ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8IVL5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name P3H2_HUMAN
Primary accession number Q8IVL5
Secondary accession number Q9NVI2
Integrated into Swiss-Prot on June 27, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 44)
Name and origin of the protein
Protein name Prolyl 3-hydroxylase 2 [Precursor]
Synonyms EC 1.14.11.7
Leprecan-like protein 1
Myxoid liposarcoma-associated protein 4
Gene name
Name: LEPREL1
Synonyms: MLAT4, P3H2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liposarcoma;
DOI=10.1002/(SICI)1097-0215(19990924)83:1<30::AID-IJC6>3.0.CO;2-4; PubMed=10449603 [NCBI, ExPASy, EBI, Israel, Japan]
Thelin-Jaernum S., Lassen C., Panagopoulos I., Mandahl N., Aaman P.;
"Identification of genes differentially expressed in TLS-CHOP carrying myxoid liposarcomas.";
Int. J. Cancer 83:30-33(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
TISSUE=Liposarcoma;
DOI=10.1016/j.bbrc.2004.03.060; PubMed=15063763 [NCBI, ExPASy, EBI, Israel, Japan]
Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K., Aaman P.;
"LEPREL1, a novel ER and Golgi resident member of the Leprecan family.";
Biochem. Biophys. Res. Commun. 317:342-351(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-708.
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
VARIANT [LARGE SCALE ANALYSIS] ASN-613.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ430351; CAD23039.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001580; BAA91769.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK056447; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC005029; AAH05029.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001127890.1; -.
NP_060662.2; -.
UniGene Hs.374191
3D structure databases
ModBase Q8IVL5.
PTM databases
PhosphoSite Q8IVL5; -.
Organism-specific databases
GeneCards GC03M191157; -.
HGNC HGNC:19317; LEPREL1.
GenAtlas LEPREL1.
HPA HPA007890; -.
HPA013355; -.
MIM 610341; gene. [NCBI / EBI]
PharmGKB PA134922807; -.
GeneCards Q8IVL5.
Gene expression databases
ArrayExpress Q8IVL5; -.
CleanEx HS_LEPREL1; -.
GermOnline ENSG00000090530; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from electronic annotation from InterPro).
GO:0005794; Cellular component: Golgi apparatus (inferred from electronic annotation from UniProtKB-KW).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0031418; Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0019797; Molecular function: procollagen-proline 3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019538; Biological process: protein metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR005123; 2OG-FeII_Oase.
IPR000886; ER_targeting_sequence.
IPR006620; Pro_4_hyd_alph.
IPR013105; TPR_2.
IPR013026; TPR_region.
Graphical view of domain structure.
Pfam PF03171; 2OG-FeII_Oxy; 1.
PF07719; TPR_2; 1.
Pfam graphical view of domain structure.
SMART SM00702; P4Hc; 1.
SMART graphical view of domain structure.
PROSITE PS00014; ER_TARGET; 1.
PS50005; TPR; FALSE_NEG.
PS50293; TPR_REGION; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q8IVL5; -.
Genome annotation databases
Ensembl ENSG00000090530; Homo sapiens. [Contig view]
GeneID 55214; -.
KEGG hsa:55214; -.
Phylogenomic databases
HOGENOM Q8IVL5; -.
HOVERGEN Q8IVL5; -.
Other
DrugBank DB00172; L-Proline.
DB00139; Succinic acid.
DB00126; Vitamin C.
NextBio 59168; -.
SOURCE LEPREL1; Homo sapiens.
ProtoNet Q8IVL5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Dioxygenase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Iron; Metal-binding; Oxidoreductase; Polymorphism; Repeat; Signal; TPR repeat; Vitamin C.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     Potential. 
CHAIN   25   708  684     Prolyl 3-hydroxylase 2. PRO_0000240356
REPEAT   44    77  34     TPR 1. 
REPEAT   148   181  34     TPR 2. 
REPEAT   210   243  34     TPR 3. 
REPEAT   306   339  34     TPR 4. 
DOMAIN   462   670  209     PKHD. 
MOTIF   705   708  4     Prevents secretion from ER (Potential). 
COMPBIAS   93    99  7     Poly-Pro. 
ACT_SITE   662   662        By similarity. 
METAL   580   580        Iron. 
METAL   582   582        Iron. 
METAL   652   652        Iron. 
CARBOHYD   449   449        N-linked (GlcNAc...) (Potential). 
CARBOHYD   549   549        N-linked (GlcNAc...) (Potential). 
VARIANT   613   613  1     D -> N (in a breast cancer sample; somatic mutation). VAR_036123 
CONFLICT   477   477        R -> Q (in Ref. 2). 
Sequence information
Length: 708 AA [This is the length of the unprocessed precursor] Molecular weight: 80984 Da [This is the MW of the unprocessed precursor] CRC64: B9E680C90D607291 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRERIWAPPL LLLLPLLLPP PLWGGPPDSP RRELELEPGP LQPFDLLYAS GAAAYYSGDY 

        70         80         90        100        110        120 
ERAVRDLEAA LRSHRRLREI RTRCARHCAA RHPLPPPPPG EGPGAELPLF RSLLGRARCY 

       130        140        150        160        170        180 
RSCETQRLGG PASRHRVSED VRSDFQRRVP YNYLQRAYIK LNQLEKAVEA AHTFFVANPE 

       190        200        210        220        230        240 
HMEMQQNIEN YRATAGVEAL QLVDREAKPH MESYNAGVKH YEADDFEMAI RHFEQALREY 

       250        260        270        280        290        300 
FVEDTECRTL CEGPQRFEEY EYLGYKAGLY EAIADHYMQV LVCQHECVRE LATRPGRLSP 

       310        320        330        340        350        360 
IENFLPLHYD YLQFAYYRVG EYVKALECAK AYLLCHPDDE DVLDNVDYYE SLLDDSIDPA 

       370        380        390        400        410        420 
SIEAREDLTM FVKRHKLESE LIKSAAEGLG FSYTEPNYWI RYGGRQDENR VPSGVNVEGA 

       430        440        450        460        470        480 
EVHGFSMGKK LSPKIDRDLR EGGPLLYENI TFVYNSEQLN GTQRVLLDNV LSEEQCRELH 

       490        500        510        520        530        540 
SVASGIMLVG DGYRGKTSPH TPNEKFEGAT VLKALKSGYE GRVPLKSARL FYDISEKARR 

       550        560        570        580        590        600 
IVESYFMLNS TLYFSYTHMV CRTALSGQQD RRNDLSHPIH ADNCLLDPEA NECWKEPPAY 

       610        620        630        640        650        660 
TFRDYSALLY MNDDFEGGEF IFTEMDAKTV TASIKPKCGR MISFSSGGEN PHGVKAVTKG 

       670        680        690        700 
KRCAVALWFT LDPLYRELER IQADEVIAIL DQEQQGKHEL NINPKDEL 

Q8IVL5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!