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Q9Y4L1

- HYOU1_HUMAN

UniProt

Q9Y4L1 - HYOU1_HUMAN

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Protein

Hypoxia up-regulated protein 1

Gene

HYOU1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum unfolded protein response Source: Reactome
  4. response to ischemia Source: Ensembl
  5. response to stress Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_163813. Scavenging by Class F Receptors.
REACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia up-regulated protein 1
Alternative name(s):
150 kDa oxygen-regulated protein
Short name:
ORP-150
170 kDa glucose-regulated protein
Short name:
GRP-170
Gene namesi
Name:HYOU1
Synonyms:GRP170, ORP150
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16931. HYOU1.

Subcellular locationi

GO - Cellular componenti

  1. endocytic vesicle lumen Source: Reactome
  2. endoplasmic reticulum Source: ProtInc
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. focal adhesion Source: UniProtKB
  7. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232By similarityAdd
BLAST
Chaini33 – 999967Hypoxia up-regulated protein 1PRO_0000013538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)1 Publication
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)5 Publications
Glycosylationi596 – 5961N-linked (GlcNAc...)2 Publications
Glycosylationi830 – 8301N-linked (GlcNAc...)3 Publications
Glycosylationi862 – 8621N-linked (GlcNAc...)2 Publications
Glycosylationi869 – 8691N-linked (GlcNAc...)1 Publication
Modified residuei883 – 8831N6-acetyllysineBy similarity
Glycosylationi922 – 9221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi931 – 9311N-linked (GlcNAc...)3 Publications

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ9Y4L1.
PaxDbiQ9Y4L1.
PeptideAtlasiQ9Y4L1.
PRIDEiQ9Y4L1.

2D gel databases

REPRODUCTION-2DPAGEIPI00000877.

PTM databases

PhosphoSiteiQ9Y4L1.

Miscellaneous databases

PMAP-CutDBQ9Y4L1.

Expressioni

Tissue specificityi

Highly expressed in tissues that contain well-developed endoplasmic reticulum and synthesize large amounts of secretory proteins. Highly expressed in liver and pancreas and lower expression in brain and kidney. Also expressed in macrophages within aortic atherosclerotic plaques, and in breast cancers.

Inductioni

By hypoxia and also by 2-deoxyglucose or tunicamycin.

Gene expression databases

BgeeiQ9Y4L1.
CleanExiHS_HYOU1.
ExpressionAtlasiQ9Y4L1. baseline and differential.
GenevestigatoriQ9Y4L1.

Organism-specific databases

HPAiHPA049296.

Interactioni

Subunit structurei

Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

Protein-protein interaction databases

BioGridi115780. 30 interactions.
IntActiQ9Y4L1. 9 interactions.
MINTiMINT-4105974.
STRINGi9606.ENSP00000278752.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4L1.
SMRiQ9Y4L1. Positions 35-613, 711-817.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9994Prevents secretion from ERSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi603 – 6064Poly-Glu
Compositional biasi636 – 6416Poly-Pro

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000007865.
HOVERGENiHBG106402.
InParanoidiQ9Y4L1.
KOiK09486.
OMAiDTKENGT.
PhylomeDBiQ9Y4L1.
TreeFamiTF105048.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4L1-1) [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

        10         20         30         40         50
MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV
60 70 80 90 100
KPGVPMEIVL NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF
110 120 130 140 150
QHLLGKQADN PHVALYQARF PEHELTFDPQ RQTVHFQISS QLQFSPEEVL
160 170 180 190 200
GMVLNYSRSL AEDFAEQPIK DAVITVPVFF NQAERRAVLQ AARMAGLKVL
210 220 230 240 250
QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC TIVTYQMVKT
260 270 280 290 300
KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR
310 320 330 340 350
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE
360 370 380 390 400
LCADLFERVP GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV
410 420 430 440 450
GKEELGKNIN ADEAAAMGAV YQAAALSKAF KVKPFVVRDA VVYPILVEFT
460 470 480 490 500
REVEEEPGIH SLKHNKRVLF SRMGPYPQRK VITFNRYSHD FNFHINYGDL
510 520 530 540 550
GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK AHFNLDESGV
560 570 580 590 600
LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT
610 620 630 640 650
VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE
660 670 680 690 700
KATEKENGDK SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG
710 720 730 740 750
VELVVLDLPD LPEDKLAQSV QKLQDLTLRD LEKQEREKAA NSLEAFIFET
760 770 780 790 800
QDKLYQPEYQ EVSTEEQREE ISGKLSAAST WLEDEGVGAT TVMLKEKLAE
810 820 830 840 850
LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR LIPEMDQIFT
860 870 880 890 900
EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
910 920 930 940 950
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED
960 970 980 990
AEPISEPEKV ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL
Length:999
Mass (Da):111,335
Last modified:November 1, 1999 - v1
Checksum:iFCE0F292466AFAB9
GO
Isoform 2 (identifier: Q9Y4L1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     603-646: EEEESPAEGS...PPPEPKGDAT → MLFLCPARLP...RARPAWRLCS
     647-999: Missing.

Note: No experimental confirmation available.

