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Protein

Neuralized-like protein 2

Gene

NEURL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. During myogenesis, controls the ubiquitination and degradation of the specific pool of CTNNB1/beta-catenin located at the sarcolemma (By similarity).By similarity

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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuralized-like protein 2
Gene namesi
Name:NEURL2
Synonyms:C20orf163
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16156. NEURL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25705.

Polymorphism and mutation databases

DMDMi33301415.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Neuralized-like protein 2PRO_0000181257Add
BLAST

Proteomic databases

PaxDbiQ9BR09.
PRIDEiQ9BR09.

Expressioni

Tissue specificityi

Expressed specifically in skeletal and cardiac muscles.1 Publication

Gene expression databases

BgeeiQ9BR09.
CleanExiHS_NEURL2.
ExpressionAtlasiQ9BR09. baseline and differential.
GenevisibleiQ9BR09. HS.

Organism-specific databases

HPAiHPA043402.

Interactioni

Subunit structurei

Probable component the ECS(NEURL2) E3 ubiquitin-protein ligase complex consisting of TCEB2/Elongin B, TCEB1/Elongin C, CUL5, RBX1 and NEURL2. Interacts with CTNNB1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000361596.

Structurei

3D structure databases

ProteinModelPortaliQ9BR09.
SMRiQ9BR09. Positions 22-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 244222NHRPROSITE-ProRule annotationAdd
BLAST
Domaini250 – 28536SOCS boxPROSITE-ProRule annotationAdd
BLAST

Domaini

The SOCS domain mediates the interaction with TCEB1 and TCEB2, while the NHR domain may be involved in ubiquitination substrate binding.By similarity

Sequence similaritiesi

Contains 1 NHR (neuralized homology repeat) domain.PROSITE-ProRule annotation
Contains 1 SOCS box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IMDX. Eukaryota.
ENOG4111F7Q. LUCA.
GeneTreeiENSGT00730000110931.
HOGENOMiHOG000231005.
HOVERGENiHBG052607.
InParanoidiQ9BR09.
KOiK16782.
OMAiTWVFAIT.
PhylomeDBiQ9BR09.
TreeFamiTF314368.

Family and domain databases

InterProiIPR006573. NHR_dom.
IPR001496. SOCS_box.
[Graphical view]
PfamiPF07177. Neuralized. 1 hit.
PF07525. SOCS_box. 1 hit.
[Graphical view]
SMARTiSM00588. NEUZ. 1 hit.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
PROSITEiPS51065. NHR. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BR09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAASEPVDS GALWGLERPE PPPTRFHRVH GANIRVDPSG TRATRVESFA
60 70 80 90 100
HGVCFSREPL APGQVFLVEI EEKELGWCGH LRLGLTALDP ASLAPVPEFS
110 120 130 140 150
LPDLVNLGHT WVFAITRHHN RVPREGRPEA EAAAPSRPPT LLVEPYLRIE
160 170 180 190 200
QFRIPRDRLV GRSRPGLYSH LLDQLYELNV LPPTARRSRL GVLFCPRPDG
210 220 230 240 250
TADMHIIING EDMGPSARGL PAAQPLYAVV DVFASTKSVR LVQLEYGLPS
260 270 280
LQTLCRLVIQ RSMVHRLAID GLHLPKELKD FCKYE
Length:285
Mass (Da):31,690
Last modified:June 1, 2001 - v1
Checksum:i6C79A17CC41BF180
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111E → K.
Corresponds to variant rs35342327 [ dbSNP | Ensembl ].
VAR_052033

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK054821 mRNA. Translation: BAB70810.1.
AJ295985 mRNA. Translation: CAC82498.1.
AL008726 Genomic DNA. Translation: CAC36018.1.
BC074737 mRNA. Translation: AAH74737.1.
BC105935 mRNA. Translation: AAI05936.1.
BC107485 mRNA. Translation: AAI07486.1.
CCDSiCCDS13384.1.
RefSeqiNP_001265464.1. NM_001278535.1.
NP_542787.1. NM_080749.3.
UniGeneiHs.517094.
Hs.609336.

Genome annotation databases

EnsembliENST00000372518; ENSP00000361596; ENSG00000124257.
GeneIDi140825.
KEGGihsa:140825.
UCSCiuc002xqg.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK054821 mRNA. Translation: BAB70810.1.
AJ295985 mRNA. Translation: CAC82498.1.
AL008726 Genomic DNA. Translation: CAC36018.1.
BC074737 mRNA. Translation: AAH74737.1.
BC105935 mRNA. Translation: AAI05936.1.
BC107485 mRNA. Translation: AAI07486.1.
CCDSiCCDS13384.1.
RefSeqiNP_001265464.1. NM_001278535.1.
NP_542787.1. NM_080749.3.
UniGeneiHs.517094.
Hs.609336.

3D structure databases

ProteinModelPortaliQ9BR09.
SMRiQ9BR09. Positions 22-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000361596.

Polymorphism and mutation databases

DMDMi33301415.

Proteomic databases

PaxDbiQ9BR09.
PRIDEiQ9BR09.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372518; ENSP00000361596; ENSG00000124257.
GeneIDi140825.
KEGGihsa:140825.
UCSCiuc002xqg.3. human.

Organism-specific databases

CTDi140825.
GeneCardsiNEURL2.
HGNCiHGNC:16156. NEURL2.
HPAiHPA043402.
MIMi608597. gene.
neXtProtiNX_Q9BR09.
PharmGKBiPA25705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IMDX. Eukaryota.
ENOG4111F7Q. LUCA.
GeneTreeiENSGT00730000110931.
HOGENOMiHOG000231005.
HOVERGENiHBG052607.
InParanoidiQ9BR09.
KOiK16782.
OMAiTWVFAIT.
PhylomeDBiQ9BR09.
TreeFamiTF314368.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GeneWikiiNEURL2.
GenomeRNAii140825.
PROiQ9BR09.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BR09.
CleanExiHS_NEURL2.
ExpressionAtlasiQ9BR09. baseline and differential.
GenevisibleiQ9BR09. HS.

Family and domain databases

InterProiIPR006573. NHR_dom.
IPR001496. SOCS_box.
[Graphical view]
PfamiPF07177. Neuralized. 1 hit.
PF07525. SOCS_box. 1 hit.
[Graphical view]
SMARTiSM00588. NEUZ. 1 hit.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
PROSITEiPS51065. NHR. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Cerebellum.
  2. "Full-length sequencing of some human and murine muscular transcripts (Telethon Italy project B41)."
    Frigimelica E., Lanfranchi G.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Brain.
  5. "Ozz-E3, a muscle-specific ubiquitin ligase, regulates beta-catenin degradation during myogenesis."
    Nastasi T., Bongiovanni A., Campos Y., Mann L., Toy J.N., Bostrom J., Rottier R., Hahn C., Conaway J.W., Harris A.J., D'Azzo A.
    Dev. Cell 6:269-282(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiNEUL2_HUMAN
AccessioniPrimary (citable) accession number: Q9BR09
Secondary accession number(s): Q3KR34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 120 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.