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O60462 (NRP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuropilin-2
Alternative name(s):
Vascular endothelial cell growth factor 165 receptor 2
Gene names
Name:NRP2
Synonyms:VEGF165R2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length931 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform ofPGF.

Subunit structure

Heterodimer with NRP1. Binds PLXNB1. Ref.9

Subcellular location

Membrane; Single-pass type I membrane protein Ref.3.

Isoform s9: Secreted Ref.3.

Domain

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

Sequence similarities

Belongs to the neuropilin family.

Contains 2 CUB domains.

Contains 2 F5/8 type C domains.

Contains 1 MAM domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Heparin-binding
Metal-binding
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Non-traceable author statement Ref.3. Source: UniProtKB

axon extension involved in axon guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

axon guidance

Non-traceable author statement PubMed 19909241. Source: BHF-UCL

cell adhesion

Non-traceable author statement Ref.3. Source: UniProtKB

heart development

Inferred from electronic annotation. Source: Ensembl

negative chemotaxis

Inferred from electronic annotation. Source: Ensembl

nerve development

Inferred from sequence or structural similarity. Source: BHF-UCL

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell migration

Traceable author statement PubMed 21245381. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Traceable author statement PubMed 21245381. Source: BHF-UCL

semaphorin-plexin signaling pathway involved in neuron projection guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

sympathetic ganglion development

Inferred from sequence or structural similarity. Source: BHF-UCL

sympathetic neuron projection extension

Inferred from sequence or structural similarity. Source: BHF-UCL

sympathetic neuron projection guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

vascular endothelial growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Non-traceable author statement Ref.3. Source: UniProtKB

membrane

Traceable author statement PubMed 9288754. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

semaphorin receptor complex

Non-traceable author statement PubMed 19909241. Source: BHF-UCL

   Molecular_functioncytokine binding

Non-traceable author statement PubMed 19909241. Source: BHF-UCL

growth factor binding

Traceable author statement PubMed 21245381. Source: BHF-UCL

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor activity

Traceable author statement PubMed 9288754. Source: ProtInc

semaphorin receptor activity

Non-traceable author statement Ref.3. Source: UniProtKB

vascular endothelial growth factor-activated receptor activity

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform A22 (identifier: O60462-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A0 (identifier: O60462-2)

The sequence of this isoform differs from the canonical sequence as follows:
     809-830: Missing.
Isoform A17 (identifier: O60462-3)

The sequence of this isoform differs from the canonical sequence as follows:
     809-813: Missing.
Isoform B0 (identifier: O60462-4)

The sequence of this isoform differs from the canonical sequence as follows:
     809-813: Missing.
     814-931: VDIPEIHERE...MNHQKCCSEA → GGTLLPGTEP...KLEQDRGSHC
Isoform B5 (identifier: O60462-5)

The sequence of this isoform differs from the canonical sequence as follows:
     814-931: VDIPEIHERE...MNHQKCCSEA → GGTLLPGTEP...KLEQDRGSHC
Isoform s9 (identifier: O60462-6)

The sequence of this isoform differs from the canonical sequence as follows:
     548-555: LFEGNMHY → VGCSWRPL
     556-931: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020Or 22 Potential
Chain21 – 931911Neuropilin-2
PRO_0000021863

Regions

Topological domain21 – 864844Extracellular Potential
Transmembrane865 – 88925Helical; Potential
Topological domain890 – 93142Cytoplasmic Potential
Domain28 – 142115CUB 1
Domain149 – 267119CUB 2
Domain277 – 427151F5/8 type C 1
Domain434 – 592159F5/8 type C 2
Domain642 – 802161MAM
Compositional bias671 – 6744Poly-Ser

