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Protein

Neuropilin-1

Gene

Nrp1

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

Functioni

Receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi195CalciumBy similarity1
Metal bindingi209CalciumBy similarity1
Metal bindingi250CalciumBy similarity1

GO - Molecular functioni

  • growth factor binding Source: MGI
  • heparin binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • semaphorin receptor activity Source: MGI
  • vascular endothelial growth factor-activated receptor activity Source: BHF-UCL
  • vascular endothelial growth factor binding Source: BHF-UCL

GO - Biological processi

  • angiogenesis Source: BHF-UCL
  • angiogenesis involved in coronary vascular morphogenesis Source: BHF-UCL
  • artery morphogenesis Source: BHF-UCL
  • axonal fasciculation Source: MGI
  • axon extension involved in axon guidance Source: BHF-UCL
  • axon guidance Source: MGI
  • axonogenesis involved in innervation Source: BHF-UCL
  • branchiomotor neuron axon guidance Source: ParkinsonsUK-UCL
  • cell migration Source: MGI
  • cell migration involved in coronary vasculogenesis Source: BHF-UCL
  • cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • cellular response to hepatocyte growth factor stimulus Source: MGI
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • commissural neuron axon guidance Source: BHF-UCL
  • coronary artery morphogenesis Source: BHF-UCL
  • dendrite development Source: MGI
  • dichotomous subdivision of terminal units involved in salivary gland branching Source: MGI
  • dorsal root ganglion morphogenesis Source: ParkinsonsUK-UCL
  • endothelial cell chemotaxis Source: MGI
  • facial nerve structural organization Source: ParkinsonsUK-UCL
  • facioacoustic ganglion development Source: ParkinsonsUK-UCL
  • gonadotrophin-releasing hormone neuronal migration to the hypothalamus Source: BHF-UCL
  • heart development Source: MGI
  • hepatocyte growth factor receptor signaling pathway Source: MGI
  • motor neuron axon guidance Source: ParkinsonsUK-UCL
  • negative regulation of axon extension Source: MGI
  • negative regulation of axon extension involved in axon guidance Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: BHF-UCL
  • nerve development Source: BHF-UCL
  • neural crest cell migration involved in autonomic nervous system development Source: ParkinsonsUK-UCL
  • neuron development Source: BHF-UCL
  • neuron migration Source: BHF-UCL
  • otic placode development Source: ParkinsonsUK-UCL
  • patterning of blood vessels Source: BHF-UCL
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • positive chemotaxis Source: BHF-UCL
  • positive regulation of axon extension involved in axon guidance Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of retinal ganglion cell axon guidance Source: BHF-UCL
  • protein localization to early endosome Source: BHF-UCL
  • regulation of axon extension involved in axon guidance Source: MGI
  • regulation of retinal ganglion cell axon guidance Source: BHF-UCL
  • renal artery morphogenesis Source: BHF-UCL
  • response to wounding Source: Ensembl
  • retinal ganglion cell axon guidance Source: BHF-UCL
  • retina vasculature morphogenesis in camera-type eye Source: BHF-UCL
  • semaphorin-plexin signaling pathway Source: MGI
  • semaphorin-plexin signaling pathway involved in axon guidance Source: ParkinsonsUK-UCL
  • semaphorin-plexin signaling pathway involved in neuron projection guidance Source: BHF-UCL
  • sensory neuron axon guidance Source: ParkinsonsUK-UCL
  • sprouting angiogenesis Source: BHF-UCL
  • sympathetic ganglion development Source: BHF-UCL
  • sympathetic nervous system development Source: MGI
  • sympathetic neuron projection extension Source: BHF-UCL
  • sympathetic neuron projection guidance Source: BHF-UCL
  • toxin transport Source: MGI
  • trigeminal ganglion development Source: ParkinsonsUK-UCL
  • trigeminal nerve morphogenesis Source: MGI
  • trigeminal nerve structural organization Source: ParkinsonsUK-UCL
  • vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • VEGF-activated neuropilin signaling pathway Source: BHF-UCL
  • VEGF-activated neuropilin signaling pathway involved in axon guidance Source: BHF-UCL
  • ventral trunk neural crest cell migration Source: ParkinsonsUK-UCL
  • vestibulocochlear nerve structural organization Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Neurogenesis

