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Q9BU40

- CRDL1_HUMAN

UniProt

Q9BU40 - CRDL1_HUMAN

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Protein
Chordin-like protein 1
Gene
CHRDL1, NRLN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Antagonizes the function of BMP4 by binding to it and preventing its interaction with receptors. Alters the fate commitment of neural stem cells from gliogenesis to neurogenesis. Contributes to neuronal differentiation of neural stem cells in the brain by preventing the adoption of a glial fate. May play a crucial role in dorsoventral axis formation. May play a role in embryonic bone formation By similarity. May also play an important role in regulating retinal angiogenesis through modulation of BMP4 actions in endothelial cells. Plays a role during anterior segment eye development.2 Publications

GO - Biological processi

  1. BMP signaling pathway Source: Reactome
  2. cell differentiation Source: UniProtKB-KW
  3. compound eye development Source: UniProtKB
  4. eye development Source: UniProtKB
  5. nervous system development Source: UniProtKB-KW
  6. ossification Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis, Osteogenesis

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.

Names & Taxonomyi

Protein namesi
Recommended name:
Chordin-like protein 1
Alternative name(s):
Neuralin-1
Neurogenesin-1
Ventroptin
Gene namesi
Name:CHRDL1
Synonyms:NRLN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:29861. CHRDL1.

Subcellular locationi

Secreted Reviewed prediction

GO - Cellular componenti

  1. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Megalocornea 1, X-linked (MGC1) [MIM:309300]: An eye disorder in which the corneal diameter is bilaterally enlarged (greater than 13 mm) without an increase in intraocular pressure. It may also be referred to as anterior megalophthalmos, since the entire anterior segment is larger than normal. Features of megalocornea in addition to a deep anterior chamber include astigmatic refractive errors, atrophy of the iris stroma, miosis secondary to decreased function of the dilator muscle, iridodonesis, and tremulousness, subluxation, or dislocation of the lens. Whereas most affected individuals exhibit normal ocular function, complications include cataract development and glaucoma following lenticular dislocation or subluxation.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti254 – 2541C → F in MGC1. 1 Publication
VAR_068175

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi309300. phenotype.
Orphaneti91489. Isolated congenital megalocornea.
PharmGKBiPA134933380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 450429Chordin-like protein 1
PRO_0000005368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi285 – 2851N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9BU40.
PRIDEiQ9BU40.

PTM databases

PhosphoSiteiQ9BU40.

Expressioni

Tissue specificityi

Expressed in the developing cornea and in the eye anterior segment in addition to the retina. Differentially expressed in the fetal brain. There is high expression in cerebellum and neocortex. Expressed in retinal pericytes.2 Publications

Inductioni

By hypoxia in retinal pericytes.1 Publication

Gene expression databases

ArrayExpressiQ9BU40.
BgeeiQ9BU40.
CleanExiHS_CHRDL1.
GenevestigatoriQ9BU40.

Organism-specific databases

HPAiHPA000226.
HPA000250.

Interactioni

Protein-protein interaction databases

IntActiQ9BU40. 2 interactions.
MINTiMINT-8201750.
STRINGi9606.ENSP00000413419.

Structurei

3D structure databases

ProteinModelPortaliQ9BU40.
SMRiQ9BU40. Positions 28-98, 103-174, 250-323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 9466VWFC 1
Add
BLAST
Domaini107 – 17367VWFC 2
Add
BLAST
Domaini252 – 31766VWFC 3
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi173 – 1753Cell attachment site Reviewed prediction

Sequence similaritiesi

Contains 3 VWFC domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG147797.
HOGENOMiHOG000049211.
HOVERGENiHBG051113.
InParanoidiQ9BU40.
OMAiCPRCPED.
OrthoDBiEOG7XH6S0.
PhylomeDBiQ9BU40.
TreeFamiTF106451.

Family and domain databases

InterProiIPR001007. VWF_C.
[Graphical view]
PfamiPF00093. VWC. 3 hits.
[Graphical view]
SMARTiSM00214. VWC. 3 hits.
[Graphical view]
PROSITEiPS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 3 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BU40-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGGMKYIFSL LFFLLLEGGK TEQVKHSETY CMFQDKKYRV GERWHPYLEP    50
YGLVYCVNCI CSENGNVLCS RVRCPNVHCL SPVHIPHLCC PRCPDSLPPV 100
NNKVTSKSCE YNGTTYQHGE LFVAEGLFQN RQPNQCTQCS CSEGNVYCGL 150
KTCPKLTCAF PVSVPDSCCR VCRGDGELSW EHSDGDIFRQ PANREARHSY 200
HRSHYDPPPS RQAGGLSRFP GARSHRGALM DSQQASGTIV QIVINNKHKH 250
GQVCVSNGKT YSHGESWHPN LRAFGIVECV LCTCNVTKQE CKKIHCPNRY 300
PCKYPQKIDG KCCKVCPGKK AKELPGQSFD NKGYFCGEET MPVYESVFME 350
DGETTRKIAL ETERPPQVEV HVWTIRKGIL QHFHIEKISK RMFEELPHFK 400
LVTRTTLSQW KIFTEGEAQI SQMCSSRVCR TELEDLVKVL YLERSEKGHC 450
Length:450
Mass (Da):51,168
Last modified:June 1, 2001 - v1
Checksum:iD5F39AB9E2EE3E71
GO
Isoform 2 (identifier: Q9BU40-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-95: D → ED
     323-323: E → EE

