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Protein

Protein kinase C-binding protein NELL1

Gene

Nell1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • calcium ion binding Source: InterPro
  • heparin binding Source: RGD
  • identical protein binding Source: RGD
  • protein kinase C binding Source: RGD

GO - Biological processi

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620998. Nell1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular space Source: RGD
  • nuclear envelope Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000000766522 – 810Protein kinase C-binding protein NELL1Add BLAST789

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)Sequence analysis1
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Glycosylationi83N-linked (GlcNAc...)Sequence analysis1
Glycosylationi224N-linked (GlcNAc...)Sequence analysis1
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi372N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi511N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi562N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi577 ↔ 594PROSITE-ProRule annotation
Disulfide bondi600 ↔ 613PROSITE-ProRule annotation
Disulfide bondi607 ↔ 622PROSITE-ProRule annotation
Glycosylationi609N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi624 ↔ 630PROSITE-ProRule annotation
Glycosylationi708N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ62919.
PRIDEiQ62919.

PTM databases

iPTMnetiQ62919.
PhosphoSitePlusiQ62919.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • identical protein binding Source: RGD
  • protein kinase C binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000052883.

Structurei

3D structure databases

ProteinModelPortaliQ62919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 227Laminin G-likeAdd BLAST171
Domaini271 – 332VWFC 1PROSITE-ProRule annotationAdd BLAST62
Domaini434 – 475EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini476 – 516EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini517 – 547EGF-like 3PROSITE-ProRule annotationAdd BLAST31
Domaini549 – 587EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini596 – 631EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini632 – 687VWFC 2PROSITE-ProRule annotationAdd BLAST56
Domaini692 – 750VWFC 3PROSITE-ProRule annotationAdd BLAST59

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

eggNOGiENOG410KD9R. Eukaryota.
ENOG410XSZA. LUCA.
HOGENOMiHOG000217920.
HOVERGENiHBG004805.
InParanoidiQ62919.
PhylomeDBiQ62919.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF02210. Laminin_G_2. 1 hit.
PF00093. VWC. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00179. EGF_CA. 5 hits.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
SM00214. VWC. 4 hits.
SM00215. VWC_out. 2 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.
PIRiT10756.
RefSeqiNP_112331.1. NM_031069.1.
UniGeneiRn.10695.

3D structure databases

ProteinModelPortaliQ62919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000052883.

PTM databases

iPTMnetiQ62919.
PhosphoSitePlusiQ62919.

Proteomic databases

PaxDbiQ62919.
PRIDEiQ62919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4745.
RGDi620998. Nell1.

Phylogenomic databases

eggNOGiENOG410KD9R. Eukaryota.
ENOG410XSZA. LUCA.
HOGENOMiHOG000217920.
HOVERGENiHBG004805.
InParanoidiQ62919.
PhylomeDBiQ62919.

Miscellaneous databases

PROiQ62919.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF02210. Laminin_G_2. 1 hit.
PF00093. VWC. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00179. EGF_CA. 5 hits.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
SM00214. VWC. 4 hits.
SM00215. VWC_out. 2 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 130 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

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.