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Protein

E3 ubiquitin-protein ligase RFWD2

Gene

RFWD2

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

Functioni

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation.7 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri136 – 174RING-typePROSITE-ProRule annotationAdd BLAST39

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: UniProtKB
  • ubiquitin-protein transferase activity Source: Reactome
  • zinc ion binding Source: InterPro

GO - Biological processi

  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143207-MONOMER.
ReactomeiR-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
SignaLinkiQ8NHY2.
SIGNORiQ8NHY2.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RFWD2 (EC:6.3.2.-)
Alternative name(s):
Constitutive photomorphogenesis protein 1 homolog
Short name:
hCOP1
RING finger and WD repeat domain protein 2
RING finger protein 200
Gene namesi
Name:RFWD2
Synonyms:COP1, RNF200
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17440. RFWD2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi111 – 113RKR → AKA: Abolishes localization to the nucleus. 1 Publication3
Mutagenesisi136C → A: Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-139. 4 Publications1
Mutagenesisi136C → S: Loss of SFN and MTA1 ubiquitination and degradation; when associated with S-139. Loss of stabilization by COPS6; when associated with S-139. 4 Publications1
Mutagenesisi139C → A: Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-136. 4 Publications1
Mutagenesisi139C → S: Loss of SFN and MTA1 ubiquitination and degradation; when associated with S-136. Loss of stabilization by COPS6; when associated with S-136. 4 Publications1
Mutagenesisi156C → S: Loss of MTA1 ubiquitination and degradation; when associated with S-159. 1 Publication1
Mutagenesisi159C → S: Loss of MTA1 ubiquitination and degradation; when associated with S-156. 1 Publication1

Organism-specific databases

DisGeNETi64326.
OpenTargetsiENSG00000143207.
PharmGKBiPA134952161.

Polymorphism and mutation databases

DMDMi55976539.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000558791 – 731E3 ubiquitin-protein ligase RFWD2Add BLAST731

Post-translational modificationi

Autoubiquitinated. MTA1 destabilizes it by promoting its autoubiquitination.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ8NHY2.
MaxQBiQ8NHY2.
PaxDbiQ8NHY2.
PeptideAtlasiQ8NHY2.
PRIDEiQ8NHY2.

PTM databases

iPTMnetiQ8NHY2.
PhosphoSitePlusiQ8NHY2.

Expressioni

Tissue specificityi

Ubiquitously expressed at low level. Expressed at higher level in testis, placenta, skeletal muscle and heart.2 Publications

Inductioni

By p53/TP53.1 Publication

Gene expression databases

BgeeiENSG00000143207.
CleanExiHS_RFWD2.
ExpressionAtlasiQ8NHY2. baseline and differential.
GenevisibleiQ8NHY2. HS.

Organism-specific databases

HPAiHPA028197.

Interactioni

Subunit structurei

Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another cullin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3. Interacts with bZIP transcription factors JUN, JUNB and JUND but not with FOS, ATF2 nor XBP1. Interacts with p53 (TP53). Interacts with COPS6; this interaction stabilizes RFWD2 through reducing its auto-ubiquitination and decelerating its turnover rate. Interacts with SFN; this interaction leads to SFN degradation. Isoform 4 forms heterodimers with isoform 1, preventing its association with DET1. Interacts with p53/TP53 and MTA1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COPS6Q7L5N13EBI-1176214,EBI-486838
ETS1P14921-13EBI-1176214,EBI-913224
ETS2P150362EBI-1176214,EBI-1646991
SFNP319476EBI-1176214,EBI-476295

Protein-protein interaction databases

BioGridi122136. 92 interactors.
DIPiDIP-36661N.
IntActiQ8NHY2. 25 interactors.
MINTiMINT-260162.
STRINGi9606.ENSP00000356641.