Show »
Length:559
Mass (Da):62,757
Checksum:i007EDC619EE8FBD0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751K → E in BAD96476. 1 PublicationCurated
Sequence conflicti92 – 921N → D in BAD96476. 1 PublicationCurated
Sequence conflicti255 – 2551M → T in BAD96476. 1 PublicationCurated
Sequence conflicti442 – 4421V → A in BAD96476. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787Missing in isoform 2. 1 PublicationVSP_056364Add
BLAST
Alternative sequencei603 – 64644EEEES…KGDAT → MLFLCPARLPQSKQAIDRFH TAVTCMEPPWGRRCRARPAW RLCS in isoform 2. 1 PublicationVSP_056365Add
BLAST
Alternative sequencei647 – 999353Missing in isoform 2. 1 PublicationVSP_056366Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U65785 mRNA. Translation: AAC50947.1.
AB009979 Genomic DNA. Translation: BAF80348.1.
DQ350134 mRNA. Translation: ABC75106.1.
DQ372932 mRNA. Translation: ABD14370.1.
AK304264 mRNA. Translation: BAH14145.1.
AK314178 mRNA. Translation: BAG36860.1.
AK222756 mRNA. Translation: BAD96476.1.
EF444986 Genomic DNA. Translation: ACA06002.1.
AP003392 Genomic DNA. No translation available.
CCDSiCCDS8408.1. [Q9Y4L1-1]
PIRiJC5278.
RefSeqiNP_001124463.1. NM_001130991.2.
NP_006380.1. NM_006389.4.
UniGeneiHs.277704.

Genome annotation databases

EnsembliENST00000617285; ENSP00000480150; ENSG00000149428. [Q9Y4L1-1]
GeneIDi10525.
KEGGihsa:10525.
UCSCiuc001put.2. human. [Q9Y4L1-1]

Polymorphism databases

DMDMi10720185.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U65785 mRNA. Translation: AAC50947.1 .
AB009979 Genomic DNA. Translation: BAF80348.1 .
DQ350134 mRNA. Translation: ABC75106.1 .
DQ372932 mRNA. Translation: ABD14370.1 .
AK304264 mRNA. Translation: BAH14145.1 .
AK314178 mRNA. Translation: BAG36860.1 .
AK222756 mRNA. Translation: BAD96476.1 .
EF444986 Genomic DNA. Translation: ACA06002.1 .
AP003392 Genomic DNA. No translation available.
CCDSi CCDS8408.1. [Q9Y4L1-1 ]
PIRi JC5278.
RefSeqi NP_001124463.1. NM_001130991.2.
NP_006380.1. NM_006389.4.
UniGenei Hs.277704.

3D structure databases

ProteinModelPortali Q9Y4L1.
SMRi Q9Y4L1. Positions 35-613, 711-817.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115780. 30 interactions.
IntActi Q9Y4L1. 9 interactions.
MINTi MINT-4105974.
STRINGi 9606.ENSP00000278752.

Chemistry

ChEMBLi CHEMBL2216741.

PTM databases

PhosphoSitei Q9Y4L1.

Polymorphism databases

DMDMi 10720185.

2D gel databases

REPRODUCTION-2DPAGE IPI00000877.

Proteomic databases

MaxQBi Q9Y4L1.
PaxDbi Q9Y4L1.
PeptideAtlasi Q9Y4L1.
PRIDEi Q9Y4L1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000617285 ; ENSP00000480150 ; ENSG00000149428 . [Q9Y4L1-1 ]
GeneIDi 10525.
KEGGi hsa:10525.
UCSCi uc001put.2. human. [Q9Y4L1-1 ]

Organism-specific databases

CTDi 10525.
GeneCardsi GC11M118914.
HGNCi HGNC:16931. HYOU1.
HPAi HPA049296.
MIMi 601746. gene.
neXtProti NX_Q9Y4L1.
PharmGKBi PA38427.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00390000016919.
HOGENOMi HOG000007865.
HOVERGENi HBG106402.
InParanoidi Q9Y4L1.
KOi K09486.
OMAi DTKENGT.
PhylomeDBi Q9Y4L1.
TreeFami TF105048.

Enzyme and pathway databases

Reactomei REACT_163813. Scavenging by Class F Receptors.
REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi HYOU1. human.
GeneWikii HYOU1.
GenomeRNAii 10525.
NextBioi 35480619.
PMAP-CutDB Q9Y4L1.
PROi Q9Y4L1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y4L1.
CleanExi HS_HYOU1.
ExpressionAtlasi Q9Y4L1. baseline and differential.
Genevestigatori Q9Y4L1.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100934. SSF100934. 1 hit.
PROSITEi PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150."
    Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T., Matsumoto M., Yura T., Yanagi H.
    Biochem. Biophys. Res. Commun. 230:94-99(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Astrocytoma.
  2. "Production of three distinct mRNAs of 150 kDa oxygen-regulated protein (ORP150) by alternative promoters: preferential induction of one species under stress conditions."
    Kaneda S., Yura T., Yanagi H.
    J. Biochem. 128:529-538(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone."
    Takeuchi S.
    Protein J. 25:517-528(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  4. "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 1 AND 2).
    Tissue: Cerebellum and Trachea.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  6. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 241-256; 541-555; 577-594 AND 754-768, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  9. "150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death."
    Ozawa K., Kuwabara K., Tamatani M., Takatsuji K., Tsukamoto Y., Kaneda S., Yanagi H., Stern D.M., Eguchi Y., Tsujimoto Y., Ogawa S., Tohyama M.
    J. Biol. Chem. 274:6397-6404(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  11. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
  12. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND ASN-931.
    Tissue: Plasma.
  13. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
    Tissue: Platelet.
  14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
    Tissue: Liver.
  15. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
    Tissue: Leukemic T-cell.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHYOU1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4L1
Secondary accession number(s): A8C1Z0
, B7Z909, Q2I204, Q53H25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 141 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3