Keywords - Ligandi

Calcium, Heparin-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-194306. Neurophilin interactions with VEGF and VEGFR.
R-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-445144. Signal transduction by L1.
R-MMU-447041. CHL1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuropilin-1
Alternative name(s):
A5 protein
CD_antigen: CD304
Gene namesi
Name:Nrp1
Synonyms:Nrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:106206. Nrp1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 856ExtracellularSequence analysisAdd BLAST835
Transmembranei857 – 879HelicalSequence analysisAdd BLAST23
Topological domaini880 – 923CytoplasmicSequence analysisAdd BLAST44

GO - Cellular componenti

  • axon Source: BHF-UCL
  • cell surface Source: Ensembl
  • cytosol Source: MGI
  • early endosome Source: BHF-UCL
  • extracellular space Source: MGI
  • focal adhesion Source: MGI
  • growth cone Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • neurofilament Source: MGI
  • neuronal cell body Source: Ensembl
  • plasma membrane Source: BHF-UCL
  • sorting endosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000002186022 – 923Neuropilin-1Add BLAST902

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 54By similarity
Disulfide bondi82 ↔ 104By similarity
Disulfide bondi147 ↔ 173By similarity
Glycosylationi150N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi206 ↔ 228By similarity
Glycosylationi261N-linked (GlcNAc...)1 Publication1
Disulfide bondi275 ↔ 424By similarity
Glycosylationi300N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi431 ↔ 583By similarity
Glycosylationi522N-linked (GlcNAc...)1 Publication1
Glycosylationi612O-linked (Xyl...) (chondroitin sulfate); alternateBy similarity1
Glycosylationi612O-linked (Xyl...) (heparan sulfate); alternateBy similarity1
Glycosylationi842N-linked (GlcNAc...)Sequence analysis1
Modified residuei894PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Heparan sulfate, Phosphoprotein, Proteoglycan

Proteomic databases

MaxQBiP97333.
PaxDbiP97333.
PeptideAtlasiP97333.
PRIDEiP97333.
TopDownProteomicsiP97333.

PTM databases

iPTMnetiP97333.
PhosphoSitePlusiP97333.
SwissPalmiP97333.

Expressioni

Tissue specificityi

Nervous system.

Gene expression databases

BgeeiENSMUSG00000025810.
CleanExiMM_NRP1.
GenevisibleiP97333. MM.

Interactioni

Subunit structurei

Homodimer, and heterodimer with NRP2. Binds PLXNB1 (By similarity). Interacts with FER.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Ptk2P341522EBI-1555129,EBI-77070

GO - Molecular functioni

  • growth factor binding Source: MGI
  • vascular endothelial growth factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi201848. 5 interactors.
DIPiDIP-39360N.
IntActiP97333. 12 interactors.
MINTiMINT-99860.
STRINGi10090.ENSMUSP00000026917.

Structurei

Secondary structure

1923
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 32Combined sources6
Beta strandi37 – 40Combined sources4
Turni42 – 46Combined sources5
Beta strandi53 – 59Combined sources7
Beta strandi67 – 71Combined sources5
Helixi80 – 82Combined sources3
Beta strandi84 – 94Combined sources11
Beta strandi97 – 103Combined sources7
Beta strandi105 – 107Combined sources3
Beta strandi115 – 124Combined sources10
Beta strandi135 – 140Combined sources6
Beta strandi146 – 151Combined sources6
Beta strandi153 – 159Combined sources7
Turni161 – 164Combined sources4
Beta strandi172 – 178Combined sources7
Helixi180 – 182Combined sources3
Beta strandi185 – 193Combined sources9
Beta strandi208 – 217Combined sources10
Turni218 – 220Combined sources3
Beta strandi223 – 227Combined sources5
Beta strandi229 – 231Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi240 – 248Combined sources9
Beta strandi257 – 264Combined sources8
Turni281 – 283Combined sources3
Beta strandi284 – 286Combined sources3
Helixi288 – 290Combined sources3
Beta strandi291 – 294Combined sources4
Helixi299 – 301Combined sources3
Helixi303 – 305Combined sources3
Beta strandi326 – 342Combined sources17
Turni347 – 349Combined sources3
Beta strandi352 – 368Combined sources17
Beta strandi373 – 378Combined sources6
Beta strandi385 – 389Combined sources5
Beta strandi391 – 414Combined sources24
Beta strandi417 – 424Combined sources8
Helixi426 – 428Combined sources3
Beta strandi429 – 431Combined sources3
Turni437 – 439Combined sources3
Beta strandi440 – 442Combined sources3
Helixi444 – 446Combined sources3
Beta strandi447 – 449Combined sources3
Turni450 – 453Combined sources4
Helixi459 – 462Combined sources4
Turni464 – 466Combined sources3
Beta strandi471 – 473Combined sources3
Beta strandi485 – 501Combined sources17
Beta strandi503 – 507Combined sources5
Beta strandi512 – 525Combined sources14
Beta strandi534 – 537Combined sources4
Beta strandi544 – 547Combined sources4
Beta strandi550 – 570Combined sources21
Beta strandi573 – 583Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GZ9X-ray2.70A22-586[»]
4GZAX-ray7.00H22-586[»]
ProteinModelPortaliP97333.
SMRiP97333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 141CUB 1PROSITE-ProRule annotationAdd BLAST115
Domaini147 – 265CUB 2PROSITE-ProRule annotationAdd BLAST119
Domaini275 – 424F5/8 type C 1PROSITE-ProRule annotationAdd BLAST150
Domaini431 – 583F5/8 type C 2PROSITE-ProRule annotationAdd BLAST153
Domaini645 – 811MAMPROSITE-ProRule annotationAdd BLAST167

Domaini

The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding.By similarity

Sequence similaritiesi

Belongs to the neuropilin family.Curated
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IE8T. Eukaryota.
ENOG410YRBE. LUCA.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000039978.
HOVERGENiHBG000502.
InParanoidiP97333.
KOiK06724.
OMAiYCACWHN.
OrthoDBiEOG091G017M.
TreeFamiTF316506.

Family and domain databases

CDDicd00041. CUB. 2 hits.
cd06263. MAM. 1 hit.
Gene3Di2.60.120.260. 2 hits.
2.60.120.290. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000859. CUB_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR000998. MAM_dom.
IPR014648. Neuropilin.
IPR022579. Neuropilin_C.
IPR027146. NRP1.
[Graphical view]
PANTHERiPTHR10127:SF654. PTHR10127:SF654. 1 hit.
PfamiPF00431. CUB. 2 hits.
PF11980. DUF3481. 1 hit.
PF00754. F5_F8_type_C. 2 hits.
PF00629. MAM. 1 hit.
[Graphical view]
PIRSFiPIRSF036960. Neuropilin. 1 hit.
PRINTSiPR00020. MAMDOMAIN.
SMARTiSM00042. CUB. 2 hits.
SM00231. FA58C. 2 hits.
SM00137. MAM. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS01180. CUB. 2 hits.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P97333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGLPLLCA TLALALALAG AFRSDKCGGT IKIENPGYLT SPGYPHSYHP
60 70 80 90 100
SEKCEWLIQA PEPYQRIMIN FNPHFDLEDR DCKYDYVEVI DGENEGGRLW
110 120 130 140 150
GKFCGKIAPS PVVSSGPFLF IKFVSDYETH GAGFSIRYEI FKRGPECSQN
160 170 180 190 200
YTAPTGVIKS PGFPEKYPNS LECTYIIFAP KMSEIILEFE SFDLEQDSNP
210 220 230 240 250
PGGMFCRYDR LEIWDGFPEV GPHIGRYCGQ KTPGRIRSSS GVLSMVFYTD
260 270 280 290 300
SAIAKEGFSA NYSVLQSSIS EDFKCMEALG MESGEIHSDQ ITASSQYGTN
310 320 330 340 350
WSVERSRLNY PENGWTPGED SYKEWIQVDL GLLRFVTAVG TQGAISKETK
360 370 380 390 400
KKYYVKTYRV DISSNGEDWI SLKEGNKAII FQGNTNPTDV VLGVFSKPLI
410 420 430 440 450
TRFVRIKPVS WETGISMRFE VYGCKITDYP CSGMLGMVSG LISDSQITAS
460 470 480 490 500
NQADRNWMPE NIRLVTSRTG WALPPSPHPY TNEWLQVDLG DEKIVRGVII
510 520 530 540 550
QGGKHRENKV FMRKFKIAYS NNGSDWKTIM DDSKRKAKSF EGNNNYDTPE
560 570 580 590 600
LRTFSPLSTR FIRIYPERAT HSGLGLRMEL LGCEVEAPTA GPTTPNGNPV
610 620 630 640 650
DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTIIDSTIQ SEFPTYGFNC
660 670 680 690 700
EFGWGSHKTF CHWEHDSHAQ LRWSVLTSKT GPIQDHTGDG NFIYSQADEN
710 720 730 740 750
QKGKVARLVS PVVYSQSSAH CMTFWYHMSG SHVGTLRVKL RYQKPEEYDQ
760 770 780 790 800
LVWMVVGHQG DHWKEGRVLL HKSLKLYQVI FEGEIGKGNL GGIAVDDISI
810 820 830 840 850
NNHISQEDCA KPTDLDKKNT EIKIDETGST PGYEGEGEGD KNISRKPGNV
860 870 880 890 900
LKTLDPILIT IIAMSALGVL LGAVCGVVLY CACWHNGMSE RNLSALENYN
910 920
FELVDGVKLK KDKLNPQSNY SEA
Length:923
Mass (Da):103,000
Last modified:July 27, 2011 - v2
Checksum:i23209818C5C42137
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68M → I in BAA08789 (PubMed:8748368).Curated1
Sequence conflicti170S → C in BAA08789 (PubMed:8748368).Curated1
Sequence conflicti601D → H in BAA08789 (PubMed:8748368).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50086 mRNA. Translation: BAA08789.1.
CH466525 Genomic DNA. Translation: EDL11828.1.
BC060129 mRNA. Translation: AAH60129.1.
CCDSiCCDS22790.1.
RefSeqiNP_032763.2. NM_008737.2.
XP_006530829.1. XM_006530766.3.
UniGeneiMm.271745.