Structurei

Secondary structure

1731
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi392 – 399Combined sources8
Beta strandi404 – 412Combined sources9
Beta strandi424 – 429Combined sources6
Beta strandi433 – 440Combined sources8
Beta strandi443 – 449Combined sources7
Helixi450 – 453Combined sources4
Beta strandi464 – 468Combined sources5
Beta strandi473 – 478Combined sources6
Beta strandi485 – 490Combined sources6
Beta strandi495 – 499Combined sources5
Turni500 – 502Combined sources3
Beta strandi505 – 509Combined sources5
Beta strandi516 – 521Combined sources6
Beta strandi528 – 533Combined sources6
Beta strandi536 – 542Combined sources7
Beta strandi549 – 553Combined sources5
Beta strandi558 – 563Combined sources6
Beta strandi570 – 575Combined sources6
Beta strandi580 – 584Combined sources5
Beta strandi592 – 595Combined sources4
Beta strandi602 – 617Combined sources16
Turni618 – 620Combined sources3
Beta strandi621 – 626Combined sources6
Beta strandi633 – 636Combined sources4
Beta strandi642 – 644Combined sources3
Beta strandi648 – 651Combined sources4
Beta strandi654 – 658Combined sources5
Beta strandi662 – 668Combined sources7
Beta strandi676 – 679Combined sources4
Beta strandi700 – 705Combined sources6
Beta strandi709 – 711Combined sources3
Beta strandi715 – 720Combined sources6
Beta strandi723 – 731Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HQGX-ray2.00A376-731[»]
5IGQX-ray3.90A/B/C/D/E/F386-731[»]
ProteinModelPortaliQ8NHY2.
SMRiQ8NHY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati419 – 458WD 1Add BLAST40
Repeati468 – 508WD 2Add BLAST41
Repeati511 – 551WD 3Add BLAST41
Repeati553 – 593WD 4Add BLAST41
Repeati597 – 635WD 5Add BLAST39
Repeati638 – 677WD 6Add BLAST40
Repeati691 – 729WD 7Add BLAST39

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili233 – 301Sequence analysisAdd BLAST69

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi109 – 113Nuclear localization signal 15
Motifi195 – 206Nuclear localization signal 2Add BLAST12
Motifi235 – 245Nuclear export signalBy similarityAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 110Ser-richAdd BLAST109

Domaini

The RING finger domain, in addition to its role in ubiquitination, functions as a structural scaffold to bring two clusters of positive-charged residues within spatial proximity to mimic a bipartite nuclear localization signal (NLS).By similarity

Sequence similaritiesi

Belongs to the COP1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri136 – 174RING-typePROSITE-ProRule annotationAdd BLAST39

Keywords - Domaini

Coiled coil, Repeat, WD repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IE71. Eukaryota.
ENOG410XNTU. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000006123.
HOVERGENiHBG054995.
InParanoidiQ8NHY2.
KOiK10143.
OMAiFSTRMTR.
OrthoDBiEOG091G0ERB.
PhylomeDBiQ8NHY2.
TreeFamiTF328912.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR033313. RFWD2/COP1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR22847:SF451. PTHR22847:SF451. 2 hits.
PfamiPF00400. WD40. 5 hits.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8NHY2-1) [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
MSGSRQAGSG SAGTSPGSSA ASSVTSASSS LSSSPSPPSV AVSAAALVSG
60 70 80 90 100
GVAQAAGSGG LGGPVRPVLV APAVSGSGGG AVSTGLSRHS CAARPSAGVG
110 120 130 140 150
GSSSSLGSGS RKRPLLAPLC NGLINSYEDK SNDFVCPICF DMIEEAYMTK
160 170 180 190 200
CGHSFCYKCI HQSLEDNNRC PKCNYVVDNI DHLYPNFLVN ELILKQKQRF
210 220 230 240 250
EEKRFKLDHS VSSTNGHRWQ IFQDWLGTDQ DNLDLANVNL MLELLVQKKK
260 270 280 290 300
QLEAESHAAQ LQILMEFLKV ARRNKREQLE QIQKELSVLE EDIKRVEEMS
310 320 330 340 350
GLYSPVSEDS TVPQFEAPSP SHSSIIDSTE YSQPPGFSGS SQTKKQPWYN
360 370 380 390 400
STLASRRKRL TAHFEDLEQC YFSTRMSRIS DDSRTASQLD EFQECLSKFT
410 420 430 440 450
RYNSVRPLAT LSYASDLYNG SSIVSSIEFD RDCDYFAIAG VTKKIKVYEY
460 470 480 490 500
DTVIQDAVDI HYPENEMTCN SKISCISWSS YHKNLLASSD YEGTVILWDG
510 520 530 540 550
FTGQRSKVYQ EHEKRCWSVD FNLMDPKLLA SGSDDAKVKL WSTNLDNSVA
560 570 580 590 600
SIEAKANVCC VKFSPSSRYH LAFGCADHCV HYYDLRNTKQ PIMVFKGHRK
610 620 630 640 650
AVSYAKFVSG EEIVSASTDS QLKLWNVGKP YCLRSFKGHI NEKNFVGLAS
660 670 680 690 700
NGDYIACGSE NNSLYLYYKG LSKTLLTFKF DTVKSVLDKD RKEDDTNEFV
710 720 730
SAVCWRALPD GESNVLIAAN SQGTIKVLEL V
Length:731
Mass (Da):80,474
Last modified:October 1, 2002 - v1
Checksum:iC4B262268D01FA00
GO
Isoform 2 (identifier: Q8NHY2-2) [UniParc]FASTAAdd to basket
Also known as: delta24