Sites

Metal binding1971Calcium
Metal binding2111Calcium
Metal binding2521Calcium

Amino acid modifications

Glycosylation1521N-linked (GlcNAc...)
Glycosylation1571N-linked (GlcNAc...)
Glycosylation6291N-linked (GlcNAc...) Potential
Glycosylation8391N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 55 Ref.9
Disulfide bond83 ↔ 105 Ref.9
Disulfide bond149 ↔ 175 Ref.9
Disulfide bond208 ↔ 230 Ref.9
Disulfide bond277 ↔ 427 Ref.9
Disulfide bond434 ↔ 592 Ref.9

Natural variations

Alternative sequence548 – 5558LFEGNMHY → VGCSWRPL in isoform s9.
VSP_044908
Alternative sequence556 – 931376Missing in isoform s9.
VSP_044909
Alternative sequence809 – 83022Missing in isoform A0.
VSP_004342
Alternative sequence809 – 8135Missing in isoform A17 and isoform B0.
VSP_004341
Alternative sequence814 – 931118VDIPE…CCSEA → GGTLLPGTEPTVDTVPMQPI PAYWYYVMAAGGAVLVLVSV ALALVLHYHRFRYAAKKTDH SITYKTSHYTNGAPLAVEPT LTIKLEQDRGSHC in isoform B0 and isoform B5.
VSP_041160
Natural variant1231R → K. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs849541 [ dbSNP | Ensembl ].
VAR_047754
Natural variant3341R → C Rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations. Ref.10
Corresponds to variant rs114144673 [ dbSNP | Ensembl ].
VAR_067537
Natural variant4281R → W Rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations. Ref.10
Corresponds to variant rs139711818 [ dbSNP | Ensembl ].
VAR_067538
Natural variant6021E → K. Ref.1 Ref.3
Corresponds to variant rs1128169 [ dbSNP | Ensembl ].
VAR_065167

Secondary structure

........................................................................................................ 931
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A22 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: EA5CDBB67F3C4B7D

FASTA931104,859
        10         20         30         40         50         60 
MDMFPLTWVF LALYFSRHQV RGQPDPPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY 

        70         80         90        100        110        120 
APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSML 

       130        140        150        160        170        180 
YIRFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL 

       190        200        210        220        230        240 
AKPKMEIILQ FLIFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSELRS 

       250        260        270        280        290        300 
STGILSLTFH TDMAVAKDGF SARYYLVHQE PLENFQCNVP LGMESGRIAN EQISASSTYS 

       310        320        330        340        350        360 
DGRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQNGYYVKS 

       370        380        390        400        410        420 
YKLEVSTNGE DWMVYRHGKN HKVFQANNDA TEVVLNKLHA PLLTRFVRIR PQTWHSGIAL 

       430        440        450        460        470        480 
RLELFGCRVT DAPCSNMLGM LSGLIADSQI SASSTQEYLW SPSAARLVSS RSGWFPRIPQ 

       490        500        510        520        530        540 
AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD 

       550        560        570        580        590        600 
PRTQQPKLFE GNMHYDTPDI RRFDPIPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT 

       610        620        630        640        650        660 
VETLGPTVKS EETTTPYPTE EEATECGENC SFEDDKDLQL PSGFNCNFDF LEEPCGWMYD 

       670        680        690        700        710        720 
HAKWLRTTWA SSSSPNDRTF PDDRNFLRLQ SDSQREGQYA RLISPPVHLP RSPVCMEFQY 

       730        740        750        760        770        780 
QATGGRGVAL QVVREASQES KLLWVIREDQ GGEWKHGRII LPSYDMEYQI VFEGVIGKGR 

       790        800        810        820        830        840 
SGEIAIDDIR ISTDVPLENC MEPISAFAGE NFKVDIPEIH EREGYEDEID DEYEVDWSNS 

       850        860        870        880        890        900 
SSATSGSGAP STDKEKSWLY TLDPILITII AMSSLGVLLG ATCAGLLLYC TCSYSGLSSR 

       910        920        930 
SCTTLENYNF ELYDGLKHKV KMNHQKCCSE A 

« Hide

Isoform A0 [UniParc].

Checksum: 7B0CE20AB8157EE8
Show »

FASTA909102,243
Isoform A17 [UniParc].

Checksum: A6320C5DFA7785A5
Show »

FASTA926104,283
Isoform B0 [UniParc].

Checksum: D9F51B545CEC6DD8
Show »

FASTA901101,409
Isoform B5 [UniParc].

Checksum: 9C83C9EB47FF74A1
Show »

FASTA906101,985
Isoform s9 [UniParc].

Checksum: 32CFC8C974D6358E
Show »

FASTA55562,458

References

« Hide 'large scale' references
[1]"Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III."
Chen H., Chedotal A., He Z.-G., Goodman C.S., Tessier-Lavigne M.
Neuron 19:547-559(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A0 AND A17), VARIANTS LYS-123 AND LYS-602.
[2]"Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor."
Soker S., Takashima S., Miao H.-Q., Neufeld G., Klagsbrun M.
Cell 92:735-745(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A22), VARIANT LYS-123.
Tissue: Mammary gland.
[3]"Genomic organization of human neuropilin-1 and neuropilin-2 genes: identification and distribution of splice variants and soluble isoforms."
Rossignol M., Gagnon M.L., Klagsbrun M.
Genomics 70:211-222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS B0; B5 AND S9), VARIANTS LYS-123 AND LYS-602, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (ISOFORM S9).
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-123.
[6]"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] (ISOFORMS B0 AND B5), VARIANT LYS-123.
Tissue: Brain.
[7]"Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165."
Gluzman-Poltorak Z., Cohen T., Herzog Y., Neufeld G.
J. Biol. Chem. 275:18040-18045(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Plexins are a large family of receptors for transmembrane, secreted and GPI-anchored semaphorins in vertebrates."
Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L., Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., Tessier-Lavigne M., Comoglio P.M.
Cell 99:71-80(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1.
[9]"Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding."
Appleton B.A., Wu P., Maloney J., Yin J., Liang W.C., Stawicki S., Mortara K., Bowman K.K., Elliott J.M., Desmarais W., Bazan J.F., Bagri A., Tessier-Lavigne M., Koch A.W., Wu Y., Watts R.J., Wiesmann C.
EMBO J. 26:4902-4912(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 23-595 ALONE AND IN COMPLEX WITH ANTIBODY, SUBUNIT, CALCIUM-BINDING SITES, DISULFIDE BONDS.
[10]"De Novo Pathogenic SCN8A Mutation Identified by Whole-Genome Sequencing of a Family Quartet Affected by Infantile Epileptic Encephalopathy and SUDEP."
Veeramah K.R., O'Brien J.E., Meisler M.H., Cheng X., Dib-Hajj S.D., Waxman S.G., Talwar D., Girirajan S., Eichler E.E., Restifo L.L., Erickson R.P., Hammer M.F.
Am. J. Hum. Genet. 90:502-510(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-334 AND TRP-428.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF022859 mRNA. Translation: AAC51788.1.
AF022860 mRNA. Translation: AAC51789.1.
AF016098 mRNA. Translation: AAC12922.1.
AF280544 mRNA. Translation: AAG41403.1.
AF280545 mRNA. Translation: AAG41404.1.
AF280546 mRNA. Translation: AAG41405.1.
AF281074 Genomic DNA. Translation: AAG41898.1.
AF281074 Genomic DNA. Translation: AAG41899.1.
AF281074 Genomic DNA. Translation: AAG41900.1.
AC007362 Genomic DNA. Translation: AAX93216.1.
AC007561 Genomic DNA. Translation: AAY14875.1.
CH471063 Genomic DNA. Translation: EAW70362.1.
CH471063 Genomic DNA. Translation: EAW70364.1.
CH471063 Genomic DNA. Translation: EAW70366.1.
CH471063 Genomic DNA. Translation: EAW70368.1.
BC101525 mRNA. Translation: AAI01526.1.
BC104770 mRNA. Translation: AAI04771.1.
BC143238 mRNA. Translation: AAI43239.1.
CCDSCCDS2364.1. [O60462-1]
CCDS2365.1. [O60462-5]
CCDS46496.1. [O60462-3]
CCDS46497.1. [O60462-2]
CCDS46498.1. [O60462-4]
CCDS46499.1. [O60462-6]
RefSeqNP_003863.2. NM_003872.2.
NP_061004.3. NM_018534.3.
NP_957716.1. NM_201264.1.
NP_957718.1. NM_201266.1.
NP_957719.1. NM_201267.1.
NP_958436.1. NM_201279.1.
XP_005246990.2. XM_005246933.2.
XP_005246991.2. XM_005246934.2.
UniGeneHs.471200.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QQJX-ray1.95A275-595[»]
2QQKX-ray2.75A23-595[»]
2QQLX-ray3.10A23-595[»]
2QQOX-ray2.30A/B145-595[»]
ProteinModelPortalO60462.
SMRO60462. Positions 26-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114355. 2 interactions.
DIPDIP-5745N.
STRING9606.ENSP00000353582.

