O75718 (CRTAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cartilage-associated protein

Gene names

Name:	CRTAP
Synonyms:	CASP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. Ref.4
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Found in articular chondrocytes. Expressed in a variety of tissues.
Involvement in disease	Osteogenesis imperfecta 7 (OI7) [MIM:610682]: A connective tissue disorder characterized by short stature, short humeri and femora, coxa vara, white sclera, and the absence of dentinogenesis imperfecta. Multiple fractures are present at birth, and patients manifest moderate-severe bone fragility. Death may occurr in the perinatal period due to secondary respiratory insufficiency. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.6 Ref.7
Sequence similarities	Belongs to the leprecan family.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism Osteogenesis imperfecta
Domain	Signal
PTM	Glycoprotein Hydroxylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	extracellular matrix organization Traceable author statement. Source: Reactome peptidyl-proline hydroxylation to 3-hydroxy-L-proline Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 401	375	Cartilage-associated protein		PRO_0000006319
Amino acid modifications
	Glycosylation	87	1	N-linked (GlcNAc...) Potential
	Glycosylation	363	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	13	1	A → E in OI7; severe form. Ref.7		VAR_063599
	Natural variant	67	1	L → P in OI7. Ref.6		VAR_054442
	Natural variant	137	1	E → D. Ref.3 Corresponds to variant rs17850371 [ dbSNP | Ensembl ].		VAR_032846
	Natural variant	157	1	K → E in OI7; severe form. Ref.7		VAR_063600
	Natural variant	261	1	L → V. Corresponds to variant rs1135127 [ dbSNP | Ensembl ].		VAR_053050

Sequences

	Sequence		Length	Mass (Da)
	O75718 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 4BEED4089195456F	FASTA	401	46,562
	10 20 30 40 50 60 MEPGRRGAAA LLALLCVACA LRAGRAQYER YSFRSFPRDE LMPLESAYRH ALDKYSGEHW 70 80 90 100 110 120 AESVGYLEIS LRLHRLLRDS EAFCHRNCSA APQPEPAAGL ASYPELRLFG GLLRRAHCLK 130 140 150 160 170 180 RCKQGLPAFR QSQPSREVLA DFQRREPYKF LQFAYFKANN LPKAIAAAHT FLLKHPDDEM 190 200 210 220 230 240 MKRNMAYYKS LPGAEDYIKD LETKSYESLF IRAVRAYNGE NWRTSITDME LALPDFFKAF 250 260 270 280 290 300 YECLAACEGS REIKDFKDFY LSIADHYVEV LECKIQCEEN LTPVIGGYPV EKFVATMYHY 310 320 330 340 350 360 LQFAYYKLND LKNAAPCAVS YLLFDQNDKV MQQNLVYYQY HRDTWGLSDE HFQPRPEAVQ 370 380 390 400 FFNVTTLQKE LYDFAKENIM DDDEGEVVEY VDDLLELEET S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, characterization and chromosome mapping of the gene encoding human cartilage associated protein (CRTAP)." Tonachini L., Morello R., Monticone M., Skaug J., Scherer S.W., Cancedda R., Castagnola P. Cytogenet. Cell Genet. 87:191-194(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[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]. Tissue: Placenta.
[3]	"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], VARIANT ASP-137. Tissue: Kidney.
[4]	"CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta." Morello R., Bertin T.K., Chen Y., Hicks J., Tonachini L., Monticone M., Castagnola P., Rauch F., Glorieux F.H., Vranka J., Baechinger H.P., Pace J.M., Schwarze U., Byers P.H., Weis M., Fernandes R.J., Eyre D.R., Yao Z., Boyce B.F., Lee B. Cell 127:291-304(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INVOLVEMENT IN OI7.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta." Baldridge D., Schwarze U., Morello R., Lennington J., Bertin T.K., Pace J.M., Pepin M.G., Weis M., Eyre D.R., Walsh J., Lambert D., Green A., Robinson H., Michelson M., Houge G., Lindman C., Martin J., Ward J. , Lemyre E., Mitchell J.J., Krakow D., Rimoin D.L., Cohn D.H., Byers P.H., Lee B. Hum. Mutat. 29:1435-1442(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI7 PRO-67.
[7]	"CRTAP mutations in lethal and severe osteogenesis imperfecta: the importance of combining biochemical and molecular genetic analysis." Van Dijk F.S., Nesbitt I.M., Nikkels P.G.J., Dalton A., Bongers E.M.H.F., van de Kamp J.M., Hilhorst-Hofstee Y., Den Hollander N.S., Lachmeijer A.M.A., Marcelis C.L., Tan-Sindhunata G.M.B., van Rijn R.R., Meijers-Heijboer H., Cobben J.M., Pals G. Eur. J. Hum. Genet. 17:1560-1569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OI7 GLU-13 AND GLU-157.
+	Additional computationally mapped references.

Web resources

GeneReviews

Osteogenesis imperfecta variant database

Cartilage-associated protein (CRTAP)

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ006470 mRNA. Translation: CAA07054.1. AK314719 mRNA. Translation: BAG37263.1. BC008745 mRNA. Translation: AAH08745.1.
IPI	IPI00748502.
RefSeq	NP_006362.1. NM_006371.4.
UniGene	Hs.517888.
3D structure databases
ProteinModelPortal	O75718.
SMR	O75718. Positions 43-74.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75718. 3 interactions.
STRING	9606.ENSP00000323696.
PTM databases
PhosphoSite	O75718.
Proteomic databases
PaxDb	O75718.
PRIDE	O75718.
Protocols and materials databases
DNASU	10491.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000320954; ENSP00000323696; ENSG00000170275.
GeneID	10491.
KEGG	hsa:10491.
UCSC	uc003cfl.4. human.
Organism-specific databases
CTD	10491.
GeneCards	GC03P033155.
HGNC	HGNC:2379. CRTAP.
HPA	HPA043598. HPA044150.
MIM	605497. gene. 610682. phenotype.
neXtProt	NX_O75718.
Orphanet	216804. Osteogenesis imperfecta type 2. 216812. Osteogenesis imperfecta type 3. 216820. Osteogenesis imperfecta type 4.
PharmGKB	PA26900.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG306541.
HOGENOM	HOG000247068.
HOVERGEN	HBG005540.
InParanoid	O75718.
OMA	KRAQCLK.
OrthoDB	EOG4PZJ6V.
PhylomeDB	O75718.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	O75718.
Bgee	O75718.
CleanEx	HS_CRTAP.
Genevestigator	O75718.
GermOnline	ENSG00000170275. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
ChiTaRS	CRTAP. human.
GenomeRNAi	10491.
NextBio	39808.
SOURCE	Search...

Entry information

Entry name

CRTAP_HUMAN

Accession

Primary (citable) accession number: O75718
Secondary accession number(s): B2RBL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.