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

P82279 (CRUM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein crumbs homolog 1
Gene names
Name:CRB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion.

Subunit structure

Forms a complex with MPDZ By similarity. Forms a complex with MPP4 and MPP5.

Subcellular location

Isoform 1: Apical cell membrane; Single-pass type I membrane protein. Note: Distributed at the apical membrane of all retinal epithelial cells. Located in the apical membrane of the adherens junction in outer limiting membrane (OLM) of the retina. Ref.3

Isoform 2: Secreted Ref.3.

Tissue specificity

Preferential expression in retina, also expressed in brain, testis, fetal brain and fetal eye. Ref.3

Post-translational modification

Extensively glycosylated.

Involvement in disease

CRB1 mutations have been found in various retinal dystrophies, chronic and disabling disorders of visual function. They predominantly involve the posterior portion of the ocular fundus, due to degeneration in the sensory layer of the retina, retinal pigment epithelium, Bruch membrane, choroid, or a combination of these tissues. Onset of inherited retinal dystrophies is painless, bilateral and typically progressive. Most people experience gradual peripheral vision loss or tunnel vision, and difficulties with poor illumination and night vision. Central vision is usually unaffected, so the person may still be able to read. However, it can also deteriorate to cause total blindness. Examples of retinal dystrophies are retinitis pigmentosa, Leber congenital amaurosis, cone-rod dystrophy among others.

Retinitis pigmentosa 12 (RP12) [MIM:600105]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP12 is an autosomal recessive, severe form often manifesting in early childhood. Patients experiment progressive visual field loss with severe visual impairment before the age of twenty. Some patients have a preserved paraarteriolar retinal pigment epithelium (PPRPE) and hypermetropia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39

Leber congenital amaurosis 8 (LCA8) [MIM:613835]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.35 Ref.37

Pigmented paravenous chorioretinal atrophy (PPCRA) [MIM:172870]: Unusual retinal degeneration characterized by accumulation of pigmentation along retinal veins. PPCRA is dominantly inherited, but exhibited variable expressivity. Males are more likely to exhibit a severe phenotype, whereas females may remain virtually asymptomatic even in later years. The PPCRA phenotype is associated with a mutation in CRB1 gene which is likely to affect the structure of the CRB1 protein.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the Crumbs protein family.

Contains 19 EGF-like domains.

Contains 3 laminin G-like domains.

Sequence caution

The sequence CAE45845.1 differs from that shown. Reason: Erroneous termination at position 567. Translated as Trp.

The sequence CAI16644.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

INADLQ8NI352EBI-1048648,EBI-724390

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P82279-1)

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: P82279-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1336-1376: LADDLISDIF...VVTSNKRATQ → VSSLSFYVSL...VVEWGEQEDY
     1377-1406: Missing.
Isoform 3 (identifier: P82279-3)

The sequence of this isoform differs from the canonical sequence as follows:
     218-329: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P82279-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-351: Missing.
     352-390: GECVELSSEK...YVCICQPGFT → MIRNSLCQPS...GFHILMAMLI
     1294-1406: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P82279-5)

The sequence of this isoform differs from the canonical sequence as follows:
     710-1245: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 14061381Protein crumbs homolog 1
PRO_0000007500

Regions

Topological domain26 – 13471322Extracellular Potential
Transmembrane1348 – 136821Helical; Potential
Topological domain1369 – 140638Cytoplasmic Potential
Domain30 – 6839EGF-like 1
Domain70 – 10839EGF-like 2
Domain110 – 14637EGF-like 3
Domain148 – 18437EGF-like 4; calcium-binding Potential
Domain186 – 22237EGF-like 5; calcium-binding Potential
Domain224 – 26037EGF-like 6; calcium-binding Potential
Domain262 – 29938EGF-like 7; calcium-binding Potential
Domain301 – 33737EGF-like 8
Domain339 – 39557EGF-like 9
Domain397 – 43943EGF-like 10; calcium-binding Potential
Domain441 – 48141EGF-like 11
Domain485 – 670186Laminin G-like 1
Domain672 – 70837EGF-like 12
Domain714 – 885172Laminin G-like 2
Domain887 – 92337EGF-like 13
Domain924 – 96037EGF-like 14
Domain950 – 1137188Laminin G-like 3
Domain1139 – 117537EGF-like 15
Domain1177 – 121236EGF-like 16; calcium-binding Potential
Domain1214 – 125037EGF-like 17
Domain1255 – 129541EGF-like 18
Domain1297 – 133337EGF-like 19; calcium-binding Potential