PTM databases

PhosphoSiteO60462.

Proteomic databases

MaxQBO60462.
PaxDbO60462.
PRIDEO60462.

Protocols and materials databases

DNASU8828.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272849; ENSP00000272849; ENSG00000118257. [O60462-5]
ENST00000355117; ENSP00000347238; ENSG00000118257. [O60462-6]
ENST00000357118; ENSP00000349632; ENSG00000118257. [O60462-4]
ENST00000357785; ENSP00000350432; ENSG00000118257. [O60462-3]
ENST00000360409; ENSP00000353582; ENSG00000118257. [O60462-1]
ENST00000412873; ENSP00000407626; ENSG00000118257. [O60462-2]
ENST00000417189; ENSP00000387519; ENSG00000118257. [O60462-6]
GeneID8828.
KEGGhsa:8828.
UCSCuc002vau.3. human. [O60462-5]
uc002vav.3. human. [O60462-4]
uc002vaw.3. human. [O60462-1]
uc002vay.3. human. [O60462-2]
uc010fud.3. human.

Organism-specific databases

CTD8828.
GeneCardsGC02P206510.
HGNCHGNC:8005. NRP2.
HPAHPA039980.
MIM602070. gene.
neXtProtNX_O60462.
PharmGKBPA31784.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150152.
HOVERGENHBG000502.
InParanoidO60462.
KOK06819.
OMANKLHTPL.
OrthoDBEOG7ZWD1D.
PhylomeDBO60462.
TreeFamTF316506.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO60462.
BgeeO60462.
CleanExHS_NRP2.
GenevestigatorO60462.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
2.60.120.290. 2 hits.
InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR000859. CUB_dom.
IPR008979. Galactose-bd-like.
IPR000998. MAM_dom.
IPR014648. Neuropilin.
IPR022579. Neuropilin1_C.
[Graphical view]
PfamPF00431. CUB. 2 hits.
PF11980. DUF3481. 1 hit.
PF00754. F5_F8_type_C. 2 hits.
PF00629. MAM. 1 hit.
[Graphical view]
PIRSFPIRSF036960. Neuropilin. 1 hit.
PRINTSPR00020. MAMDOMAIN.
SMARTSM00042. CUB. 2 hits.
SM00231. FA58C. 2 hits.
SM00137. MAM. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
SSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEPS01180. CUB. 2 hits.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS50060. MAM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNRP2. human.
EvolutionaryTraceO60462.
GeneWikiNRP2.
GenomeRNAi8828.
NextBio33120.
PROO60462.
SOURCESearch...

Entry information

Entry nameNRP2_HUMAN
AccessionPrimary (citable) accession number: O60462
Secondary accession number(s): E9PF66 expand/collapse secondary AC list , O14820, O14821, Q53TQ4, Q53TS3, Q7LBX7, Q9H2D4, Q9H2D5, Q9H2E2, Q9H2E3, Q9H2E4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM