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Protein

Hornerin

Gene

HRNR

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

Functioni

Component of the epidermal cornified cell envelopes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi19 – 32141PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi62 – 73122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell envelope organization Source: UniProtKB
  • establishment of skin barrier Source: UniProtKB
  • keratinization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Keratinization

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hornerin
Gene namesi
Name:HRNR
Synonyms:S100A18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20846. HRNR.

Subcellular locationi

GO - Cellular componenti

  • cell envelope Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • keratohyalin granule Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134936141.

Polymorphism and mutation databases

DMDMi45476906.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 28502850HornerinPRO_0000144038Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei659 – 6591PhosphoserineCombined sources
Modified residuei661 – 6611PhosphoserineCombined sources
Modified residuei890 – 8901PhosphoserineCombined sources
Modified residuei993 – 9931PhosphoserineCombined sources
Modified residuei1008 – 10081PhosphoserineCombined sources
Modified residuei1463 – 14631PhosphoserineCombined sources
Modified residuei1478 – 14781PhosphoserineCombined sources
Modified residuei1712 – 17121PhosphoserineCombined sources
Modified residuei1714 – 17141PhosphoserineCombined sources
Modified residuei1829 – 18291PhosphoserineCombined sources
Modified residuei1831 – 18311PhosphoserineCombined sources
Modified residuei1933 – 19331PhosphoserineCombined sources
Modified residuei1948 – 19481PhosphoserineCombined sources
Modified residuei2299 – 22991PhosphoserineCombined sources
Modified residuei2301 – 23011PhosphoserineCombined sources
Modified residuei2403 – 24031PhosphoserineCombined sources
Modified residuei2418 – 24181PhosphoserineCombined sources
Modified residuei2652 – 26521PhosphoserineCombined sources
Modified residuei2654 – 26541PhosphoserineCombined sources

Post-translational modificationi

Processed during the process of epidermal differentiation.By similarity
Forms covalent cross-links mediated by transglutaminase TGM3, between glutamine and the epsilon-amino group of lysine residues (in vitro).

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ86YZ3.
MaxQBiQ86YZ3.
PaxDbiQ86YZ3.
PRIDEiQ86YZ3.

2D gel databases

UCD-2DPAGEQ86YZ3.

PTM databases

iPTMnetiQ86YZ3.
PhosphoSiteiQ86YZ3.

Expressioni

Tissue specificityi

Expressed in cornified epidermis, psoriatic and regenerating skin after wounding. Found in the upper granular layer and in the entire cornified layer of epidermis.2 Publications

Inductioni

By UV-B irradiation.1 Publication

Gene expression databases

BgeeiQ86YZ3.
CleanExiHS_HRNR.

Organism-specific databases

HPAiHPA031469.

Interactioni

Protein-protein interaction databases

BioGridi132814. 22 interactions.
IntActiQ86YZ3. 11 interactions.
MINTiMINT-2809380.
STRINGi9606.ENSP00000357791.

Structurei

3D structure databases

ProteinModelPortaliQ86YZ3.
SMRiQ86YZ3. Positions 4-84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 4836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini49 – 8436EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Repeati97 – 187911Add
BLAST
Repeati188 – 278912Add
BLAST
Repeati279 – 369913Add
BLAST
Repeati370 – 460914Add
BLAST
Repeati474 – 566935Add
BLAST
Repeati593 – 683916Add
BLAST
Repeati685 – 747637Add
BLAST
Repeati748 – 836898Add
BLAST
Repeati839 – 875379Add
BLAST
Repeati876 – 9659010Add
BLAST
Repeati966 – 10043911Add
BLAST
Repeati1007 – 10979112Add
BLAST
Repeati1098 – 11889113Add
BLAST
Repeati1215 – 13059114Add
BLAST
Repeati1332 – 14229115Add
BLAST
Repeati1423 – 14745216Add
BLAST
Repeati1477 – 15679117Add
BLAST
Repeati1568 – 16589118Add
BLAST
Repeati1685 – 17759119Add
BLAST
Repeati1802 – 18929120Add
BLAST
Repeati1893 – 19445221Add
BLAST
Repeati1947 – 20379122Add
BLAST
Repeati2038 – 21289123Add
BLAST
Repeati2155 – 22459124Add
BLAST
Repeati2272 – 23629125Add
BLAST
Repeati2363 – 24145226Add
BLAST
Repeati2417 – 25079127Add
BLAST
Repeati2508 – 25989128Add
BLAST
Repeati2625 – 27159129Add
BLAST
Repeati2716 – 28069130Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8181S-100-likeAdd
BLAST