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation5611N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Potential
Glycosylation7571N-linked (GlcNAc...) Potential
Glycosylation8711N-linked (GlcNAc...) Potential
Glycosylation8801N-linked (GlcNAc...) Potential
Glycosylation9681N-linked (GlcNAc...) Potential
Glycosylation9751N-linked (GlcNAc...) Potential
Glycosylation10001N-linked (GlcNAc...) Potential
Glycosylation11901N-linked (GlcNAc...) Potential
Glycosylation12431N-linked (GlcNAc...) Potential
Glycosylation12651N-linked (GlcNAc...) Potential
Glycosylation12731N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 45 By similarity
Disulfide bond39 ↔ 54 By similarity
Disulfide bond56 ↔ 67 By similarity
Disulfide bond74 ↔ 85 By similarity
Disulfide bond79 ↔ 96 By similarity
Disulfide bond98 ↔ 107 By similarity
Disulfide bond114 ↔ 125 By similarity
Disulfide bond119 ↔ 134 By similarity
Disulfide bond136 ↔ 145 By similarity
Disulfide bond152 ↔ 163 By similarity
Disulfide bond157 ↔ 172 By similarity
Disulfide bond174 ↔ 183 By similarity
Disulfide bond190 ↔ 201 By similarity
Disulfide bond195 ↔ 210 By similarity
Disulfide bond212 ↔ 221 By similarity
Disulfide bond228 ↔ 239 By similarity
Disulfide bond233 ↔ 248 By similarity
Disulfide bond250 ↔ 259 By similarity
Disulfide bond266 ↔ 277 By similarity
Disulfide bond271 ↔ 286 By similarity
Disulfide bond288 ↔ 298 By similarity
Disulfide bond305 ↔ 316 By similarity
Disulfide bond310 ↔ 325 By similarity
Disulfide bond327 ↔ 336 By similarity
Disulfide bond343 ↔ 354 By similarity
Disulfide bond348 ↔ 383 By similarity
Disulfide bond385 ↔ 394 By similarity
Disulfide bond401 ↔ 412 By similarity
Disulfide bond406 ↔ 421 By similarity
Disulfide bond423 ↔ 438 By similarity
Disulfide bond445 ↔ 456 By similarity
Disulfide bond450 ↔ 469 By similarity
Disulfide bond471 ↔ 480 By similarity
Disulfide bond642 ↔ 670 By similarity
Disulfide bond676 ↔ 687 By similarity
Disulfide bond681 ↔ 696 By similarity
Disulfide bond698 ↔ 707 By similarity
Disulfide bond851 ↔ 885 By similarity
Disulfide bond891 ↔ 902 By similarity
Disulfide bond896 ↔ 911 By similarity
Disulfide bond913 ↔ 922 By similarity
Disulfide bond928 ↔ 939 By similarity
Disulfide bond933 ↔ 948 By similarity
Disulfide bond1096 ↔ 1137 By similarity
Disulfide bond1143 ↔ 1154 By similarity
Disulfide bond1148 ↔ 1163 By similarity
Disulfide bond1165 ↔ 1174 By similarity
Disulfide bond1181 ↔ 1191 By similarity
Disulfide bond1186 ↔ 1200 By similarity
Disulfide bond1202 ↔ 1211 By similarity
Disulfide bond1218 ↔ 1229 By similarity
Disulfide bond1223 ↔ 1238 By similarity
Disulfide bond1240 ↔ 1249 By similarity
Disulfide bond1259 ↔ 1274 By similarity
Disulfide bond1268 ↔ 1283 By similarity
Disulfide bond1285 ↔ 1294 By similarity
Disulfide bond1301 ↔ 1312 By similarity
Disulfide bond1306 ↔ 1321 By similarity
Disulfide bond1323 ↔ 1332 By similarity

