Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5IJ48 (CRUM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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:
Protein crumbs homolog 2
Alternative name(s):
Crumbs-like protein 2
Gene names
Name:CRB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1285 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in polarized cells morphogenesis.

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Tissue specificity

Expressed in retina, fetal eye and brain. Also expressed in kidney, ARPE-19 and RPE/choroid cell lines, and at low levels in lung, placenta, and heart. Ref.1

Sequence similarities

Belongs to the Crumbs protein family.

Contains 15 EGF-like domains.

Contains 3 laminin G-like domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiovascular system development

Inferred from sequence or structural similarity. Source: UniProt

maintenance of epithelial cell apical/basal polarity

Inferred from sequence or structural similarity. Source: UniProt

mesoderm formation

Inferred from sequence or structural similarity. Source: UniProt

negative regulation of endopeptidase activity

Inferred from mutant phenotype PubMed 20299451. Source: UniProt

notochord formation

Inferred from sequence or structural similarity. Source: UniProt

positive regulation of BMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProt

positive regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProt

somitogenesis

Inferred from sequence or structural similarity. Source: UniProt

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred by curator PubMed 20299451. Source: UniProt

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 20299451. Source: UniProt

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from mutant phenotype PubMed 20299451. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5IJ48-1)

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 2 (identifier: Q5IJ48-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1131-1176: LPVPSKECSL...GQRCQVPTLP → WDGWAGGWAA...VLICDMRRTV
     1177-1285: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5IJ48-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-332: Missing.
     333-351: GHCQDLPNGFQCHCPDGYA → MAMEPGALWTFLGHLWLLA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 12851257Protein crumbs homolog 2
PRO_0000007502

Regions

Topological domain29 – 12241196Extracellular Potential
Transmembrane1225 – 124521Helical; Potential
Topological domain1246 – 128540Cytoplasmic Potential
Domain67 – 10640EGF-like 1
Domain108 – 14437EGF-like 2; calcium-binding Potential
Domain146 – 18237EGF-like 3; calcium-binding Potential
Domain184 – 22138EGF-like 4; calcium-binding Potential
Domain223 – 25937EGF-like 5
Domain261 – 31858EGF-like 6
Domain320 – 35637EGF-like 7; calcium-binding Potential
Domain358 – 39437EGF-like 8; calcium-binding Potential
Domain396 – 43641EGF-like 9
Domain431 – 603173Laminin G-like 1
Domain605 – 64137EGF-like 10
Domain647 – 805159Laminin G-like 2
Domain807 – 84337EGF-like 11
Domain871 – 1054184Laminin G-like 3
Domain1056 – 109237EGF-like 12
Domain1094 – 113037EGF-like 13
Domain1134 – 117138EGF-like 14
Domain1173 – 120937EGF-like 15

Amino acid modifications

Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Potential
Glycosylation6901N-linked (GlcNAc...) Potential
Glycosylation7861N-linked (GlcNAc...) Potential
Glycosylation8001N-linked (GlcNAc...) Potential
Glycosylation8361N-linked (GlcNAc...) Potential
Glycosylation8861N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation10091N-linked (GlcNAc...) Potential
Glycosylation11411N-linked (GlcNAc...) Potential
Glycosylation11581N-linked (GlcNAc...) Potential
Disulfide bond71 ↔ 82 By similarity
Disulfide bond76 ↔ 94 By similarity
Disulfide bond96 ↔ 105 By similarity
Disulfide bond112 ↔ 123 By similarity
Disulfide bond117 ↔ 132 By similarity
Disulfide bond134 ↔ 143 By similarity
Disulfide bond150 ↔ 161 By similarity
Disulfide bond155 ↔ 170 By similarity
Disulfide bond172 ↔ 181 By similarity
Disulfide bond188 ↔ 199 By similarity
Disulfide bond193 ↔ 208 By similarity
Disulfide bond210 ↔ 220 By similarity
Disulfide bond227 ↔ 238 By similarity
Disulfide bond232 ↔ 247 By similarity
Disulfide bond249 ↔ 258 By similarity
Disulfide bond265 ↔ 276 By similarity
Disulfide bond270 ↔ 306 By similarity
Disulfide bond308 ↔ 317 By similarity
Disulfide bond324 ↔ 335 By similarity
Disulfide bond329 ↔ 344 By similarity
Disulfide bond346 ↔ 355 By similarity
Disulfide bond362 ↔ 373 By similarity
Disulfide bond367 ↔ 382 By similarity
Disulfide bond384 ↔ 393 By similarity
Disulfide bond400 ↔ 411 By similarity
Disulfide bond405 ↔ 424 By similarity
Disulfide bond426 ↔ 435 By similarity
Disulfide bond579 ↔ 603 By similarity
Disulfide bond609 ↔ 620 By similarity
Disulfide bond614 ↔ 629 By similarity
Disulfide bond631 ↔ 640 By similarity
Disulfide bond766 ↔ 805 By similarity
Disulfide bond811 ↔ 822 By similarity
Disulfide bond816 ↔ 831 By similarity
Disulfide bond833 ↔ 842 By similarity
Disulfide bond1013 ↔ 1054 By similarity
Disulfide bond1060 ↔ 1071 By similarity
Disulfide bond1065 ↔ 1080 By similarity
Disulfide bond1082 ↔ 1091 By similarity
Disulfide bond1098 ↔ 1108 By similarity
Disulfide bond1103 ↔ 1118 By similarity
Disulfide bond1120 ↔ 1129 By similarity
Disulfide bond1138 ↔ 1150 By similarity
Disulfide bond1144 ↔ 1159 By similarity
Disulfide bond1161 ↔ 1170 By similarity
Disulfide bond1177 ↔ 1188 By similarity
Disulfide bond1182 ↔ 1197 By similarity
Disulfide bond1199 ↔ 1208 By similarity

Natural variations

Alternative sequence1 – 332332Missing in isoform 3.
VSP_014737
Alternative sequence333 – 35119GHCQD…PDGYA → MAMEPGALWTFLGHLWLLA in isoform 3.
VSP_014738
Alternative sequence1131 – 117646LPVPS…VPTLP → WDGWAGGWAANAPWGYGGAE KSARSVDESLPFPGPHVLIC DMRRTV in isoform 2.
VSP_014739
Alternative sequence1177 – 1285109Missing in isoform 2.
VSP_014740
Natural variant461P → L. Ref.1
Corresponds to variant rs73571404 [ dbSNP | Ensembl ].
VAR_022984
Natural variant901T → N. Ref.2
Corresponds to variant rs2808415 [ dbSNP | Ensembl ].
VAR_048974
Natural variant971V → L. Ref.1
VAR_022985
Natural variant1161P → L. Ref.1
VAR_022986
Natural variant1451M → T. Ref.1 Ref.2
Corresponds to variant rs1105223 [ dbSNP | Ensembl ].
VAR_022987
Natural variant1591G → A. Ref.1 Ref.2
Corresponds to variant rs1105222 [ dbSNP | Ensembl ].
VAR_022988
Natural variant1871E → D. Ref.1
VAR_022989
Natural variant3511A → T. Ref.1
VAR_022990
Natural variant5341R → Q. Ref.1
VAR_022991
Natural variant6101R → W. Ref.1
Corresponds to variant rs145286619 [ dbSNP | Ensembl ].
VAR_022992
Natural variant7091V → A. Ref.1 Ref.2
Corresponds to variant rs2488602 [ dbSNP | Ensembl ].
VAR_061153
Natural variant7461H → Q. Ref.1
VAR_022993
Natural variant11101T → M. Ref.1
Corresponds to variant rs73571431 [ dbSNP | Ensembl ].
VAR_022994

Experimental info

Sequence conflict4301T → A in BAC86684. Ref.2
Sequence conflict9691T → A in AK123000. Ref.2
Sequence conflict9691T → A in BAC86684. Ref.2
Sequence conflict11531G → R in BAC86684. Ref.2
Sequence conflict12391Missing in BAC86684. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: C5B7E9D7A91CD703

FASTA1,285134,265
        10         20         30         40         50         60 
MALARPGTPD PQALASVLLL LLWAPALSLL AGTVPSEPPS ACASDPCAPG TECQATESGG 

        70         80         90        100        110        120 
YTCGPMEPRG CATQPCHHGA LCVPQGPDPT GFRCYCVPGF QGPRCELDID ECASRPCHHG 

       130        140        150        160        170        180 
ATCRNLADRY ECHCPLGYAG VTCEMEVDEC ASAPCLHGGS CLDGVGSFRC VCAPGYGGTR 

       190        200        210        220        230        240 
CQLDLDECQS QPCAHGGTCH DLVNGFRCDC AGTGYEGTHC EREVLECASA PCEHNASCLE 

       250        260        270        280        290        300 
GLGSFRCLCW PGYSGELCEV DEDECASSPC QHGGRCLQRS DPALYGGVQA AFPGAFSFRH 

       310        320        330        340        350        360 
AAGFLCHCPP GFEGADCGVE VDECASRPCL NGGHCQDLPN GFQCHCPDGY AGPTCEEDVD 

       370        380        390        400        410        420 
ECLSDPCLHG GTCSDTVAGY ICRCPETWGG RDCSVQLTGC QGHTCPLAAT CIPIFESGVH 

       430        440        450        460        470        480 
SYVCHCPPGT HGPFCGQNTT FSVMAGSPIQ ASVPAGGPLG LALRFRTTLP AGTLATRNDT 

       490        500        510        520        530        540 
KESLELALVA ATLQATLWSY STTVLVLRLP DLALNDGHWH QVEVVLHLAT LELRLWHEGC 

       550        560        570        580        590        600 
PARLCVASGP VALASTASAT PLPAGISSAQ LGDATFAGCL QDVRVDGHLL LPEDLGENVL 

       610        620        630        640        650        660 
LGCERREQCR PLPCVHGGSC VDLWTHFRCD CARPHRGPTC ADEIPAATFG LGGAPSSASF 

       670        680        690        700        710        720 
LLQELPGPNL TVSFLLRTRE SAGLLLQFAN DSAAGLTVFL SEGRIRAEVP GSPAVVLPGR 

       730        740        750        760        770        780 
WDDGLRHLVM LSFGPDQLQD LGQHVHVGGR LLAADSQPWG GPFRGCLQDL RLDGCHLPFF 

       790        800        810        820        830        840 
PLPLDNSSQP SELGGRQSWN LTAGCVSEDM CSPDPCFNGG TCLVTWNDFH CTCPANFTGP 

       850        860        870        880        890        900 
TCAQQLWCPG QPCLPPATCE EVPDGFVCVA EATFREGPPA AFSGHNASSG RLLGGLSLAF 

       910        920        930        940        950        960 
RTRDSEAWLL RAAAGALEGV WLAVRNGSLA GGVRGGHGLP GAVLPIPGPR VADGAWHRVR 

       970        980        990       1000       1010       1020 
LAMERPAATT SRWLLWLDGA ATPVALRGLA SDLGFLQGPG AVRILLAENF TGCLGRVALG 

      1030       1040       1050       1060       1070       1080 
GLPLPLARPR PGAAPGAREH FASWPGTPAP ILGCRGAPVC APSPCLHDGA CRDLFDAFAC 

      1090       1100       1110       1120       1130       1140 
ACGPGWEGPR CEAHVDPCHS APCARGRCHT HPDGRFECRC PPGFGGPRCR LPVPSKECSL 

      1150       1160       1170       1180       1190       1200 
NVTCLDGSPC EGGSPAANCS CLEGLAGQRC QVPTLPCEAN PCLNGGTCRA AGGVSECICN 

      1210       1220       1230       1240       1250       1260 
ARFSGQFCEV AKGLPLPLPF PLLEVAVPAA CACLLLLLLG LLSGILAARK RRQSEGTYSP 

      1270       1280 
SQQEVAGARL EMDSVLKVPP EERLI 

« Hide

Isoform 2 [UniParc].

Checksum: A33CB9D605EDE5A0
Show »

FASTA1,176123,213
Isoform 3 [UniParc].

Checksum: 277A62189E3BEC0D
Show »

FASTA95399,830

References

« Hide 'large scale' references
[1]"Characterization of the crumbs homolog 2 (CRB2) gene and analysis of its role in retinitis pigmentosa and Leber congenital amaurosis."
van den Hurk J.A.J.M., Rashbass P., Roepman R., Davis J., Voesenek K.E.J., Arends M.L., Zonneveld M.N., van Roekel M.H.G., Cameron K., Rohrschneider K., Heckenlively J.R., Koenekoop R.K., Hoyng C.B., Cremers F.P.M., den Hollander A.I.
Mol. Vis. 11:263-273(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS LEU-46; LEU-97; LEU-116; THR-145; ALA-159; ASP-187; THR-351; GLN-534; TRP-610; ALA-709; GLN-746 AND MET-1110.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANTS ASN-90; THR-145; ALA-159 AND ALA-709.
Tissue: Cerebellum.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Roni V., Carpio R., Wissinger B.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
Tissue: Retina.
[5]"The crystal structure of the human dual specificity tyrosine-phosphorylation-regulated kinase 1A."
Structural genomics consortium (SGC)
Submitted (AUG-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-9 IN COMPLEX WITH DYRK1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY720432 mRNA. Translation: AAU14134.1.
AK123000 mRNA. No translation available.
AK126775 mRNA. Translation: BAC86684.1.
AL445489, AL365504 Genomic DNA. Translation: CAI39793.1.
AL365504, AL445489 Genomic DNA. Translation: CAI41011.1.
AL445489, AL365504 Genomic DNA. Translation: CAM14433.1.
AL365504, AL445489 Genomic DNA. Translation: CAM21391.1.
DQ426866 mRNA. Translation: ABD90532.1.
CCDSCCDS6852.2. [Q5IJ48-1]
RefSeqNP_775960.4. NM_173689.6. [Q5IJ48-1]
XP_005251991.1. XM_005251934.1. [Q5IJ48-3]
UniGeneHs.568340.
Hs.710092.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WO6X-ray2.50C4-9[»]
ProteinModelPortalQ5IJ48.
SMRQ5IJ48. Positions 37-438, 440-705, 828-881, 1060-1210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130332. 2 interactions.
STRING9606.ENSP00000362734.

PTM databases

PhosphoSiteQ5IJ48.

Polymorphism databases

DMDM116241316.

Proteomic databases

PaxDbQ5IJ48.
PRIDEQ5IJ48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359999; ENSP00000353092; ENSG00000148204. [Q5IJ48-2]
ENST00000373629; ENSP00000362732; ENSG00000148204. [Q5IJ48-3]
ENST00000373631; ENSP00000362734; ENSG00000148204. [Q5IJ48-1]
ENST00000460253; ENSP00000435279; ENSG00000148204. [Q5IJ48-3]
GeneID286204.
KEGGhsa:286204.
UCSCuc004bnw.1. human. [Q5IJ48-2]
uc004bnx.1. human. [Q5IJ48-1]

Organism-specific databases

CTD286204.
GeneCardsGC09P126118.
H-InvDBHIX0008365.
HGNCHGNC:18688. CRB2.
HPAHPA043674.
MIM609720. gene.
neXtProtNX_Q5IJ48.
PharmGKBPA134910460.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG080001.
InParanoidQ5IJ48.
KOK16681.
OMAGACVDLW.
OrthoDBEOG7PVWNH.
PhylomeDBQ5IJ48.
TreeFamTF316224.

Gene expression databases

BgeeQ5IJ48.
CleanExHS_CRB2.
GenevestigatorQ5IJ48.

Family and domain databases

Gene3D2.60.120.200. 4 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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.
IPR001791. Laminin_G.
[Graphical view]
PfamPF00008. EGF. 7 hits.
PF12661. hEGF. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
SMARTSM00181. EGF. 9 hits.
SM00179. EGF_CA. 6 hits.
SM00282. LamG. 3 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 3 hits.
PROSITEPS00010. ASX_HYDROXYL. 7 hits.
PS00022. EGF_1. 14 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 5 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5IJ48.
GenomeRNAi286204.
NextBio96074.
PROQ5IJ48.
SOURCESearch...

Entry information

Entry nameCRUM2_HUMAN
AccessionPrimary (citable) accession number: Q5IJ48
Secondary accession number(s): A2A3N4 expand/collapse secondary AC list , Q0QD46, Q5JS41, Q5JS43, Q6ZTA9, Q6ZWI6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 101 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 9

Human chromosome 9: entries, gene names and cross-references to MIM