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Q62919

- NELL1_RAT

UniProt

Q62919 - NELL1_RAT

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Protein

Protein kinase C-binding protein NELL1

Gene

Nell1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization (By similarity).By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. heparin binding Source: RGD
  3. identical protein binding Source: RGD
  4. protein kinase C binding Source: RGD

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. negative regulation of cyclin catabolic process Source: UniProtKB
  3. negative regulation of osteoblast proliferation Source: UniProtKB
  4. positive regulation of apoptotic process Source: RGD
  5. positive regulation of bone mineralization Source: UniProtKB
  6. positive regulation of ossification Source: RGD
  7. positive regulation of osteoblast differentiation Source: UniProtKB
  8. protein homotrimerization Source: RGD
  9. regulation of gene expression Source: UniProtKB
  10. regulation of osteoblast differentiation Source: RGD
Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C-binding protein NELL1
Alternative name(s):
NEL-like protein 1
Gene namesi
Name:Nell1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620998. Nell1.

Subcellular locationi

Cytoplasm By similarity. Nucleus envelope By similarity. Secreted
Note: Colocalizes with ATRAID on the nuclear envelope and the perinuclear region.By similarity

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. extracellular space Source: RGD
  3. nuclear envelope Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 810789Protein kinase C-binding protein NELL1PRO_0000007665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi395 ↔ 407PROSITE-ProRule annotation
Disulfide bondi401 ↔ 416PROSITE-ProRule annotation
Disulfide bondi418 ↔ 432PROSITE-ProRule annotation
Disulfide bondi438 ↔ 451PROSITE-ProRule annotation
Disulfide bondi445 ↔ 460PROSITE-ProRule annotation
Disulfide bondi462 ↔ 474PROSITE-ProRule annotation
Disulfide bondi480 ↔ 493PROSITE-ProRule annotation
Disulfide bondi487 ↔ 502PROSITE-ProRule annotation
Disulfide bondi504 ↔ 515PROSITE-ProRule annotation
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi519 ↔ 529PROSITE-ProRule annotation
Disulfide bondi523 ↔ 535PROSITE-ProRule annotation
Disulfide bondi537 ↔ 546PROSITE-ProRule annotation
Disulfide bondi553 ↔ 566PROSITE-ProRule annotation
Disulfide bondi560 ↔ 575PROSITE-ProRule annotation
Glycosylationi562 – 5621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi577 ↔ 594PROSITE-ProRule annotation
Disulfide bondi600 ↔ 613PROSITE-ProRule annotation
Disulfide bondi607 ↔ 622PROSITE-ProRule annotation
Glycosylationi609 – 6091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi624 ↔ 630PROSITE-ProRule annotation
Glycosylationi708 – 7081N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ62919.
PRIDEiQ62919.

PTM databases

PhosphoSiteiQ62919.

Expressioni

Gene expression databases

GenevestigatoriQ62919.

Interactioni

Subunit structurei

Interacts with ATRAID; the interaction promotes osteoblast cell differentiation and mineralization (By similarity). Homotrimer. Binds to PKC beta-1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021340.

Structurei

3D structure databases

ProteinModelPortaliQ62919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 227171Laminin G-likeAdd
BLAST
Domaini271 – 33262VWFC 1PROSITE-ProRule annotationAdd
BLAST
Domaini434 – 47542EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini476 – 51641EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini517 – 54731EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini549 – 58739EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini596 – 63136EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini632 – 68756VWFC 2PROSITE-ProRule annotationAdd
BLAST
Domaini692 – 75059VWFC 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 5 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 3 VWFC domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG253557.
HOGENOMiHOG000217920.
HOVERGENiHBG004805.
InParanoidiQ62919.
PhylomeDBiQ62919.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
IPR001007. VWF_C.
[Graphical view]
PfamiPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF12661. hEGF. 1 hit.
PF02210. Laminin_G_2. 1 hit.
PF00093. VWC. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
SM00214. VWC. 4 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 3 hits.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q62919-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMDVILVLW FCVCTARTVL GFGMDPDLQL DIISELDLVN TTLGVTQVAG
60 70 80 90 100
LHNASKAFLF QDVQREIHSA PHVSEKLIQL FRNKSEFTFL ATVQQKPSTS
110 120 130 140 150
GVILSIRELE HSYFELESSG PREEIRYHYI HGGKPRTEAL PYRMADGQWH
160 170 180 190 200
KVALSVSASH LLLHIDCNRI YERVIDPPET NLPPGSNLWL GQRNQKHGFF
210 220 230 240 250
KGIIQDGKII FMPNGFITQC PNLNRTCPTC SDFLSLVQGI MDLQELLAKM
260 270 280 290 300
TAKLNYAETR LGQLENCHCE KTCQVSGLLY RDQDSWVDGD NCGNCTCKSG
310 320 330 340 350
AVECRRMSCP PLNCSPDSLP VHISGQCCKV CRPKCIYGGK VLAEGQRILT
360 370 380 390 400
KTCRECRGGV LVKITEACPP LNCSAKDHIL PENQCCRVCP GHNFCAEAPK
410 420 430 440 450
CGENSECKNW NTKATCECKN GYISVQGNSA YCEDIDECAA KMHYCHANTV
460 470 480 490 500
CVNLPGLYRC DCVPGYIRVD DFSCTEHDDC GSGQHNCDKN AICTNTVQGH
510 520 530 540 550
SCTCQPGYVG NGTICKAFCE EGCRYGGTCV APNKCVCPSG FTGSHCEKDI
560 570 580 590 600
DECAEGFVEC HNYSRCVNLP GWYHCECRSG FHDDGTYSLS GESCIDIDEC
610 620 630 640 650
ALRTHTCWND SACINLAGGF DCLCPSGPSC SGDCPHEGGL KHNGQVWILR
660 670 680 690 700
EDRCSVCSCK DGKIFCRRTA CDCQNPNVDL FCCPECDTRV TSQCLDQSGQ
710 720 730 740 750
KLYRSGDNWT HSCQQCRCLE GEADCWPLAC PSLGCEYTAM FEGECCPRCV
760 770 780 790 800
SDPCLAGNIA YDIRKTCLDS FGVSRLSGAV WTMAGSPCTT CKCKNGRVCC
810
SVDLECIENN
Length:810
Mass (Da):89,212
Last modified:May 30, 2000 - v2
Checksum:i46F09C466AF9AB0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48246 mRNA. Translation: AAC72252.1.
PIRiT10756.
RefSeqiNP_112331.1. NM_031069.1.
UniGeneiRn.10695.

Genome annotation databases

GeneIDi81733.
KEGGirno:81733.
UCSCiRGD:620998. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48246 mRNA. Translation: AAC72252.1 .
PIRi T10756.
RefSeqi NP_112331.1. NM_031069.1.
UniGenei Rn.10695.

3D structure databases

ProteinModelPortali Q62919.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021340.

PTM databases

PhosphoSitei Q62919.

Proteomic databases

PaxDbi Q62919.
PRIDEi Q62919.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81733.
KEGGi rno:81733.
UCSCi RGD:620998. rat.

Organism-specific databases

CTDi 4745.
RGDi 620998. Nell1.

Phylogenomic databases

eggNOGi NOG253557.
HOGENOMi HOG000217920.
HOVERGENi HBG004805.
InParanoidi Q62919.
PhylomeDBi Q62919.

Miscellaneous databases

NextBioi 615404.
PROi Q62919.

Gene expression databases

Genevestigatori Q62919.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF12661. hEGF. 1 hit.
PF02210. Laminin_G_2. 1 hit.
PF00093. VWC. 2 hits.
[Graphical view ]
SMARTi SM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
SM00214. VWC. 4 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 3 hits.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Biochemical characterization and expression analysis of neural thrombospondin-1-like proteins NELL1 and NELL2."
    Kuroda S., Oyasu M., Kawakami M., Kanayama N., Tanizawa K., Saito N., Abe T., Matsuhashi S., Ting K.
    Biochem. Biophys. Res. Commun. 265:79-86(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiNELL1_RAT
AccessioniPrimary (citable) accession number: Q62919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 120 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3