Natural variations

Alternative sequence1 – 351351Missing in isoform 4.
VSP_014724
Alternative sequence218 – 329112Missing in isoform 3.
VSP_014725
Alternative sequence352 – 39039GECVE…QPGFT → MIRNSLCQPSRCLDEYLFFN RKMFGARTHGFHILMAMLI in isoform 4.
VSP_014726
Alternative sequence710 – 1245536Missing in isoform 5.
VSP_045332
Alternative sequence1294 – 1406113Missing in isoform 4.
VSP_014727
Alternative sequence1336 – 137641LADDL…KRATQ → VSSLSFYVSLLFWQNLFQLL SYLILRMNDEPVVEWGEQED Y in isoform 2.
VSP_014728
Alternative sequence1377 – 140630Missing in isoform 2.
VSP_014729
Natural variant271C → F in RP12. Ref.30
VAR_064180
Natural variant451C → W in RP12. Ref.33
VAR_067125
Natural variant1441F → V in LCA8. Ref.12
Corresponds to variant rs62636262 [ dbSNP | Ensembl ].
VAR_022941
Natural variant1571C → S in RP12. Ref.35
VAR_067126
Natural variant1611A → V in RP12. Ref.1
VAR_011641
Natural variant1621V → M in PPCRA. Ref.19
Corresponds to variant rs137853138 [ dbSNP | Ensembl ].
VAR_022942
Natural variant165 – 1673Missing in RP12.
VAR_067127
Natural variant1951C → F in RP12. Ref.18
VAR_022943
Natural variant2051I → T Found in patients with Leber congenital amaurosis; unknown pathological significance. Ref.16 Ref.18 Ref.35
VAR_022944
Natural variant2221E → K. Ref.37
Corresponds to variant rs114846212 [ dbSNP | Ensembl ].
VAR_067128
Natural variant2501C → W in RP12. Ref.1 Ref.35
VAR_011642
Natural variant2891T → M Rare variant found in patients with retinal dystrophy; does not segregate with the disease in a family; unlikely to be pathogenic. Ref.10 Ref.12 Ref.16 Ref.26 Ref.37
VAR_022945
Natural variant3101C → Y Probable disease-associated mutation found in patients with early-onset retinal dystrophy. Ref.32
VAR_067129
Natural variant3121N → K in RP12. Ref.35
VAR_067130
Natural variant3331G → D in LCA8. Ref.28
VAR_067131
Natural variant3831C → Y in LCA8. Ref.12
VAR_022946
Natural variant4331Y → C in RP12. Ref.10
VAR_022947
Natural variant4381C → Y in LCA8. Ref.26
VAR_067132
Natural variant4541G → R in LCA8. Ref.23
VAR_067133
Natural variant4801C → G in LCA8. Ref.12
VAR_022948
Natural variant4801C → R in LCA8. Ref.12 Ref.21
VAR_022949
Natural variant4881F → S. Ref.21
VAR_067134
Natural variant4911D → V Found in a patient with early-onset retinal dystrophy; unknown pathological significance. Ref.32
VAR_067135
Natural variant5341K → N in RP12. Ref.39
VAR_068363
Natural variant5351L → P in LCA8. Ref.25
VAR_067136
Natural variant5641D → Y in LCA8. Ref.22
VAR_067137
Natural variant5781V → E in RP12. Ref.18
VAR_022950
Natural variant5841D → Y in LCA8. Ref.17 Ref.38
VAR_022951
Natural variant5871C → Y in RP12. Ref.18
VAR_022952
Natural variant6351S → P Found in a patient with Leber congenital amaurosis; unknown pathological significance. Ref.37
VAR_067138
Natural variant6751W → C in RP12. Ref.35
VAR_067139
Natural variant6791Q → E. Ref.16
VAR_022953
Natural variant6811C → Y in LCA8. Ref.12 Ref.21
VAR_022954
Natural variant7101E → Q in LCA8. Ref.17
VAR_022955
Natural variant7101E → V in RP12. Ref.33 Ref.35
VAR_067140
Natural variant7401S → F in RP12. Ref.38
VAR_067141
Natural variant7411M → T in LCA8 and early-onset retinal dystrophy. Ref.17 Ref.35 Ref.37 Ref.38
VAR_022956
Natural variant7451T → M in RP12 and LCA8. Ref.1 Ref.17 Ref.18 Ref.24 Ref.26 Ref.33 Ref.35 Ref.39
Corresponds to variant rs28939720 [ dbSNP | Ensembl ].
VAR_011643
Natural variant7491Missing in RP12 and LCA8. Ref.15 Ref.16
VAR_022957
Natural variant7531L → P in LCA8. Ref.20 Ref.21
VAR_067142
Natural variant7641R → C in RP12 and LCA8. Ref.1 Ref.10 Ref.12 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.32 Ref.35
VAR_011644
Natural variant7691R → H. Ref.16 Ref.28 Ref.33
Corresponds to variant rs62636287 [ dbSNP | Ensembl ].
VAR_022958
Natural variant7691R → Q. Ref.12
VAR_022959
Natural variant7891Missing in early-onset retinal dystrophy; probable disease-associated mutation. Ref.38
VAR_067143
Natural variant8211T → M. Ref.10
VAR_067144
Natural variant8361P → T in RP12. Ref.18 Ref.35 Ref.38
Corresponds to variant rs116471343 [ dbSNP | Ensembl ].
VAR_022960
Natural variant8371D → H in RP12; located on the same allele as T-1354. Ref.10
VAR_022961
Natural variant8461G → R in RP12. Ref.14 Ref.35
VAR_022962
Natural variant8501G → S in RP12 and LCA8. Ref.18 Ref.33 Ref.35
VAR_022963
Natural variant8521I → T in LCA8. Ref.17 Ref.26
VAR_022964
Natural variant8911C → G in RP12; without preservation of the paraarteriolar retinal pigment epithelium. Ref.16
VAR_022965
Natural variant8941N → S in RP12. Ref.10
VAR_022966
Natural variant9011V → I Found in a patient with RP12; unknown pathological significance. Ref.33
VAR_067145
Natural variant9051R → Q. Ref.18
Corresponds to variant rs114052315 [ dbSNP | Ensembl ].
VAR_022967
Natural variant9371A → T Found in a patient with Leber congenital amaurosis; unknown pathological significance. Ref.28
VAR_067146
Natural variant9391C → Y in LCA8. Ref.27
VAR_067147
Natural variant9481C → Y in RP12 and LCA8; without preservation of the paraarteriolar retinal pigment epithelium. Ref.1 Ref.10 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.27 Ref.32 Ref.33 Ref.35 Ref.38
VAR_011645
Natural variant9591G → S Found in a patient with RP12; unknown pathological significance. Ref.18
VAR_022968
Natural variant9621Missing in RP12; without preservation of the paraarteriolar retinal pigment epithelium. Ref.16
VAR_022969
Natural variant9861N → I in RP12. Ref.18
VAR_022970
Natural variant9891I → T in LCA8. Ref.14
VAR_022971
Natural variant10031I → T in LCA8. Ref.35
VAR_067148
Natural variant10121L → S in RP12. Ref.35
VAR_067149
Natural variant10251S → I in LCA8. Ref.17
VAR_022972
Natural variant10251S → N in RP12. Ref.35
VAR_067150
Natural variant10411M → T in RP12. Ref.1
VAR_011646
Natural variant10711L → P in RP12. Ref.1 Ref.14
VAR_011647
Natural variant10991T → K in RP12. Ref.34
VAR_067151
Natural variant11001I → R in LCA8. Ref.10
VAR_011648
Natural variant11001I → T in RP12. Ref.16 Ref.18
VAR_022973
Natural variant11031G → R in LCA8 and RP12. Ref.17 Ref.26 Ref.29 Ref.35 Ref.38
VAR_022974
Natural variant11071L → P in LCA8. Ref.17 Ref.35
VAR_022975
Natural variant11071L → R in LCA8. Ref.17
VAR_022976
Natural variant11611Y → C in LCA8. Ref.31
VAR_067152
Natural variant11651C → W in RP12. Ref.30
VAR_064181
Natural variant11741C → G in LCA8 and RP12. Ref.35
VAR_067153
Natural variant11811C → R in RP12. Ref.10
VAR_011649
Natural variant11981Y → C Probable disease-associated mutation found in patients with early-onset retinal dystrophy. Ref.38
VAR_067154
Natural variant12051G → R in LCA8. Ref.12
VAR_022977
Natural variant12181C → F in LCA8. Ref.15
VAR_022978
Natural variant12231C → S Probable disease-associated mutation found in patients with early-onset retinal dystrophy. Ref.38
VAR_067155
Natural variant13051P → L in RP12. Ref.36
VAR_067156
Natural variant13171N → H in LCA8. Ref.12
VAR_022979
Natural variant13211C → S in LCA8; also early onset RP without preservation of the paraarteriolar retinal pigment epithelium. Ref.13 Ref.17
VAR_022980
Natural variant13311R → H. Ref.10 Ref.12 Ref.16
Corresponds to variant rs62636285 [ dbSNP | Ensembl ].
VAR_022981
Natural variant13321C → F in LCA8. Ref.27
VAR_067157
Natural variant13541A → T Found in a patient with RP12; located on the same allele as H-837. Ref.10
VAR_022982
Natural variant13651A → D Probable disease-associated mutation found in patients with early-onset retinal dystrophy. Ref.35
VAR_067158
Natural variant13811P → L in LCA8. Ref.35
VAR_067159
Natural variant13831R → H in RP12. Ref.18 Ref.33
Corresponds to variant rs200573274 [ dbSNP | Ensembl ].
VAR_022983
Isoform 2:
Natural variant13611R → H Found in a patient with Leber congenital amaurosis, unknown pathological significance.