Show »
Length:452
Mass (Da):51,426
Checksum:iE214F9A68D8EE072
GO
Isoform 3 (identifier: Q9BU40-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM
     95-173: Missing.
     323-323: E → EE

Note: No experimental confirmation available.

Show »
Length:378
Mass (Da):43,516
Checksum:iEA581757BD2A66F2
GO
Isoform 4 (identifier: Q9BU40-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM
     95-95: D → ED
     323-323: E → EE

Show »
Length:458
Mass (Da):52,284
Checksum:i2E6FD80F2B44960F
GO
Isoform 5 (identifier: Q9BU40-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM
     323-323: E → EE

Note: No experimental confirmation available.

Show »
Length:457
Mass (Da):52,155
Checksum:iE306E04B501FE8D1
GO
Isoform 6 (identifier: Q9BU40-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM

Show »
Length:456
Mass (Da):52,026
Checksum:i345A3C739493A545
GO

Sequence cautioni

The sequence AAH02909.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAU25841.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAF85795.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti254 – 2541C → F in MGC1. 1 Publication
VAR_068175

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRKKWKM in isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_043260
Alternative sequencei95 – 17379Missing in isoform 3.
VSP_043261Add
BLAST
Alternative sequencei95 – 951D → ED in isoform 2 and isoform 4.
VSP_036469
Alternative sequencei323 – 3231E → EE in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_036470

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY608914 mRNA. Translation: AAU25841.1. Different initiation.
AK293106 mRNA. Translation: BAF85795.1. Different initiation.
AK297563 mRNA. Translation: BAG59955.1.
AK312270 mRNA. No translation available.
AL049176, AL591489 Genomic DNA. Translation: CAI42037.1.
AL591489, AL049176 Genomic DNA. Translation: CAI41336.1.
AL591489, AL049176 Genomic DNA. Translation: CAI41337.1.
AL049176, AL591489 Genomic DNA. Translation: CAI42038.1.
CH471120 Genomic DNA. Translation: EAX02656.1.
CH471120 Genomic DNA. Translation: EAX02657.1.
BC002909 mRNA. Translation: AAH02909.2. Different initiation.
CCDSiCCDS14553.1. [Q9BU40-6]
CCDS48148.2. [Q9BU40-3]
CCDS48149.1. [Q9BU40-4]
CCDS48150.1. [Q9BU40-5]
RefSeqiNP_001137453.1. NM_001143981.1. [Q9BU40-4]
NP_001137454.1. NM_001143982.1. [Q9BU40-5]
NP_001137455.2. NM_001143983.2. [Q9BU40-3]
NP_660277.2. NM_145234.3. [Q9BU40-6]
XP_005262278.1. XM_005262221.1. [Q9BU40-4]
XP_005262279.1. XM_005262222.2. [Q9BU40-5]
UniGeneiHs.496587.

Genome annotation databases

EnsembliENST00000218054; ENSP00000218054; ENSG00000101938. [Q9BU40-6]
ENST00000372042; ENSP00000361112; ENSG00000101938. [Q9BU40-4]
ENST00000372045; ENSP00000361115; ENSG00000101938. [Q9BU40-1]
ENST00000394797; ENSP00000378276; ENSG00000101938. [Q9BU40-6]
ENST00000444321; ENSP00000399739; ENSG00000101938. [Q9BU40-5]
ENST00000482160; ENSP00000418443; ENSG00000101938. [Q9BU40-3]
GeneIDi91851.
KEGGihsa:91851.
UCSCiuc004eou.4. human.
uc004eov.3. human. [Q9BU40-2]
uc004eow.3. human. [Q9BU40-1]
uc011mss.2. human. [Q9BU40-3]

Polymorphism databases

DMDMi27805644.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY608914 mRNA. Translation: AAU25841.1 . Different initiation.
AK293106 mRNA. Translation: BAF85795.1 . Different initiation.
AK297563 mRNA. Translation: BAG59955.1 .
AK312270 mRNA. No translation available.
AL049176 , AL591489 Genomic DNA. Translation: CAI42037.1 .
AL591489 , AL049176 Genomic DNA. Translation: CAI41336.1 .
AL591489 , AL049176 Genomic DNA. Translation: CAI41337.1 .
AL049176 , AL591489 Genomic DNA. Translation: CAI42038.1 .
CH471120 Genomic DNA. Translation: EAX02656.1 .
CH471120 Genomic DNA. Translation: EAX02657.1 .
BC002909 mRNA. Translation: AAH02909.2 . Different initiation.
CCDSi CCDS14553.1. [Q9BU40-6 ]
CCDS48148.2. [Q9BU40-3 ]
CCDS48149.1. [Q9BU40-4 ]
CCDS48150.1. [Q9BU40-5 ]
RefSeqi NP_001137453.1. NM_001143981.1. [Q9BU40-4 ]
NP_001137454.1. NM_001143982.1. [Q9BU40-5 ]
NP_001137455.2. NM_001143983.2. [Q9BU40-3 ]
NP_660277.2. NM_145234.3. [Q9BU40-6 ]
XP_005262278.1. XM_005262221.1. [Q9BU40-4 ]
XP_005262279.1. XM_005262222.2. [Q9BU40-5 ]
UniGenei Hs.496587.

3D structure databases

ProteinModelPortali Q9BU40.
SMRi Q9BU40. Positions 28-98, 103-174, 250-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9BU40. 2 interactions.
MINTi MINT-8201750.
STRINGi 9606.ENSP00000413419.

PTM databases

PhosphoSitei Q9BU40.

Polymorphism databases

DMDMi 27805644.

Proteomic databases

PaxDbi Q9BU40.
PRIDEi Q9BU40.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000218054 ; ENSP00000218054 ; ENSG00000101938 . [Q9BU40-6 ]
ENST00000372042 ; ENSP00000361112 ; ENSG00000101938 . [Q9BU40-4 ]
ENST00000372045 ; ENSP00000361115 ; ENSG00000101938 . [Q9BU40-1 ]
ENST00000394797 ; ENSP00000378276 ; ENSG00000101938 . [Q9BU40-6 ]
ENST00000444321 ; ENSP00000399739 ; ENSG00000101938 . [Q9BU40-5 ]
ENST00000482160 ; ENSP00000418443 ; ENSG00000101938 . [Q9BU40-3 ]
GeneIDi 91851.
KEGGi hsa:91851.
UCSCi uc004eou.4. human.
uc004eov.3. human. [Q9BU40-2 ]
uc004eow.3. human. [Q9BU40-1 ]
uc011mss.2. human. [Q9BU40-3 ]

Organism-specific databases

CTDi 91851.
GeneCardsi GC0XM109917.
HGNCi HGNC:29861. CHRDL1.
HPAi HPA000226.
HPA000250.
MIMi 300350. gene.
309300. phenotype.
neXtProti NX_Q9BU40.
Orphaneti 91489. Isolated congenital megalocornea.
PharmGKBi PA134933380.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG147797.
HOGENOMi HOG000049211.
HOVERGENi HBG051113.
InParanoidi Q9BU40.
OMAi CPRCPED.
OrthoDBi EOG7XH6S0.
PhylomeDBi Q9BU40.
TreeFami TF106451.

Enzyme and pathway databases

Reactomei REACT_12034. Signaling by BMP.

Miscellaneous databases

ChiTaRSi CHRDL1. human.
GenomeRNAii 91851.
NextBioi 77488.
PROi Q9BU40.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BU40.
Bgeei Q9BU40.
CleanExi HS_CHRDL1.
Genevestigatori Q9BU40.

Family and domain databases

InterProi IPR001007. VWF_C.
[Graphical view ]
Pfami PF00093. VWC. 3 hits.
[Graphical view ]
SMARTi SM00214. VWC. 3 hits.
[Graphical view ]
PROSITEi PS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Chordin-like 1, a bone morphogenetic protein-4 antagonist, is upregulated by hypoxia in human retinal pericytes and plays a role in regulating angiogenesis."
    Kane R., Godson C., O'Brien C.
    Mol. Vis. 14:1138-1148(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  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.
    , 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; 3 AND 5).
    Tissue: Astrocyte, Brain and Uterus.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Lung.
  6. Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANT MGC1 PHE-254.

Entry informationi

Entry nameiCRDL1_HUMAN
AccessioniPrimary (citable) accession number: Q9BU40
Secondary accession number(s): B1AKD0
, B4DMP3, D3DUY6, E9PGS5, Q539E4, Q9Y3H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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