The sequence of this isoform differs from the canonical sequence as follows:
     211-214: Missing.
     277-296: Missing.

Show »
Length:707
Mass (Da):77,691
Checksum:iF2FC1F37C42BDAE2
GO
Isoform 3 (identifier: Q8NHY2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-264: Missing.
     342-342: Q → QAGVQWRYLGSLQPPPPRYKRFSCLTLPSSWDYRRLPPHL

Note: No experimental confirmation available.
Show »
Length:506
Mass (Da):57,527
Checksum:i7B428234153E7490
GO
Isoform 4 (identifier: Q8NHY2-4) [UniParc]FASTAAdd to basket
Also known as: COP1D

The sequence of this isoform differs from the canonical sequence as follows:
     277-296: Missing.

Note: Unable to associate with other components of the CRL complex. Acts as a dominant-negative.
Show »
Length:711
Mass (Da):78,066
Checksum:i6E3E5405CD510EB8
GO
Isoform 5 (identifier: Q8NHY2-5) [UniParc]FASTAAdd to basket
Also known as: E

The sequence of this isoform differs from the canonical sequence as follows:
     157-157: Y → E
     158-731: Missing.

Show »
Length:157
Mass (Da):14,914
Checksum:i544697228ACBECC6
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0120261 – 264Missing in isoform 3. 1 PublicationAdd BLAST264
Alternative sequenceiVSP_055894157Y → E in isoform 5. 1 Publication1
Alternative sequenceiVSP_055895158 – 731Missing in isoform 5. 1 PublicationAdd BLAST574
Alternative sequenceiVSP_012024211 – 214Missing in isoform 2. 1 Publication4
Alternative sequenceiVSP_012025277 – 296Missing in isoform 2 and isoform 4. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_012027342Q → QAGVQWRYLGSLQPPPPRYK RFSCLTLPSSWDYRRLPPHL in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF508940 mRNA. Translation: AAM34692.1.
BK000438 Genomic DNA. Translation: DAA01050.1.
AF527539 mRNA. Translation: AAQ08989.1.
AY509921 mRNA. Translation: AAS82851.1.
KJ534928 mRNA. Translation: AHW56568.1.
KJ535076 mRNA. Translation: AHW56715.1.
AK025789 mRNA. Translation: BAB15239.1.
AK314750 mRNA. Translation: BAG37289.1.
AL359265
, AL162736, AL513329, AL590723 Genomic DNA. Translation: CAH71140.1.
AL513329
, AL162736, AL359265, AL590723 Genomic DNA. Translation: CAH72425.1.
AL162736
, AL359265, AL513329, AL590723 Genomic DNA. Translation: CAH73625.1.
AL590723
, AL162736, AL359265, AL513329 Genomic DNA. Translation: CAI14643.1.
CH471067 Genomic DNA. Translation: EAW91000.1.
BC094728 mRNA. Translation: AAH94728.1.
CCDSiCCDS30944.1. [Q8NHY2-1]
CCDS44279.1. [Q8NHY2-2]
RefSeqiNP_001001740.1. NM_001001740.3. [Q8NHY2-2]
NP_001273573.1. NM_001286644.1.
NP_071902.2. NM_022457.6. [Q8NHY2-1]
UniGeneiHs.523744.

Genome annotation databases

EnsembliENST00000308769; ENSP00000310943; ENSG00000143207. [Q8NHY2-2]
ENST00000367669; ENSP00000356641; ENSG00000143207. [Q8NHY2-1]
ENST00000474194; ENSP00000433517; ENSG00000143207. [Q8NHY2-5]
GeneIDi64326.
KEGGihsa:64326.
UCSCiuc001gku.3. human. [Q8NHY2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF508940 mRNA. Translation: AAM34692.1.
BK000438 Genomic DNA. Translation: DAA01050.1.
AF527539 mRNA. Translation: AAQ08989.1.
AY509921 mRNA. Translation: AAS82851.1.
KJ534928 mRNA. Translation: AHW56568.1.
KJ535076 mRNA. Translation: AHW56715.1.
AK025789 mRNA. Translation: BAB15239.1.
AK314750 mRNA. Translation: BAG37289.1.
AL359265
, AL162736, AL513329, AL590723 Genomic DNA. Translation: CAH71140.1.
AL513329
, AL162736, AL359265, AL590723 Genomic DNA. Translation: CAH72425.1.
AL162736
, AL359265, AL513329, AL590723 Genomic DNA. Translation: CAH73625.1.
AL590723
, AL162736, AL359265, AL513329 Genomic DNA. Translation: CAI14643.1.
CH471067 Genomic DNA. Translation: EAW91000.1.
BC094728 mRNA. Translation: AAH94728.1.
CCDSiCCDS30944.1. [Q8NHY2-1]
CCDS44279.1. [Q8NHY2-2]
RefSeqiNP_001001740.1. NM_001001740.3. [Q8NHY2-2]
NP_001273573.1. NM_001286644.1.
NP_071902.2. NM_022457.6. [Q8NHY2-1]
UniGeneiHs.523744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HQGX-ray2.00A376-731[»]
5IGQX-ray3.90A/B/C/D/E/F386-731[»]
ProteinModelPortaliQ8NHY2.
SMRiQ8NHY2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122136. 92 interactors.
DIPiDIP-36661N.
IntActiQ8NHY2. 25 interactors.
MINTiMINT-260162.
STRINGi9606.ENSP00000356641.

PTM databases

iPTMnetiQ8NHY2.
PhosphoSitePlusiQ8NHY2.

Polymorphism and mutation databases

DMDMi55976539.

Proteomic databases

EPDiQ8NHY2.
MaxQBiQ8NHY2.
PaxDbiQ8NHY2.
PeptideAtlasiQ8NHY2.
PRIDEiQ8NHY2.

Protocols and materials databases

DNASUi64326.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308769; ENSP00000310943; ENSG00000143207. [Q8NHY2-2]
ENST00000367669; ENSP00000356641; ENSG00000143207. [Q8NHY2-1]
ENST00000474194; ENSP00000433517; ENSG00000143207. [Q8NHY2-5]
GeneIDi64326.
KEGGihsa:64326.
UCSCiuc001gku.3. human. [Q8NHY2-1]

Organism-specific databases

CTDi64326.
DisGeNETi64326.
GeneCardsiRFWD2.
HGNCiHGNC:17440. RFWD2.
HPAiHPA028197.
MIMi608067. gene.
neXtProtiNX_Q8NHY2.
OpenTargetsiENSG00000143207.
PharmGKBiPA134952161.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE71. Eukaryota.
ENOG410XNTU. LUCA.
GeneTreeiENSGT00570000079069.
HOGENOMiHOG000006123.
HOVERGENiHBG054995.
InParanoidiQ8NHY2.
KOiK10143.
OMAiFSTRMTR.
OrthoDBiEOG091G0ERB.
PhylomeDBiQ8NHY2.
TreeFamiTF328912.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000143207-MONOMER.
ReactomeiR-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
SignaLinkiQ8NHY2.
SIGNORiQ8NHY2.

Miscellaneous databases

ChiTaRSiRFWD2. human.
GeneWikiiRFWD2.
GenomeRNAii64326.
PROiQ8NHY2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143207.
CleanExiHS_RFWD2.
ExpressionAtlasiQ8NHY2. baseline and differential.
GenevisibleiQ8NHY2. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR033313. RFWD2/COP1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR22847:SF451. PTHR22847:SF451. 2 hits.
PfamiPF00400. WD40. 5 hits.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRFWD2_HUMAN
AccessioniPrimary (citable) accession number: Q8NHY2
Secondary accession number(s): E9PKI0
, Q504W6, Q6H103, Q9H6L7, X5D9B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 138 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 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.