Genome annotation databases

EnsembliENSMUST00000026917; ENSMUSP00000026917; ENSMUSG00000025810.
GeneIDi18186.
KEGGimmu:18186.
UCSCiuc009nzr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50086 mRNA. Translation: BAA08789.1.
CH466525 Genomic DNA. Translation: EDL11828.1.
BC060129 mRNA. Translation: AAH60129.1.
CCDSiCCDS22790.1.
RefSeqiNP_032763.2. NM_008737.2.
XP_006530829.1. XM_006530766.3.
UniGeneiMm.271745.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GZ9X-ray2.70A22-586[»]
4GZAX-ray7.00H22-586[»]
ProteinModelPortaliP97333.
SMRiP97333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201848. 5 interactors.
DIPiDIP-39360N.
IntActiP97333. 12 interactors.
MINTiMINT-99860.
STRINGi10090.ENSMUSP00000026917.

PTM databases

iPTMnetiP97333.
PhosphoSitePlusiP97333.
SwissPalmiP97333.

Proteomic databases

MaxQBiP97333.
PaxDbiP97333.
PeptideAtlasiP97333.
PRIDEiP97333.
TopDownProteomicsiP97333.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026917; ENSMUSP00000026917; ENSMUSG00000025810.
GeneIDi18186.
KEGGimmu:18186.
UCSCiuc009nzr.2. mouse.

Organism-specific databases

CTDi8829.
MGIiMGI:106206. Nrp1.

Phylogenomic databases

eggNOGiENOG410IE8T. Eukaryota.
ENOG410YRBE. LUCA.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000039978.
HOVERGENiHBG000502.
InParanoidiP97333.
KOiK06724.
OMAiYCACWHN.
OrthoDBiEOG091G017M.
TreeFamiTF316506.

Enzyme and pathway databases

ReactomeiR-MMU-194306. Neurophilin interactions with VEGF and VEGFR.
R-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-445144. Signal transduction by L1.
R-MMU-447041. CHL1 interactions.

Miscellaneous databases

ChiTaRSiNrp1. mouse.
PROiP97333.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025810.
CleanExiMM_NRP1.
GenevisibleiP97333. MM.

Family and domain databases

CDDicd00041. CUB. 2 hits.
cd06263. MAM. 1 hit.
Gene3Di2.60.120.260. 2 hits.
2.60.120.290. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000859. CUB_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR000998. MAM_dom.
IPR014648. Neuropilin.
IPR022579. Neuropilin_C.
IPR027146. NRP1.
[Graphical view]
PANTHERiPTHR10127:SF654. PTHR10127:SF654. 1 hit.
PfamiPF00431. CUB. 2 hits.
PF11980. DUF3481. 1 hit.
PF00754. F5_F8_type_C. 2 hits.
PF00629. MAM. 1 hit.
[Graphical view]
PIRSFiPIRSF036960. Neuropilin. 1 hit.
PRINTSiPR00020. MAMDOMAIN.
SMARTiSM00042. CUB. 2 hits.
SM00231. FA58C. 2 hits.
SM00137. MAM. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS01180. CUB. 2 hits.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNRP1_MOUSE
AccessioniPrimary (citable) accession number: P97333
Secondary accession number(s): Q6PAR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 164 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.