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Protein

Ectoderm-neural cortex protein 1

Gene

ENC1

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

Functioni

Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. Down-regulates transcription factor NF2L2/NRF2 by decreasing the rate of protein synthesis and not via a ubiquitin-mediated proteasomal degradation mechanism.1 Publication

GO - Biological processi

  • multicellular organism development Source: ProtInc
  • negative regulation of translation Source: UniProtKB
  • nervous system development Source: ProtInc
  • positive regulation of neuron projection development Source: Ensembl
  • proteasomal ubiquitin-independent protein catabolic process Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ectoderm-neural cortex protein 1
Short name:
ENC-1
Alternative name(s):
Kelch-like protein 37
Nuclear matrix protein NRP/B
p53-induced gene 10 protein
Gene namesi
Name:ENC1
Synonyms:KLHL37, NRPB, PIG10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3345. ENC1.

Subcellular locationi

  • Nucleus matrix 1 Publication
  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • neuronal cell body Source: Ensembl
  • nuclear chromatin Source: Ensembl
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleolus Source: Ensembl
  • nucleoplasm Source: Ensembl
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27782.

Polymorphism and mutation databases

BioMutaiENC1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Ectoderm-neural cortex protein 1PRO_0000119068Add
BLAST

Post-translational modificationi

Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiO14682.
PaxDbiO14682.
PeptideAtlasiO14682.
PRIDEiO14682.

PTM databases

iPTMnetiO14682.
PhosphoSiteiO14682.

Expressioni

Tissue specificityi

Detected in fetal brain tissue, moderate expression in fetal heart, lung and kidney. Highly expressed in adult brain, particularly high in the hippocampus and amygdala, and spinal chord. Detectable in adult pancreas. May be down-regulated in neuroblastoma tumors.

Developmental stagei

Dramatically up-regulated upon neuronal differentiation.

Inductioni

By p53/TP53.1 Publication

Gene expression databases

BgeeiO14682.
CleanExiHS_ENC1.
ExpressionAtlasiO14682. baseline and differential.
GenevisibleiO14682. HS.

Organism-specific databases

HPAiHPA030726.

Interactioni

Subunit structurei

Binds to RB1. Hypophosphorylated RB1 associates with ENC1 during neuronal differentiation, while hyperphosphorylated RB1 associates with ENC1 in undifferentiating cells. Part of a complex that contains CUL3, RBX1 and ENC1. Interacts indirectly with KEAP1.2 Publications

Protein-protein interaction databases

BioGridi114079. 14 interactions.
IntActiO14682. 1 interaction.
STRINGi9606.ENSP00000306356.

Structurei

3D structure databases

ProteinModelPortaliO14682.
SMRiO14682. Positions 23-270, 277-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 11469BTBPROSITE-ProRule annotationAdd
BLAST
Repeati296 – 34045Kelch 1Add
BLAST
Repeati341 – 38848Kelch 2Add
BLAST
Repeati389 – 44456Kelch 3Add
BLAST
Repeati446 – 49247Kelch 4Add
BLAST
Repeati494 – 53845Kelch 5Add
BLAST
Repeati539 – 58547Kelch 6Add
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 6 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiKOG4441. Eukaryota.
ENOG410XNX8. LUCA.
GeneTreeiENSGT00840000129689.
HOGENOMiHOG000232171.
HOVERGENiHBG000905.
InParanoidiO14682.
KOiK10462.
OMAiLDAWNSI.
OrthoDBiEOG7FJGZZ.
PhylomeDBiO14682.
TreeFamiTF329218.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ_dom.
IPR030562. ENC1.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PANTHERiPTHR24410:SF5. PTHR24410:SF5. 1 hit.
PfamiPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 4 hits.
[Graphical view]
PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 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: O14682-1) [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
MSVSVHENRK SRASSGSINI YLFHKSSYAD SVLTHLNLLR QQRLFTDVLL
60 70 80 90 100
HAGNRTFPCH RAVLAACSRY FEAMFSGGLK ESQDSEVNFD NSIHPEVLEL
110 120 130 140 150
LLDYAYSSRV IINEENAESL LEAGDMLEFQ DIRDACAEFL EKNLHPTNCL
160 170 180 190 200
GMLLLSDAHQ CTKLYELSWR MCLSNFQTIR KNEDFLQLPQ DMVVQLLSSE
210 220 230 240 250
ELETEDERLV YESAINWISY DLKKRYCYLP ELLQTVRLAL LPAIYLMENV
260 270 280 290 300
AMEELITKQR KSKEIVEEAI RCKLKILQND GVVTSLCARP RKTGHALFLL
310 320 330 340 350
GGQTFMCDKL YLVDQKAKEI IPKADIPSPR KEFSACAIGC KVYITGGRGS
360 370 380 390 400
ENGVSKDVWV YDTLHEEWSK AAPMLVARFG HGSAELKHCL YVVGGHTAAT
410 420 430 440 450
GCLPASPSVS LKQVEHYDPT INKWTMVAPL REGVSNAAVV SAKLKLFAFG
460 470 480 490 500
GTSVSHDKLP KVQCYDQCEN RWTVPATCPQ PWRYTAAAVL GNQIFIMGGD
510 520 530 540 550
TEFSACSAYK FNSETYQWTK VGDVTAKRMS CHAVASGNKL YVVGGYFGIQ
560 570 580
RCKTLDCYDP TLDVWNSITT VPYSLIPTAF VSTWKHLPS
Length:589
Mass (Da):66,130
Last modified:December 1, 2000 - v2
Checksum:iDB003A1DFA65BAA0
GO
Isoform 2 (identifier: O14682-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Note: No experimental confirmation available.
Show »
Length:516
Mass (Da):57,854
Checksum:i4A30529496E087EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081S → F in BAG58153 (PubMed:14702039).Curated
Sequence conflicti112 – 13019INEEN…MLEFQ → HQLEGKCRNSLLGSLVTCWS FK (PubMed:9305847).CuratedAdd
BLAST
Sequence conflicti237 – 2382RL → TR in AAC39532 (PubMed:9305847).Curated
Sequence conflicti378 – 3781R → M in BAG58153 (PubMed:14702039).Curated
Sequence conflicti402 – 4021C → S in AAC64498 (PubMed:9683534).Curated
Sequence conflicti427 – 4271V → A (PubMed:9305847).Curated
Sequence conflicti430 – 4389LREGVSNAA → RPRRRYNCAQ (PubMed:9305847).Curated
Sequence conflicti484 – 589106YTAAA…KHLPS → IHSQASCPGGTQDFLLWGVI QNFSACFCL in AAC39532 (PubMed:9305847).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561I → S.
Corresponds to variant rs16872126 [ dbSNP | Ensembl ].
VAR_050040

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 2. 1 PublicationVSP_045074Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010314 mRNA. Translation: AAC39532.1.
AF005381 mRNA. Translation: AAC64498.1.
AF059611 mRNA. Translation: AAC26109.1.
AK295128 mRNA. Translation: BAG58153.1.
AC026405 Genomic DNA. No translation available.
BC000418 mRNA. Translation: AAH00418.1.
CCDSiCCDS4021.1. [O14682-1]
CCDS58958.1. [O14682-2]
RefSeqiNP_001243503.1. NM_001256574.1. [O14682-1]
NP_001243504.1. NM_001256575.1. [O14682-1]
NP_001243505.1. NM_001256576.1. [O14682-2]
NP_003624.1. NM_003633.3. [O14682-1]
XP_011541998.1. XM_011543696.1. [O14682-1]
XP_011541999.1. XM_011543697.1. [O14682-1]
UniGeneiHs.104925.
Hs.744844.

Genome annotation databases

EnsembliENST00000302351; ENSP00000306356; ENSG00000171617. [O14682-1]
ENST00000510316; ENSP00000423804; ENSG00000171617. [O14682-2]
ENST00000537006; ENSP00000446289; ENSG00000171617. [O14682-1]
ENST00000618628; ENSP00000479101; ENSG00000171617. [O14682-1]
GeneIDi8507.
KEGGihsa:8507.
UCSCiuc011css.4. human. [O14682-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010314 mRNA. Translation: AAC39532.1.
AF005381 mRNA. Translation: AAC64498.1.
AF059611 mRNA. Translation: AAC26109.1.
AK295128 mRNA. Translation: BAG58153.1.
AC026405 Genomic DNA. No translation available.
BC000418 mRNA. Translation: AAH00418.1.
CCDSiCCDS4021.1. [O14682-1]
CCDS58958.1. [O14682-2]
RefSeqiNP_001243503.1. NM_001256574.1. [O14682-1]
NP_001243504.1. NM_001256575.1. [O14682-1]
NP_001243505.1. NM_001256576.1. [O14682-2]
NP_003624.1. NM_003633.3. [O14682-1]
XP_011541998.1. XM_011543696.1. [O14682-1]
XP_011541999.1. XM_011543697.1. [O14682-1]
UniGeneiHs.104925.
Hs.744844.

3D structure databases

ProteinModelPortaliO14682.
SMRiO14682. Positions 23-270, 277-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114079. 14 interactions.
IntActiO14682. 1 interaction.
STRINGi9606.ENSP00000306356.

PTM databases

iPTMnetiO14682.
PhosphoSiteiO14682.

Polymorphism and mutation databases

BioMutaiENC1.

Proteomic databases

EPDiO14682.
PaxDbiO14682.
PeptideAtlasiO14682.
PRIDEiO14682.

Protocols and materials databases

DNASUi8507.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302351; ENSP00000306356; ENSG00000171617. [O14682-1]
ENST00000510316; ENSP00000423804; ENSG00000171617. [O14682-2]
ENST00000537006; ENSP00000446289; ENSG00000171617. [O14682-1]
ENST00000618628; ENSP00000479101; ENSG00000171617. [O14682-1]
GeneIDi8507.
KEGGihsa:8507.
UCSCiuc011css.4. human. [O14682-1]

Organism-specific databases

CTDi8507.
GeneCardsiENC1.
HGNCiHGNC:3345. ENC1.
HPAiHPA030726.
MIMi605173. gene.
neXtProtiNX_O14682.
PharmGKBiPA27782.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4441. Eukaryota.
ENOG410XNX8. LUCA.
GeneTreeiENSGT00840000129689.
HOGENOMiHOG000232171.
HOVERGENiHBG000905.
InParanoidiO14682.
KOiK10462.
OMAiLDAWNSI.
OrthoDBiEOG7FJGZZ.
PhylomeDBiO14682.
TreeFamiTF329218.

Miscellaneous databases

ChiTaRSiENC1. human.
GeneWikiiENC1.
GenomeRNAii8507.
PROiO14682.
SOURCEiSearch...

Gene expression databases

BgeeiO14682.
CleanExiHS_ENC1.
ExpressionAtlasiO14682. baseline and differential.
GenevisibleiO14682. HS.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ_dom.
IPR030562. ENC1.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PANTHERiPTHR24410:SF5. PTHR24410:SF5. 1 hit.
PfamiPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 4 hits.
[Graphical view]
PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION BY TP53.
    Tissue: Colon cancer.
  2. "Cloning of human ENC-1 and evaluation of its expression and regulation in nervous system tumors."
    Hernandez M.-C., Andres-Barquin P.J., Holt I., Israel M.A.
    Exp. Cell Res. 242:470-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation."
    Kim T.-A., Lim J., Ota S., Raja S., Rogers R., Rivnay B., Avraham H., Avraham S.
    J. Cell Biol. 141:553-566(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain and Hippocampus.
  4. "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 2).
    Tissue: Brain.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Muscle.
  7. "Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway."
    Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.
    J. Biol. Chem. 280:30091-30099(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CUL3 AND RBX1, UBIQUITINATION.
  8. "Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational level."
    Wang X.J., Zhang D.D.
    PLoS ONE 4:E5492-E5492(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KEAP1.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiENC1_HUMAN
AccessioniPrimary (citable) accession number: O14682
Secondary accession number(s): B4DHJ1
, E9PFU0, O75464, Q9UPG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 153 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 5
    Human chromosome 5: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.