Sequences

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

Last modified July 19, 2005. Version 2.
Checksum: F2D04D20FAA6E37D

FASTA1,406154,183
        10         20         30         40         50         60 
MALKNINYLL IFYLSFSLLI YIKNSFCNKN NTRCLSNSCQ NNSTCKDFSK DNDCSCSDTA 

        70         80         90        100        110        120 
NNLDKDCDNM KDPCFSNPCQ GSATCVNTPG ERSFLCKCPP GYSGTICETT IGSCGKNSCQ 

       130        140        150        160        170        180 
HGGICHQDPI YPVCICPAGY AGRFCEIDHD ECASSPCQNG AVCQDGIDGY SCFCVPGYQG 

       190        200        210        220        230        240 
RHCDLEVDEC ASDPCKNEAT CLNEIGRYTC ICPHNYSGVN CELEIDECWS QPCLNGATCQ 

       250        260        270        280        290        300 
DALGAYFCDC APGFLGDHCE LNTDECASQP CLHGGLCVDG ENRYSCNCTG SGFTGTHCET 

       310        320        330        340        350        360 
LMPLCWSKPC HNNATCEDSV DNYTCHCWPG YTGAQCEIDL NECNSNPCQS NGECVELSSE 

       370        380        390        400        410        420 
KQYGRITGLP SSFSYHEASG YVCICQPGFT GIHCEEDVNE CSSNPCQNGG TCENLPGNYT 

       430        440        450        460        470        480 
CHCPFDNLSR TFYGGRDCSD ILLGCTHQQC LNNGTCIPHF QDGQHGFSCL CPSGYTGSLC 

       490        500        510        520        530        540 
EIATTLSFEG DGFLWVKSGS VTTKGSVCNI ALRFQTVQPM ALLLFRSNRD VFVKLELLSG 

       550        560        570        580        590        600 
YIHLSIQVNN QSKVLLFISH NTSDGEWHFV EVIFAEAVTL TLIDDSCKEK CIAKAPTPLE 

       610        620        630        640        650        660 
SDQSICAFQN SFLGGLPVGM TSNGVALLNF YNMPSTPSFV GCLQDIKIDW NHITLENISS 

       670        680        690        700        710        720 
GSSLNVKAGC VRKDWCESQP CQSRGRCINL WLSYQCDCHR PYEGPNCLRE YVAGRFGQDD 

       730        740        750        760        770        780 
STGYVIFTLD ESYGDTISLS MFVRTLQPSG LLLALENSTY QYIRVWLERG RLAMLTPNSP 

       790        800        810        820        830        840 
KLVVKFVLND GNVHLISLKI KPYKIELYQS SQNLGFISAS TWKIEKGDVI YIGGLPDKQE 

       850        860        870        880        890        900 
TELNGGFFKG CIQDVRLNNQ NLEFFPNPTN NASLNPVLVN VTQGCAGDNS CKSNPCHNGG 

       910        920        930        940        950        960 
VCHSRWDDFS CSCPALTSGK ACEEVQWCGF SPCPHGAQCQ PVLQGFECIA NAVFNGQSGQ 

       970        980        990       1000       1010       1020 
ILFRSNGNIT RELTNITFGF RTRDANVIIL HAEKEPEFLN ISIQDSRLFF QLQSGNSFYM 

      1030       1040       1050       1060       1070       1080 
LSLTSLQSVN DGTWHEVTLS MTDPLSQTSR WQMEVDNETP FVTSTIATGS LNFLKDNTDI 

      1090       1100       1110       1120       1130       1140 
YVGDRAIDNI KGLQGCLSTI EIGGIYLSYF ENVHGFINKP QEEQFLKIST NSVVTGCLQL 

      1150       1160       1170       1180       1190       1200 
NVCNSNPCLH GGNCEDIYSS YHCSCPLGWS GKHCELNIDE CFSNPCIHGN CSDRVAAYHC 

      1210       1220       1230       1240       1250       1260 
TCEPGYTGVN CEVDIDNCQS HQCANGATCI SHTNGYSCLC FGNFTGKFCR QSRLPSTVCG 

      1270       1280       1290       1300       1310       1320 
NEKTNLTCYN GGNCTEFQTE LKCMCRPGFT GEWCEKDIDE CASDPCVNGG LCQDLLNKFQ 

      1330       1340       1350       1360       1370       1380 
CLCDVAFAGE RCEVDLADDL ISDIFTTIGS VTVALLLILL LAIVASVVTS NKRATQGTYS 

      1390       1400 
PSRQEKEGSR VEMWNLMPPP AMERLI 

« Hide

Isoform 2 [UniParc].

Checksum: F380DF2AA046A2FE
Show »

FASTA1,376151,413
Isoform 3 [UniParc].

Checksum: 469C464159974813
Show »

FASTA1,294142,088
Isoform 4 [UniParc].

Checksum: A95CA11C40DAAF47
Show »

FASTA942104,250
Isoform 5 [UniParc].

Checksum: EAC761848F0392AE
Show »

FASTA87095,046

References

« Hide 'large scale' references
[1]"Mutations in a human homologue of Drosophila crumbs cause retinitis pigmentosa (RP12)."
den Hollander A.I., ten Brink J.B., de Kok Y.J.M., van Soest S., van den Born L.I., van Driel M.A., van de Pol D.J.R., Payne A.M., Bhattacharya S.S., Kellner U., Hoyng C.B., Westerveld A., Brunner H.G., Bleeker-Wagemakers E.M., Deutman A.F., Heckenlively J.R., Cremers F.P.M., Bergen A.A.B.
Nat. Genet. 23:217-221(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS RP12 VAL-161; TRP-250; MET-745; CYS-764; TYR-948; THR-1041 AND PRO-1071.
Tissue: Fetal brain and Retina.
[2]"CRB1 has a cytoplasmic domain that is functionally conserved between human and Drosophila."
den Hollander A.I., Johnson K., de Kok Y.J.M., Klebes A., Brunner H.G., Knust E., Cremers F.P.M.
Hum. Mol. Genet. 10:2767-2773(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"MPP5 recruits MPP4 to the CRB1 complex in photoreceptors."
Kantardzhieva A., Gosens I., Alexeeva S., Punte I.M., Versteeg I., Krieger E., Neefjes-Mol C.A., den Hollander A.I., Letteboer S.J.F., Klooster J., Cremers F.P.M., Roepman R., Wijnholds J.
Invest. Ophthalmol. Vis. Sci. 46:2192-2201(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), COMPLEX FORMATION WITH MPP4 AND MPP5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Retina.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Retina.
[5]"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] (ISOFORM 5).
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORM 1).
Tissue: Cerebellum.
[9]"A novel mutation disrupting the cytoplasmic domain of CRB1 in a large consanguineous family of Palestinian origin affected with Leber congenital amaurosis."
Gerber S., Perrault I., Hanein S., Shalev S., Zlotogora J., Barbet F., Ducroq D., Dufier J.-L., Munnich A., Rozet J., Kaplan J.
Ophthalmic Genet. 23:225-235(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LCA8.
[10]"Leber congenital amaurosis and retinitis pigmentosa with Coats-like exudative vasculopathy are associated with mutations in the crumbs homologue 1 (CRB1) gene."
den Hollander A.I., Heckenlively J.R., van den Born L.I., de Kok Y.J.M., van der Velde-Visser S.D., Kellner U., Jurklies B., van Schooneveld M.J., Blankenagel A., Rohrschneider K., Wissinger B., Cruysberg J.R.M., Deutman A.F., Brunner H.G., Apfelstedt-Sylla E., Hoyng C.B., Cremers F.P.M.
Am. J. Hum. Genet. 69:198-203(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 TYR-948 AND ARG-1100, VARIANTS RP12 CYS-433; CYS-764; HIS-837; SER-894; TYR-948 AND ARG-1181, VARIANTS MET-289; MET-821; HIS-1331 AND THR-1354.
[11]Erratum
den Hollander A.I., Heckenlively J.R., van den Born L.I., de Kok Y.J.M., van der Velde-Visser S.D., Kellner U., Jurklies B., van Schooneveld M.J., Blankenagel A., Rohrschneider K., Wissinger B., Cruysberg J.R.M., Deutman A.F., Brunner H.G., Apfelstedt-Sylla E., Hoyng C.B., Cremers F.P.M.
Am. J. Hum. Genet. 69:1160-1160(2001)
[12]"Mutations in the CRB1 gene cause Leber congenital amaurosis."
Lotery A.J., Jacobson S.G., Fishman G.A., Weleber R.G., Fulton A.B., Namperumalsamy P., Heon E., Levin A.V., Grover S., Rosenow J.R., Kopp K.K., Sheffield V.C., Stone E.M.
Arch. Ophthalmol. 119:415-420(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 VAL-144; TYR-383; GLY-480; ARG-480; TYR-681; CYS-764; TYR-948; ARG-1205 AND HIS-1317, VARIANTS MET-289; GLN-769 AND HIS-1331.
[13]"CRB1 mutations may result in retinitis pigmentosa without para-arteriolar RPE preservation."
Lotery A.J., Malik A., Shami S.A., Sindhi M., Chohan B., Maqbool C., Moore P.A., Denton M.J., Stone E.M.
Ophthalmic Genet. 22:163-169(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP12 SER-1321.
[14]"Mutation screening of Pakistani families with congenital eye disorders."
Khaliq S., Abid A., Hameed A., Anwar K., Mohyuddin A., Azmat Z., Shami S.A., Ismail M., Mehdi S.Q.
Exp. Eye Res. 76:343-348(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 ARG-846 AND PRO-1071, VARIANT LCA8 THR-989.
[15]"Crumbs homolog 1 (CRB1) mutations result in a thick human retina with abnormal lamination."
Jacobson S.G., Cideciyan A.V., Aleman T.S., Pianta M.J., Sumaroka A., Schwartz S.B., Smilko E.E., Milam A.H., Sheffield V.C., Stone E.M.
Hum. Mol. Genet. 12:1073-1078(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 SER-749 DEL; CYS-764; TYR-948 AND PHE-1218.
[16]"Study of the involvement of the RGR, CRPB1, and CRB1 genes in the pathogenesis of autosomal recessive retinitis pigmentosa."
Bernal S., Calaf M., Garcia-Hoyos M., Garcia-Sandoval B., Rosell J., Adan A., Ayuso C., Baiget M.
J. Med. Genet. 40:E89-E89(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 SER-749 DEL; GLY-891; TYR-948; LEU-962 DEL AND THR-1100, VARIANTS THR-205; MET-289; GLU-679; HIS-769 AND HIS-1331.
[17]"Leber congenital amaurosis: comprehensive survey of the genetic heterogeneity, refinement of the clinical definition, and genotype-phenotype correlations as a strategy for molecular diagnosis."
Hanein S., Perrault I., Gerber S., Tanguy G., Barbet F., Ducroq D., Calvas P., Dollfus H., Hamel C., Lopponen T., Munier F., Santos L., Shalev S., Zafeiriou D., Dufier J.-L., Munnich A., Rozet J.-M., Kaplan J.
Hum. Mutat. 23:306-317(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 TYR-584; GLN-710; THR-741; MET-745; CYS-764; THR-852; TYR-948; ILE-1025; ARG-1103; ARG-1107; PRO-1107 AND SER-1321.
[18]"CRB1 mutation spectrum in inherited retinal dystrophies."
den Hollander A.I., Davis J., van der Velde-Visser S.D., Zonneveld M.N., Pierrottet C.O., Koenekoop R.K., Kellner U., van den Born L.I., Heckenlively J.R., Hoyng C.B., Handford P.A., Roepman R., Cremers F.P.M.
Hum. Mutat. 24:355-369(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 PHE-195; GLU-578; TYR-587; MET-745; CYS-764; THR-836; SER-850; TYR-948; ILE-986; THR-1100 AND HIS-1383, VARIANTS THR-205; GLN-905 AND SER-959.
[19]"Pigmented paravenous chorioretinal atrophy is associated with a mutation within the crumbs homolog 1 (CRB1) gene."
McKay G.J., Clarke S., Davis J.A., Simpson D.A., Silvestri G.
Invest. Ophthalmol. Vis. Sci. 46:322-328(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PPCRA MET-162.
[20]"Clinical phenotypes in carriers of Leber congenital amaurosis mutations."
Galvin J.A., Fishman G.A., Stone E.M., Koenekoop R.K.
Ophthalmology 112:349-356(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 PRO-753; CYS-764 AND TYR-948.
[21]"Evaluation of genotype-phenotype associations in Leber congenital amaurosis."
Galvin J.A., Fishman G.A., Stone E.M., Koenekoop R.K.
Retina 25:919-929(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 ARG-480; TYR-681; PRO-753; CYS-764 AND TYR-948, VARIANT SER-488.
[22]"Gene symbol: CRB1. Disease: early onset retinitis pigmentosa."
Vallespin E., Riveiro-Alvarez R., Aguirre-Lamban J., Cantalapiedra D., Tapias I., Garcia-Sandoval B., Trujillo-Tiebas M.J., Ayuso C.
Hum. Genet. 119:681-681(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA8 TYR-564.
[23]"CRB1 heterozygotes with regional retinal dysfunction: implications for genetic testing of Leber congenital amaurosis."
Yzer S., Fishman G.A., Racine J., Al-Zuhaibi S., Chakor H., Dorfman A., Szlyk J., Lachapelle P., van den Born L.I., Allikmets R., Lopez I., Cremers F.P., Koenekoop R.K.
Invest. Ophthalmol. Vis. Sci. 47:3736-3744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA8 ARG-454.
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-745.
[25]"Gene symbol: CRB1."
Vallespin E., Millan J.M., Riveiro-Alvarez R., Aguirre-Lamban J., Cantalapiedra D., Gallego J., Trujillo-Tiebas M.J., Ayuso C.
Hum. Genet. 120:914-914(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA8 PRO-535.
[26]"Clinical and molecular genetics of Leber's congenital amaurosis: a multicenter study of Italian patients."
Simonelli F., Ziviello C., Testa F., Rossi S., Fazzi E., Bianchi P.E., Fossarello M., Signorini S., Bertone C., Galantuomo S., Brancati F., Valente E.M., Ciccodicola A., Rinaldi E., Auricchio A., Banfi S.
Invest. Ophthalmol. Vis. Sci. 48:4284-4290(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 TYR-438; MET-745; THR-852 AND ARG-1103, VARIANT MET-289.
[27]"Identification of novel mutations in patients with Leber congenital amaurosis and juvenile RP by genome-wide homozygosity mapping with SNP microarrays."
den Hollander A.I., Lopez I., Yzer S., Zonneveld M.N., Janssen I.M., Strom T.M., Hehir-Kwa J.Y., Veltman J.A., Arends M.L., Meitinger T., Musarella M.A., van den Born L.I., Fishman G.A., Maumenee I.H., Rohrschneider K., Cremers F.P., Koenekoop R.K.
Invest. Ophthalmol. Vis. Sci. 48:5690-5698(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA8 TYR-939; TYR-948 AND PHE-1332.
[28]"Molecular characterization of Leber congenital amaurosis in Koreans."
Seong M.W., Kim S.Y., Yu Y.S., Hwang J.M., Kim J.Y., Park S.S.
Mol. Vis. 14:1429-1436(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA8 ASP-333, VARIANTS HIS-769 AND THR-937.
[29]"Genetic heterogeneity in two consanguineous families segregating early onset retinal degeneration: the pitfalls of homozygosity mapping."
Benayoun L., Spiegel R., Auslender N., Abbasi A.H., Rizel L., Hujeirat Y., Salama I., Garzozi H.J., Allon-Shalev S., Ben-Yosef T.
Am. J. Med. Genet. A 149:650-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP12 ARG-1103.
[30]"Molecular characterization of retinitis pigmentosa in Saudi Arabia."
Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H., Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.
Mol. Vis. 15:2464-2469(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 PHE-27 AND TRP-1165.
[31]"Novel human pathological mutations. Gene symbol: CRB1. Disease: Leber congenital amaurosis."
Vallespin E., Avila-Fernandez A., Velez-Monsalve C., Almoguera B., Martinez-Garcia M., Gomez-Dominguez B., Gonzalez-Roubaud C., Cantalapiedra D., Trujillo-Tiebas M.J., Ayuso C.
Hum. Genet. 127:119-119(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA8 CYS-1161.
[32]"Genetic screening of LCA in Belgium: predominance of CEP290 and identification of potential modifier alleles in AHI1 of CEP290-related phenotypes."
Coppieters F., Casteels I., Meire F., De Jaegere S., Hooghe S., van Regemorter N., Van Esch H., Matuleviciene A., Nunes L., Meersschaut V., Walraedt S., Standaert L., Coucke P., Hoeben H., Kroes H.Y., Vande Walle J., de Ravel T., Leroy B.P., De Baere E.
Hum. Mutat. 31:E1709-E1766(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EARLY-ONSET RETINAL DYSTROPHY TYR-310; CYS-764 AND TYR-948, VARIANT VAL-491.
[33]"Development of a diagnostic genetic test for simplex and autosomal recessive retinitis pigmentosa."
Clark G.R., Crowe P., Muszynska D., O'Prey D., O'Neill J., Alexander S., Willoughby C.E., McKay G.J., Silvestri G., Simpson D.A.
Ophthalmology 117:2169-2177(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 TRP-45; VAL-710; MET-745; SER-850; TYR-948 AND HIS-1383, VARIANTS HIS-769 AND ILE-901.
[34]"Identification of novel mutations in Pakistani families with autosomal recessive retinitis pigmentosa."
Azam M., Collin R.W., Malik A., Khan M.I., Shah S.T., Shah A.A., Hussain A., Sadeque A., Arimadyo K., Ajmal M., Azam A., Qureshi N., Bokhari H., Strom T.M., Cremers F.P., Qamar R., den Hollander A.I.
Arch. Ophthalmol. 129:1377-1378(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP12 LYS-1099.
[35]"Phenotypic variability in patients with retinal dystrophies due to mutations in CRB1."
Henderson R.H., Mackay D.S., Li Z., Moradi P., Sergouniotis P., Russell-Eggitt I., Thompson D.A., Robson A.G., Holder G.E., Webster A.R., Moore A.T.
Br. J. Ophthalmol. 95:811-817(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 SER-157; TRP-250; LYS-312; CYS-675; VAL-710; MET-745; CYS-764; THR-836; ARG-846; TYR-948; SER-1012; ASN-1025 AND GLY-1174, VARIANTS LCA8 SER-850; THR-1003; ARG-1103; PRO-1107; GLY-1174 AND LEU-1381, VARIANTS EARLY-ONSET RETINAL DYSTROPHY THR-741 AND ASP-1365, VARIANT THR-205.
[36]"Molecular genetic analysis of retinitis pigmentosa in Indonesia using genome-wide homozygosity mapping."
Siemiatkowska A.M., Arimadyo K., Moruz L.M., Astuti G.D., de Castro-Miro M., Zonneveld M.N., Strom T.M., de Wijs I.J., Hoefsloot L.H., Faradz S.M., Cremers F.P., den Hollander A.I., Collin R.W.
Mol. Vis. 17:3013-3024(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP12 LEU-1305.
[37]"Detection of variants in 15 genes in 87 unrelated Chinese patients with Leber congenital amaurosis."
Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q., Hejtmancik J.F.
PLoS ONE 6:E19458-E19458(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA8 THR-741, VARIANTS LYS-222; MET-289 AND PRO-635.
[38]"CRB1 mutations in inherited retinal dystrophies."
Bujakowska K., Audo I., Mohand-Said S., Lancelot M.E., Antonio A., Germain A., Leveillard T., Letexier M., Saraiva J.P., Lonjou C., Carpentier W., Sahel J.A., Bhattacharya S.S., Zeitz C.
Hum. Mutat. 33:306-315(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 TYR-584; PHE-740; THR-741; THR-836; TYR-948 AND ARG-1103, VARIANTS EARLY-ONSET RETINAL DYSTROPHY ASN-789 DEL; CYS-1198 AND SER-1223.
[39]"Next-generation genetic testing for retinitis pigmentosa."
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. expand/collapse author list , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.
Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP12 ASN-534 AND MET-745.
+Additional computationally mapped references.

