

  • histone H3 acetylation Source: BHF-UCL
  • histone H3-K4 methylation Source: UniProtKB
  • histone H4-K16 acetylation Source: UniProtKB
  • histone H4-K5 acetylation Source: UniProtKB
  • histone H4-K8 acetylation Source: UniProtKB
  • neuron projection development Source: Ensembl
  • positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • skeletal system development Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiP61964.
SIGNORiP61964.

Names & Taxonomyi

Protein namesi
Recommended name:
WD repeat-containing protein 5
Alternative name(s):
BMP2-induced 3-kb gene protein
Gene namesi
Name:WDR5
Synonyms:BIG3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12757. WDR5.

Subcellular locationi

GO - Cellular componenti

  • Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  • histone acetyltransferase complex Source: UniProtKB
  • histone methyltransferase complex Source: UniProtKB
  • MLL1 complex Source: UniProtKB
  • MLL3/4 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
  • Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47A → E: Strongly reduced affinity for histone H3. 1 Publication1
Mutagenesisi91S → F: Strongly reduced affinity for histone H3. 1 Publication1
Mutagenesisi107D → A or N: Strongly reduced affinity for histone H3. 2 Publications1
Mutagenesisi133F → A, D or L: Strongly reduced affinity for histone H3. 2 Publications1
Mutagenesisi263F → A or W: Strongly reduced affinity for histone H3. 1 Publication1
Mutagenesisi321L → A: Abolishes histone H3 binding. 1 Publication1
Mutagenesisi322E → A: Strongly reduced affinity for histone H3. 1 Publication1

Organism-specific databases

DisGeNETi11091.
OpenTargetsiENSG00000196363.
PharmGKBiPA37361.

Chemistry databases

ChEMBLiCHEMBL1075317.
GuidetoPHARMACOLOGYi2831.

Polymorphism and mutation databases

BioMutaiWDR5.
DMDMi48429182.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000513502 – 334WD repeat-containing protein 5Add BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei112N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP61964.
MaxQBiP61964.
PaxDbiP61964.
PeptideAtlasiP61964.
PRIDEiP61964.

PTM databases

iPTMnetiP61964.
PhosphoSitePlusiP61964.

Expressioni

Gene expression databases

BgeeiENSG00000196363.
CleanExiHS_WDR5.
ExpressionAtlasiP61964. baseline and differential.
GenevisibleiP61964. HS.

Organism-specific databases

HPAiHPA047182.

Interactioni

Subunit structurei

Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3. Interacts with HCFC1. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KMT2A/MLL1 and RBBP5; the interaction is direct. Component ofthe ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, MBIP and KAT14. Interacts with histone H3. Interacts with SETD1A. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with PER1.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9H8913EBI-540834,EBI-10218875
ArntlQ9WTL82EBI-540834,EBI-644534From a different organism.
C1orf104A2RRG23EBI-540834,EBI-10173042
CHD8Q9HCK83EBI-540834,EBI-1169146
FAM199XQ6PEV83EBI-540834,EBI-4280426
HCFC1P516105EBI-540834,EBI-396176
HIST1H3DP6843111EBI-540834,EBI-79722
HSF2Q039335EBI-540834,EBI-2556750
KANSL1Q7Z3B310EBI-540834,EBI-740244
KANSL2Q9H9L43EBI-540834,EBI-2560840
KAT6AQ927944EBI-540834,EBI-948013
KMT2AQ0316411EBI-540834,EBI-591370
KMT2BQ9UMN63EBI-540834,EBI-765774
KMT2CQ8NEZ44EBI-540834,EBI-1042997
MBIPQ9NS73-53EBI-540834,EBI-10182361
NCOA6Q146865EBI-540834,EBI-78670
PAXIP1Q6ZW498EBI-540834,EBI-743225
RBBP5Q1529112EBI-540834,EBI-592823
SSX2IPQ9Y2D83EBI-540834,EBI-2212028
TERF2IPQ9NYB02EBI-540834,EBI-750109
ZXDCQ2QGD73EBI-540834,EBI-1538838

GO - Molecular functioni

  • methylated histone binding Source: GO_Central

Protein-protein interaction databases

BioGridi116272. 164 interactors.
DIPiDIP-29223N.
IntActiP61964. 136 interactors.
MINTiMINT-1464227.
STRINGi9606.ENSP00000351446.

Chemistry databases

BindingDBiP61964.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 15Combined sources3
Beta strandi25 – 27Combined sources3
Beta strandi36 – 41Combined sources6
Beta strandi48 – 53Combined sources6
Beta strandi57 – 64Combined sources8
Beta strandi69 – 73Combined sources5
Turni74 – 76Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi90 – 95Combined sources6
Beta strandi99 – 106Combined sources8
Beta strandi109 – 115Combined sources7
Turni116 – 118Combined sources3
Beta strandi121 – 126Combined sources6
Beta strandi132 – 137Combined sources6
Beta strandi139 – 148Combined sources10
Beta strandi153 – 157Combined sources5
Turni158 – 160Combined sources3
Beta strandi163 – 167Combined sources5
Beta strandi174 – 179Combined sources6
Beta strandi183 – 190Combined sources8
Beta strandi195 – 199Combined sources5
Turni200 – 202Combined sources3
Beta strandi205 – 209Combined sources5
Beta strandi217 – 222Combined sources6
Beta strandi226 – 233Combined sources8
Turni234 – 236Combined sources3
Beta strandi237 – 242Combined sources6
Turni243 – 246Combined sources4
Beta strandi247 – 252Combined sources6
Beta strandi258 – 260Combined sources3
Beta strandi264 – 267Combined sources4
Beta strandi269 – 271Combined sources3
Beta strandi273 – 276Combined sources4
Beta strandi279 – 281Combined sources3
Beta strandi283 – 287Combined sources5
Turni288 – 290Combined sources3
Beta strandi293 – 297Combined sources5
Beta strandi304 – 309Combined sources6
Beta strandi311 – 320Combined sources10
Turni322 – 324Combined sources3
Beta strandi327 – 331Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CNXX-ray2.10A20-334[»]
2CO0X-ray2.25A/C20-334[»]
2G99X-ray1.90A/B27-334[»]
2G9AX-ray2.70A29-334[»]
2GNQX-ray1.80A1-334[»]
2H13X-ray1.58A22-334[»]
2H14X-ray1.48A22-334[»]
2H68X-ray1.79A/B23-334[»]
2H6KX-ray1.89A/B23-334[»]
2H6NX-ray1.50A/B23-334[»]
2H6QX-ray1.87A/B23-334[»]
2H9LX-ray1.75A24-334[»]
2H9MX-ray1.90A/C24-334[»]
2H9NX-ray2.00A/C24-334[»]
2H9PX-ray1.91A24-334[»]
2O9KX-ray1.90A/C24-334[»]
3EG6X-ray1.72A23-334[»]
3EMHX-ray1.37A25-334[»]
3MXXX-ray2.05A31-334[»]
3N0DX-ray2.30A31-334[»]
3N0EX-ray2.50A31-334[»]
3P4FX-ray2.35A22-334[»]
3PSLX-ray1.70A/B21-334[»]
3SMRX-ray1.82A/B/C/D24-334[»]
3UR4X-ray1.80A/B24-334[»]
3UVKX-ray1.40A21-334[»]
3UVLX-ray2.20A21-334[»]
3UVMX-ray1.57A21-334[»]
3UVNX-ray1.79A/C21-334[»]
3UVOX-ray2.20A21-334[»]
4A7JX-ray1.90A21-334[»]
4CY1X-ray1.50A/B23-334[»]
4CY2X-ray2.00A23-334[»]
4ERQX-ray1.91A/B/C23-334[»]
4ERYX-ray1.30A23-334[»]
4ERZX-ray1.75A/B/C23-334[»]
4ES0X-ray1.82A23-334[»]
4ESGX-ray1.70A/B23-334[»]
4EWRX-ray1.50A23-334[»]
4GM3X-ray3.39A/B/C/D/E/F/G/H22-334[»]
4GM8X-ray2.60A/B/C/D22-334[»]
4GM9X-ray2.10A/B22-334[»]
4GMBX-ray2.78A22-334[»]
4IA9X-ray1.66A24-334[»]
4O45X-ray1.87A24-334[»]
4QL1X-ray1.50A/B24-334[»]
4Y7RX-ray1.90A22-334[»]
5EALX-ray1.80A/B24-334[»]
5EAMX-ray1.80A/B24-334[»]
5EAPX-ray1.73A24-334[»]
5EARX-ray1.80A/B24-334[»]
5SXMX-ray2.00A/B23-334[»]
ProteinModelPortaliP61964.
SMRiP61964.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61964.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati43 – 82WD 1Add BLAST40
Repeati85 – 126WD 2Add BLAST42
Repeati128 – 168WD 3Add BLAST41
Repeati169 – 208WD 4Add BLAST40
Repeati212 – 253WD 5Add BLAST42
Repeati256 – 296WD 6Add BLAST41
Repeati299 – 333WD 7Add BLAST35

Sequence similaritiesi

Belongs to the WD repeat WDR5/wds family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0266. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000091642.
HOVERGENiHBG055117.
InParanoidiP61964.
KOiK14963.
OMAiCIKTLPA.
OrthoDBiEOG091G0CM2.
PhylomeDBiP61964.
TreeFamiTF314125.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS
60 70 80 90 100
VKFSPNGEWL ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN
110 120 130 140 150
LLVSASDDKT LKIWDVSSGK CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD
160 170 180 190 200
ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN RDGSLIVSSS YDGLCRIWDT
210 220 230 240 250
ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL WDYSKGKCLK
260 270 280 290 300
TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH
310 320 330
TDVVISTACH PTENIIASAA LENDKTIKLW KSDC
Length:334
Mass (Da):36,588
Last modified:June 7, 2004 - v1
Checksum:i4BF30914A2250286
GO

Sequence cautioni

The sequence CAB66159 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011376 mRNA. Translation: CAB66159.1. Different initiation.
AK000552 mRNA. Translation: BAA91248.1.
BC001635 mRNA. Translation: AAH01635.1.
CCDSiCCDS6981.1.
RefSeqiNP_060058.1. NM_017588.2.
NP_438172.1. NM_052821.3.
XP_005272220.1. XM_005272163.1.
UniGeneiHs.397638.

Genome annotation databases

EnsembliENST00000358625; ENSP00000351446; ENSG00000196363.
GeneIDi11091.
KEGGihsa:11091.
UCSCiuc004cey.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011376 mRNA. Translation: CAB66159.1. Different initiation.
AK000552 mRNA. Translation: BAA91248.1.
BC001635 mRNA. Translation: AAH01635.1.
CCDSiCCDS6981.1.
RefSeqiNP_060058.1. NM_017588.2.
NP_438172.1. NM_052821.3.
XP_005272220.1. XM_005272163.1.
UniGeneiHs.397638.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CNXX-ray2.10A20-334[»]
2CO0X-ray2.25A/C20-334[»]
2G99X-ray1.90A/B27-334[»]
2G9AX-ray2.70A29-334[»]
2GNQX-ray1.80A1-334[»]
2H13X-ray1.58A22-334[»]
2H14X-ray1.48A22-334[»]
2H68X-ray1.79A/B23-334[»]
2H6KX-ray1.89A/B23-334[»]
2H6NX-ray1.50A/B23-334[»]
2H6QX-ray1.87A/B23-334[»]
2H9LX-ray1.75A24-334[»]
2H9MX-ray1.90A/C24-334[»]
2H9NX-ray2.00A/C24-334[»]
2H9PX-ray1.91A24-334[»]
2O9KX-ray1.90A/C24-334[»]
3EG6X-ray1.72A23-334[»]
3EMHX-ray1.37A25-334[»]
3MXXX-ray2.05A31-334[»]
3N0DX-ray2.30A31-334[»]
3N0EX-ray2.50A31-334[»]
3P4FX-ray2.35A22-334[»]
3PSLX-ray1.70A/B21-334[»]
3SMRX-ray1.82A/B/C/D24-334[»]
3UR4X-ray1.80A/B24-334[»]
3UVKX-ray1.40A21-334[»]
3UVLX-ray2.20A21-334[»]
3UVMX-ray1.57A21-334[»]
3UVNX-ray1.79A/C21-334[»]
3UVOX-ray2.20A21-334[»]
4A7JX-ray1.90A21-334[»]
4CY1X-ray1.50A/B23-334[»]
4CY2X-ray2.00A23-334[»]
4ERQX-ray1.91A/B/C23-334[»]
4ERYX-ray1.30A23-334[»]
4ERZX-ray1.75A/B/C23-334[»]
4ES0X-ray1.82A23-334[»]
4ESGX-ray1.70A/B23-334[»]
4EWRX-ray1.50A23-334[»]
4GM3X-ray3.39A/B/C/D/E/F/G/H22-334[»]
4GM8X-ray2.60A/B/C/D22-334[»]
4GM9X-ray2.10A/B22-334[»]
4GMBX-ray2.78A22-334[»]
4IA9X-ray1.66A24-334[»]
4O45X-ray1.87A24-334[»]
4QL1X-ray1.50A/B24-334[»]
4Y7RX-ray1.90A22-334[»]
5EALX-ray1.80A/B24-334[»]
5EAMX-ray1.80A/B24-334[»]
5EAPX-ray1.73A24-334[»]
5EARX-ray1.80A/B24-334[»]
5SXMX-ray2.00A/B23-334[»]
ProteinModelPortaliP61964.
SMRiP61964.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116272. 164 interactors.
DIPiDIP-29223N.
IntActiP61964. 136 interactors.
MINTiMINT-1464227.
STRINGi9606.ENSP00000351446.

Chemistry databases

BindingDBiP61964.
ChEMBLiCHEMBL1075317.
GuidetoPHARMACOLOGYi2831.

PTM databases

iPTMnetiP61964.
PhosphoSitePlusiP61964.

Polymorphism and mutation databases

BioMutaiWDR5.
DMDMi48429182.

Proteomic databases

EPDiP61964.
MaxQBiP61964.
PaxDbiP61964.
PeptideAtlasiP61964.
PRIDEiP61964.

Protocols and materials databases

DNASUi11091.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358625; ENSP00000351446; ENSG00000196363.
GeneIDi11091.
KEGGihsa:11091.
UCSCiuc004cey.4. human.

Organism-specific databases

CTDi11091.
DisGeNETi11091.
GeneCardsiWDR5.
HGNCiHGNC:12757. WDR5.
HPAiHPA047182.
MIMi609012. gene.
neXtProtiNX_P61964.
OpenTargetsiENSG00000196363.
PharmGKBiPA37361.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0266. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000091642.
HOVERGENiHBG055117.
InParanoidiP61964.
KOiK14963.
OMAiCIKTLPA.
OrthoDBiEOG091G0CM2.
PhylomeDBiP61964.
TreeFamiTF314125.

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiP61964.
SIGNORiP61964.

Miscellaneous databases

EvolutionaryTraceiP61964.
GeneWikiiWDR5.
GenomeRNAii11091.
PROiP61964.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196363.
CleanExiHS_WDR5.
ExpressionAtlasiP61964. baseline and differential.
GenevisibleiP61964. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiWDR5_HUMAN
AccessioniPrimary (citable) accession number: P61964
Secondary accession number(s): Q91VA5, Q9NWX7, Q9UGP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: November 30, 2016
This is version 152 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.