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Protein

Protein NOV homolog

Gene

Nov

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Immediate-early protein likely to play a role in cell growth regulation.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Names & Taxonomyi

Protein namesi
Recommended name:
Protein NOV homolog
Short name:
NovH
Alternative name(s):
CCN family member 3
Nephroblastoma-overexpressed gene protein homolog
Gene namesi
Name:Nov
Synonyms:Ccn3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:109185. Nov.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 354333Protein NOV homologPRO_0000014416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi261 ↔ 298By similarity
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi278 ↔ 312By similarity
Disulfide bondi289 ↔ 328By similarity
Disulfide bondi292 ↔ 330By similarity
Disulfide bondi297 ↔ 334By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ64299.
PRIDEiQ64299.

Expressioni

Gene expression databases

BgeeiQ64299.
CleanExiMM_NOV.
GenevisibleiQ64299. MM.

Interactioni

Subunit structurei

Interacts with FBLN1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054389.

Structurei

3D structure databases

ProteinModelPortaliQ64299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 9975IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini102 – 16867VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini202 – 24746TSP type-1PROSITE-ProRule annotationAdd
BLAST
Domaini261 – 33575CTCKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CCN family.Curated
Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG72934.
GeneTreeiENSGT00760000119225.
HOGENOMiHOG000231462.
HOVERGENiHBG000635.
InParanoidiQ64299.
OMAiQCEMVKQ.
OrthoDBiEOG7N8ZXB.
PhylomeDBiQ64299.
TreeFamiTF326070.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000867. IGFBP-like.
IPR012395. IGFBP_CNN.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000884. Thrombospondin_1_rpt.
IPR001007. VWF_C.
[Graphical view]
PfamiPF00007. Cys_knot. 1 hit.
PF00219. IGFBP. 1 hit.
PF00090. TSP_1. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PIRSFiPIRSF036495. IGFBP_rP_CNN. 1 hit.
SMARTiSM00041. CT. 1 hit.
SM00121. IB. 1 hit.
SM00209. TSP1. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS50092. TSP1. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q64299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFLRKRCL CLGFLLFHLL SQVSASLRCP SRCPPKCPSI SPTCAPGVRS
60 70 80 90 100
VLDGCSCCPV CARQRGESCS EMRPCDQSSG LYCDRSADPN NQTGICMVPE
110 120 130 140 150
GDNCVFDGVI YRNGEKFEPN CQYFCTCRDG QIGCLPRCQL DVLLPGPDCP
160 170 180 190 200
APRKVAVPGE CCEKWTCGSD EQGTQGTLGG LALPAYRPEA TVGVEVSDSS
210 220 230 240 250
INCIEQTTEW SACSKSCGMG VSTRVTNRNR QCEMVKQTRL CIVRPCEQEP
260 270 280 290 300
EEVTDKKGKK CLRTKKSLKA IHLQFENCTS LYTYKPRFCG VCSDGRCCTP
310 320 330 340 350
HNTKTIQVEF QCLPGEIIKK PVMVIGTCTC YSNCPQNNEA FLQDLELKTS

RGEI
Length:354
Mass (Da):38,928
Last modified:November 1, 1996 - v1
Checksum:i08ECE8CFC67829DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → G in BAC30363 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97863 Genomic DNA. Translation: CAA66457.1.
Y09257 mRNA. Translation: CAA70454.1.
X96585 mRNA. Translation: CAA65404.1.
AK039481 mRNA. Translation: BAC30363.1.
AK081944 mRNA. Translation: BAC38378.1.
BC003774 mRNA. Translation: AAH03774.1.
CCDSiCCDS27471.1.
RefSeqiNP_035060.1. NM_010930.4.
UniGeneiMm.5167.

Genome annotation databases

EnsembliENSMUST00000050027; ENSMUSP00000054389; ENSMUSG00000037362.
GeneIDi18133.
KEGGimmu:18133.
UCSCiuc007vrn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97863 Genomic DNA. Translation: CAA66457.1.
Y09257 mRNA. Translation: CAA70454.1.
X96585 mRNA. Translation: CAA65404.1.
AK039481 mRNA. Translation: BAC30363.1.
AK081944 mRNA. Translation: BAC38378.1.
BC003774 mRNA. Translation: AAH03774.1.
CCDSiCCDS27471.1.
RefSeqiNP_035060.1. NM_010930.4.
UniGeneiMm.5167.

3D structure databases

ProteinModelPortaliQ64299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054389.

Proteomic databases

PaxDbiQ64299.
PRIDEiQ64299.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050027; ENSMUSP00000054389; ENSMUSG00000037362.
GeneIDi18133.
KEGGimmu:18133.
UCSCiuc007vrn.1. mouse.

Organism-specific databases

CTDi4856.
MGIiMGI:109185. Nov.

Phylogenomic databases

eggNOGiNOG72934.
GeneTreeiENSGT00760000119225.
HOGENOMiHOG000231462.
HOVERGENiHBG000635.
InParanoidiQ64299.
OMAiQCEMVKQ.
OrthoDBiEOG7N8ZXB.
PhylomeDBiQ64299.
TreeFamiTF326070.

Miscellaneous databases

NextBioi293376.
PROiQ64299.
SOURCEiSearch...

Gene expression databases

BgeeiQ64299.
CleanExiMM_NOV.
GenevisibleiQ64299. MM.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000867. IGFBP-like.
IPR012395. IGFBP_CNN.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000884. Thrombospondin_1_rpt.
IPR001007. VWF_C.
[Graphical view]
PfamiPF00007. Cys_knot. 1 hit.
PF00219. IGFBP. 1 hit.
PF00090. TSP_1. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PIRSFiPIRSF036495. IGFBP_rP_CNN. 1 hit.
SMARTiSM00041. CT. 1 hit.
SM00121. IB. 1 hit.
SM00209. TSP1. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS50092. TSP1. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/Sv and ICR.
    Tissue: Brain.
  2. "Regulation of nov by WT1: a potential role for nov in nephrogenesis."
    Martinerie C., Chevalier G., Rauscher F.J. III, Perbal B.
    Oncogene 12:1479-1492(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic head and Spinal cord.
  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].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiNOV_MOUSE
AccessioniPrimary (citable) accession number: Q64299
Secondary accession number(s): Q8CA67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.