Web resources

Mutations of the CRB1 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF154671 mRNA. Translation: AAF01361.1.
AY043323 mRNA. Translation: AAL10680.1.
AY043324 mRNA. Translation: AAL10681.1.
AY043325 mRNA. Translation: AAL10682.1.
AJ748821 mRNA. Translation: CAG38658.1.
BX640729 mRNA. Translation: CAE45845.1. Sequence problems.
AK299368 mRNA. Translation: BAH13018.1.
AL513325, AL136322, AL139136 Genomic DNA. Translation: CAH72584.1.
AL139136, AL136322 Genomic DNA. Translation: CAI15310.1.
AL139136, AL513325, AL136322 Genomic DNA. Translation: CAI15311.1.
AL136322 Genomic DNA. Translation: CAI16644.1. Sequence problems.
AL136322, AL139136 Genomic DNA. Translation: CAI16645.1.
AL136322, AL513325, AL139136 Genomic DNA. Translation: CAI16646.1.
AL513325, AL136322, AL139136 Genomic DNA. Translation: CAM17208.1.
AL139136, AL136322, AL513325 Genomic DNA. Translation: CAM21656.1.
AL136322, AL139136, AL513325 Genomic DNA. Translation: CAM23328.1.
AL356315 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW91277.1.
BC136271 mRNA. Translation: AAI36272.1.
CCDSCCDS1390.1. [P82279-1]
CCDS53454.1. [P82279-3]
CCDS58052.1. [P82279-5]
RefSeqNP_001180569.1. NM_001193640.1. [P82279-3]
NP_001244894.1. NM_001257965.1.
NP_001244895.1. NM_001257966.1. [P82279-5]
NP_957705.1. NM_201253.2. [P82279-1]
UniGeneHs.126135.

3D structure databases

ProteinModelPortalP82279.
SMRP82279. Positions 24-482, 736-923, 971-1336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116990. 3 interactions.
IntActP82279. 3 interactions.
MINTMINT-1774304.
STRING9606.ENSP00000356370.

PTM databases

PhosphoSiteP82279.

Polymorphism databases

DMDM71153499.

Proteomic databases

PaxDbP82279.
PRIDEP82279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367399; ENSP00000356369; ENSG00000134376. [P82279-3]
ENST00000367400; ENSP00000356370; ENSG00000134376. [P82279-1]
ENST00000448952; ENSP00000395407; ENSG00000134376.
ENST00000484075; ENSP00000433932; ENSG00000134376. [P82279-2]
ENST00000538660; ENSP00000438091; ENSG00000134376. [P82279-5]
GeneID23418.
KEGGhsa:23418.
UCSCuc001gtz.3. human. [P82279-1]
uc001gub.1. human. [P82279-4]
uc009wza.3. human. [P82279-3]
uc010ppb.2. human.

Organism-specific databases

CTD23418.
GeneCardsGC01P197170.
GeneReviewsCRB1.
HGNCHGNC:2343. CRB1.
MIM172870. phenotype.
268000. phenotype.
600105. phenotype.
604210. gene.
613835. phenotype.
neXtProtNX_P82279.
Orphanet65. Leber congenital amaurosis.
251295. Pigmented paravenous retinochoroidal atrophy.
791. Retinitis pigmentosa.
PharmGKBPA26863.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG080001.
InParanoidP82279.
KOK16681.
OMAQSICAFQ.
OrthoDBEOG7KH9HX.
PhylomeDBP82279.
TreeFamTF316224.

Gene expression databases

ArrayExpressP82279.
BgeeP82279.
CleanExHS_CRB1.
GenevestigatorP82279.

Family and domain databases

Gene3D2.60.120.200. 3 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.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamPF00008. EGF. 13 hits.
PF12661. hEGF. 1 hit.
PF02210. Laminin_G_2. 3 hits.
[Graphical view]
SMARTSM00181. EGF. 9 hits.
SM00179. EGF_CA. 8 hits.
SM00282. LamG. 3 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 3 hits.
SSF57184. SSF57184. 2 hits.
PROSITEPS00010. ASX_HYDROXYL. 10 hits.
PS00022. EGF_1. 15 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 19 hits.
PS01187. EGF_CA. 7 hits.
PS50025. LAM_G_DOMAIN. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCRB1.
GenomeRNAi23418.
NextBio45631.
PROP82279.
SOURCESearch...

Entry information

Entry nameCRUM1_HUMAN
AccessionPrimary (citable) accession number: P82279
Secondary accession number(s): A2A308 expand/collapse secondary AC list , B7Z5T2, B9EG71, Q5K3A6, Q5TC28, Q5VUT1, Q6N027, Q8WWY0, Q8WWY1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 147 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM