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Protein

E3 ubiquitin-protein ligase DZIP3

Gene

DZIP3

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

Functioni

E3 Ubiquitin ligase proteins mediate 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. Able to specifically bind RNA.1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1148 – 118841RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • phosphatase binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • polyubiquitin binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase DZIP3 (EC:6.3.2.-)
Alternative name(s):
DAZ-interacting protein 3
RNA-binding ubiquitin ligase of 138 kDa
Short name:
hRUL138
Gene namesi
Name:DZIP3
Synonyms:KIAA0675
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:30938. DZIP3.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi662 – 6665KKKTK → SGSTA: Strongly decreases RNA-binding activity. 1 Publication
Mutagenesisi1187 – 11871C → S: Abolishes ubiquitin ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA162384137.

Polymorphism and mutation databases

BioMutaiDZIP3.
DMDMi50400482.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12081208E3 ubiquitin-protein ligase DZIP3PRO_0000055898Add
BLAST

Proteomic databases

EPDiQ86Y13.
MaxQBiQ86Y13.
PaxDbiQ86Y13.
PRIDEiQ86Y13.

PTM databases

iPTMnetiQ86Y13.
PhosphoSiteiQ86Y13.

Expressioni

Tissue specificityi

Widely expressed at low level. Highly expressed in skeletal muscle, kidney and heart. Expressed at low level in placenta, lung, brain, liver and pancreas.1 Publication

Gene expression databases

BgeeiQ86Y13.
ExpressionAtlasiQ86Y13. baseline and differential.
GenevisibleiQ86Y13. HS.

Organism-specific databases

HPAiHPA035066.
HPA049232.

Interactioni

Subunit structurei

Interacts with DAZ proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AP1M1Q9BXS53EBI-948630,EBI-541426
ARHGAP32A7KAX93EBI-948630,EBI-308663
CEP63Q96MT83EBI-948630,EBI-741977
GTF2H2C_2Q6P1K83EBI-948630,EBI-8469755
HNRNPFP525973EBI-948630,EBI-352986
HNRNPUL1Q9BUJ23EBI-948630,EBI-1018153
RBM4BQ9BQ043EBI-948630,EBI-715531
TOLLIPQ9H0E22EBI-948630,EBI-74615
ZCCHC10Q8TBK63EBI-948630,EBI-597063
ZNF24P170283EBI-948630,EBI-707773
ZNF765Q7L2R63EBI-948630,EBI-9676069

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB
  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115021. 50 interactions.
IntActiQ86Y13. 41 interactions.
MINTiMINT-2867156.
STRINGi9606.ENSP00000355028.

Structurei

3D structure databases

ProteinModelPortaliQ86Y13.
SMRiQ86Y13. Positions 1137-1188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili14 – 4330Sequence analysisAdd
BLAST
Coiled coili647 – 67630Sequence analysisAdd
BLAST
Coiled coili792 – 85362Sequence analysisAdd
BLAST
Coiled coili904 – 93936Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi607 – 6104Poly-Glu
Compositional biasi661 – 67111Poly-LysAdd
BLAST
Compositional biasi952 – 9587Poly-Pro
Compositional biasi1140 – 11467Poly-Glu

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1148 – 118841RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFEY. Eukaryota.
ENOG410Y41H. LUCA.
GeneTreeiENSGT00530000063254.
HOVERGENiHBG051428.
InParanoidiQ86Y13.
KOiK10642.
OMAiRLCKYRD.
OrthoDBiEOG790G24.
PhylomeDBiQ86Y13.
TreeFamiTF333981.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033103. DZIP3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR22763:SF55. PTHR22763:SF55. 2 hits.
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86Y13-1) [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
MDSLPDEFFV RHPAVEDQRK EETENKLEKS SGQLNKQEND IPTDLVPVNL
60 70 80 90 100
LLEVKKLLNA INTLPKGVVP HIKKFLQEDF SFQTMQREVA ANSQNGEEIV
110 120 130 140 150
PALTLRFLIT QLEAALRNIQ AGNYTAHQIN IGYYLTLLFL YGVALTERGK
160 170 180 190 200
KEDYTEAENK FLVMKMMIQE NEICENFMSL VYFGRGLLRC AQKRYNGGLL
210 220 230 240 250
EFHKSLQEIG DKNDHWFDID PTEDEDLPTT FKDLLNNFIK TTESNIMKQT
260 270 280 290 300
ICSYLDCERS CEADILKNTS YKGFFQLMCS KSCCVYFHKI CWKKFKNLKY
310 320 330 340 350
PGENDQSFSG KKCLKEGCTG DMVRMLQCDV PGIVKILFEV VRKDEYITIE
360 370 380 390 400
NLGASYRKLI SLKITDTDIR PKISLKFNTK DEMPIFKLDY NYFYHLLHII
410 420 430 440 450
IISGTDIVRQ IFDEAMPPPL LKKELLIHKN VLESYYNHLW TNHPLGGSWH
460 470 480 490 500
LLYPPNKELP QSKQFDLCLL LALIKHLNVF PAPKKGWNME PPSSDISKSA
510 520 530 540 550
DILRLCKYRD ILLSEILMNG LTESQFNSIW KKVSDILLRL GMMQEDIDKV
560 570 580 590 600
KENPIENISL DYHQLSVYLG IPVPEIIQRM LSCYQQGIAL QSITGSQRIE
610 620 630 640 650
IEELQNEEEE LSPPLMEYNI NVKSHPEIQF AEINKDGTSI PSESSTESLK
660 670 680 690 700
DLQEVKSKQR KKKKTKNKKN KDSKEDQVPY VVEKEEQLRK EQANPHSVSR
710 720 730 740 750
LIKDDASDVQ EDSAMEDKFY SLDELHILDM IEQGSAGKVT TDYGETEKER
760 770 780 790 800
LARQRQLYKL HYQCEDFKRQ LRTVTFRWQE NQMQIKKKDK IIASLNQQVA
810 820 830 840 850
FGINKVSKLQ RQIHAKDNEI KNLKEQLSMK RSQWEMEKHN LESTMKTYVS
860 870 880 890 900
KLNAETSRAL TAEVYFLQCR RDFGLLHLEQ TEKECLNQLA RVTHMAASNL
910 920 930 940 950
ESLQLKAAVD SWNAIVADVR NKIAFLRTQY NEQINKVKQG FALSTLPPVQ
960 970 980 990 1000
LPPPPPSPEI LMQQFLGRPL VKESFFRPIL TVPQMPAVCP GVVSATGQPR
1010 1020 1030 1040 1050
APLMTGIAWA LPAPVGDAVP PSAGLRSDPS IMNWERITDR LKTAFPQQTR
1060 1070 1080 1090 1100
KELTDFLRKL KDAYGKSLSE LTFDEIVCKI SQFIDPKKSQ SQGKSVSNVN
1110 1120 1130 1140 1150
CVSPSHSPSQ PDAAQPPKPA WRPLTSQGPA TWEGASNPDE EEEEEEPCVI
1160 1170 1180 1190 1200
CHENLSPENL SVLPCAHKFH AQCIRPWLMQ QGTCPTCRLH VLLPEEFPGH

PSRQLPKI
Length:1,208
Mass (Da):138,604
Last modified:July 19, 2004 - v2
Checksum:i76945A63AF85207E
GO
Isoform 2 (identifier: Q86Y13-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     302-303: GE → EF
     304-1208: Missing.

Show »
Length:303
Mass (Da):35,240
Checksum:iAACC1AF978138456
GO

Sequence cautioni

The sequence AAH39018.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH56674.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAK69484.1 differs from that shown. Reason: Frameshift at position 1127. Curated
The sequence BAA31650.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681D → G in AAH56674 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei302 – 3032GE → EF in isoform 2. CuratedVSP_010971
Alternative sequencei304 – 1208905Missing in isoform 2. CuratedVSP_010972Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY227651 mRNA. Translation: AAO72967.1.
AY227652 mRNA. Translation: AAO72968.1.
AY227653 Transcribed RNA. Translation: AAO72969.1.
AY227654 mRNA. Translation: AAO72970.1.
AB014575 mRNA. Translation: BAA31650.2. Different initiation.
AK023138 mRNA. Translation: BAG51163.1.
BC039018 mRNA. Translation: AAH39018.1. Sequence problems.
BC056674 mRNA. Translation: AAH56674.1. Sequence problems.
BC063882 mRNA. Translation: AAH63882.1.
AF279370 mRNA. Translation: AAK69484.1. Frameshift.
CCDSiCCDS2952.1. [Q86Y13-1]
PIRiT00362.
RefSeqiNP_055463.1. NM_014648.3. [Q86Y13-1]
XP_005247971.1. XM_005247914.2. [Q86Y13-1]
XP_005247972.1. XM_005247915.2. [Q86Y13-1]
XP_005247973.1. XM_005247916.2. [Q86Y13-1]
XP_005247974.1. XM_005247917.2. [Q86Y13-1]
XP_005247975.1. XM_005247918.2. [Q86Y13-1]
UniGeneiHs.409210.

Genome annotation databases

EnsembliENST00000361582; ENSP00000355028; ENSG00000198919. [Q86Y13-1]
ENST00000463306; ENSP00000419981; ENSG00000198919. [Q86Y13-1]
ENST00000495008; ENSP00000418871; ENSG00000198919. [Q86Y13-2]
GeneIDi9666.
KEGGihsa:9666.
UCSCiuc003dxd.4. human. [Q86Y13-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY227651 mRNA. Translation: AAO72967.1.
AY227652 mRNA. Translation: AAO72968.1.
AY227653 Transcribed RNA. Translation: AAO72969.1.
AY227654 mRNA. Translation: AAO72970.1.
AB014575 mRNA. Translation: BAA31650.2. Different initiation.
AK023138 mRNA. Translation: BAG51163.1.
BC039018 mRNA. Translation: AAH39018.1. Sequence problems.
BC056674 mRNA. Translation: AAH56674.1. Sequence problems.
BC063882 mRNA. Translation: AAH63882.1.
AF279370 mRNA. Translation: AAK69484.1. Frameshift.
CCDSiCCDS2952.1. [Q86Y13-1]
PIRiT00362.
RefSeqiNP_055463.1. NM_014648.3. [Q86Y13-1]
XP_005247971.1. XM_005247914.2. [Q86Y13-1]
XP_005247972.1. XM_005247915.2. [Q86Y13-1]
XP_005247973.1. XM_005247916.2. [Q86Y13-1]
XP_005247974.1. XM_005247917.2. [Q86Y13-1]
XP_005247975.1. XM_005247918.2. [Q86Y13-1]
UniGeneiHs.409210.

3D structure databases

ProteinModelPortaliQ86Y13.
SMRiQ86Y13. Positions 1137-1188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115021. 50 interactions.
IntActiQ86Y13. 41 interactions.
MINTiMINT-2867156.
STRINGi9606.ENSP00000355028.

PTM databases

iPTMnetiQ86Y13.
PhosphoSiteiQ86Y13.

Polymorphism and mutation databases

BioMutaiDZIP3.
DMDMi50400482.

Proteomic databases

EPDiQ86Y13.
MaxQBiQ86Y13.
PaxDbiQ86Y13.
PRIDEiQ86Y13.

Protocols and materials databases

DNASUi9666.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361582; ENSP00000355028; ENSG00000198919. [Q86Y13-1]
ENST00000463306; ENSP00000419981; ENSG00000198919. [Q86Y13-1]
ENST00000495008; ENSP00000418871; ENSG00000198919. [Q86Y13-2]
GeneIDi9666.
KEGGihsa:9666.
UCSCiuc003dxd.4. human. [Q86Y13-1]

Organism-specific databases

CTDi9666.
GeneCardsiDZIP3.
HGNCiHGNC:30938. DZIP3.
HPAiHPA035066.
HPA049232.
MIMi608672. gene.
neXtProtiNX_Q86Y13.
PharmGKBiPA162384137.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFEY. Eukaryota.
ENOG410Y41H. LUCA.
GeneTreeiENSGT00530000063254.
HOVERGENiHBG051428.
InParanoidiQ86Y13.
KOiK10642.
OMAiRLCKYRD.
OrthoDBiEOG790G24.
PhylomeDBiQ86Y13.
TreeFamiTF333981.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiDZIP3. human.
GenomeRNAii9666.
NextBioi36295.
PROiQ86Y13.
SOURCEiSearch...

Gene expression databases

BgeeiQ86Y13.
ExpressionAtlasiQ86Y13. baseline and differential.
GenevisibleiQ86Y13. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033103. DZIP3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR22763:SF55. PTHR22763:SF55. 2 hits.
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "hRUL138, a novel human RNA-binding RING-H2 ubiquitin-protein ligase."
    Kreft S.G., Nassal M.
    J. Cell Sci. 116:605-616(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, TISSUE SPECIFICITY, MUTAGENESIS OF 662-LYS--LYS-666 AND CYS-1187.
    Tissue: Liver and Uterus.
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin and Testis.
  5. "Human Pumilio-2 is expressed in embryonic stem cells and germ cells and interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins."
    Moore F.L., Jaruzelska J., Fox M.S., Urano J., Firpo M.T., Turek P.J., Dorfman D.M., Reijo Pera R.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:538-543(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 641-1208, INTERACTION WITH DAZ.

Entry informationi

Entry nameiDZIP3_HUMAN
AccessioniPrimary (citable) accession number: Q86Y13
Secondary accession number(s): B3KN01
, O75162, Q6P3R9, Q6PH82, Q86Y14, Q86Y15, Q86Y16, Q8IWI0, Q96RS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 13, 2016
This is version 116 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. 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.