Sequence similaritiesi

Belongs to the S100-fused protein family.Curated
In the N-terminal section; belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IX7U. Eukaryota.
ENOG410ZH9F. LUCA.
GeneTreeiENSGT00530000063634.
HOGENOMiHOG000112590.
InParanoidiQ86YZ3.
OMAiSHHESSQ.
OrthoDBiEOG7QC7VH.
TreeFamiTF338665.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR033201. HRNR.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR22571:SF25. PTHR22571:SF25. 2 hits.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86YZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKLLQGVIT VIDVFYQYAT QHGEYDTLNK AELKELLENE FHQILKNPND
60 70 80 90 100
PDTVDIILQS LDRDHNKKVD FTEYLLMIFK LVQARNKIIG KDYCQVSGSK
110 120 130 140 150
LRDDTHQHQE EQEETEKEEN KRQESSFSHS SWSAGENDSY SRNVRGSLKP
160 170 180 190 200
GTESISRRLS FQRDFSGQHN SYSGQSSSYG EQNSDSHQSS GRGQCGSGSG
210 220 230 240 250
QSPNYGQHGS GSGQSSSNDT HGSGSGQSSG FSQHKSSSGQ SSGYSQHGSG
260 270 280 290 300
SGHSSGYGQH GSRSGQSSRG ERHRSSSGSS SSYGQHGSGS RQSLGHGRQG
310 320 330 340 350
SGSRQSPSHV RHGSGSGHSS SHGQHGSGSS YSYSRGHYES GSGQTSGFGQ
360 370 380 390 400
HESGSGQSSG YSKHGSGSGH SSSQGQHGST SGQASSSGQH GSSSRQSSSY
410 420 430 440 450
GQHESASRHS SGRGQHSSGS GQSPGHGQRG SGSGQSPSSG QHGTGFGRSS
460 470 480 490 500
SSGPYVSGSG YSSGFGHHES SSEHSSGYTQ HGSGSGHSSG HGQHGSRSGQ
510 520 530 540 550
SSRGERQGSS AGSSSSYGQH GSGSRQSLGH SRHGSGSGQS PSPSRGRHES
560 570 580 590 600
GSRQSSSYGP HGYGSGRSSS RGPYESGSGH SSGLGHQESR SGQSSGYGQH
610 620 630 640 650
GSSSGHSSTH GQHGSTSGQS SSCGQHGATS GQSSSHGQHG SGSSQSSRYG
660 670 680 690 700
QQGSGSGQSP SRGRHGSDFG HSSSYGQHGS GSGWSSSNGP HGSVSGQSSG
710 720 730 740 750
FGHKSGSGQS SGYSQHGSGS SHSSGYRKHG SRSGQSSRSE QHGSSSGLSS
760 770 780 790 800
SYGQHGSGSH QSSGHGRQGS GSGHSPSRVR HGSSSGHSSS HGQHGSGTSC
810 820 830 840 850
SSSCGHYESG SGQASGFGQH ESGSGQGYSQ HGSASGHFSS QGRHGSTSGQ
860 870 880 890 900
SSSSGQHDSS SGQSSSYGQH ESASHHASGR GRHGSGSGQS PGHGQRGSGS
910 920 930 940 950
GQSPSYGRHG SGSGRSSSSG RHGSGSGQSS GFGHKSSSGQ SSGYTQHGSG
960 970 980 990 1000
SGHSSSYEQH GSRSGQSSRS EQHGSSSGSS SSYGQHGSGS RQSLGHGQHG
1010 1020 1030 1040 1050
SGSGQSPSPS RGRHGSGSGQ SSSYGPYRSG SGWSSSRGPY ESGSGHSSGL
1060 1070 1080 1090 1100
GHRESRSGQS SGYGQHGSSS GHSSTHGQHG STSGQSSSCG QHGASSGQSS
1110 1120 1130 1140 1150
SHGQHGSGSS QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS YGRHGSGSGR
1160 1170 1180 1190 1200
SSSSGQHGSG LGESSGFGHH ESSSGQSSSY SQHGSGSGHS SGYGQHGSRS
1210 1220 1230 1240 1250
GQSSRGERHG SSSGSSSHYG QHGSGSRQSS GHGRQGSGSG HSPSRGRHGS
1260 1270 1280 1290 1300
GLGHSSSHGQ HGSGSGRSSS RGPYESRSGH SSVFGQHESG SGHSSAYSQH
1310 1320 1330 1340 1350
GSGSGHFCSQ GQHGSTSGQS STFDQEGSST GQSSSYGHRG SGSSQSSGYG
1360 1370 1380 1390 1400
RHGAGSGQSP SRGRHGSGSG HSSSYGQHGS GSGWSSSSGR HGSGSGQSSG
1410 1420 1430 1440 1450
FGHHESSSWQ SSGCTQHGSG SGHSSSYEQH GSRSGQSSRG ERHGSSSGSS
1460 1470 1480 1490 1500
SSYGQHGSGS RQSLGHGQHG SGSGQSPSPS RGRHGSGSGQ SSSYSPYGSG
1510 1520 1530 1540 1550
SGWSSSRGPY ESGSSHSSGL GHRESRSGQS SGYGQHGSSS GHSSTHGQHG
1560 1570 1580 1590 1600
STSGQSSSCG QHGASSGQSS SHGQHGSGSS QSSGYGRQGS GSGQSPGHGQ
1610 1620 1630 1640 1650
RGSGSRQSPS YGRHGSGSGR SSSSGQHGSG LGESSGFGHH ESSSGQSSSY
1660 1670 1680 1690 1700
SQHGSGSGHS SGYGQHGSRS GQSSRGERHG SSSRSSSRYG QHGSGSRQSS
1710 1720 1730 1740 1750
GHGRQGSGSG QSPSRGRHGS GLGHSSSHGQ HGSGSGRSSS RGPYESRSGH
1760 1770 1780 1790 1800
SSVFGQHESG SGHSSAYSQH GSGSGHFCSQ GQHGSTSGQS STFDQEGSST
1810 1820 1830 1840 1850
GQSSSHGQHG SGSSQSSSYG QQGSGSGQSP SRGRHGSGSG HSSSYGQHGS
1860 1870 1880 1890 1900
GSGWSSSSGR HGSGSGQSSG FGHHESSSWQ SSGYTQHGSG SGHSSSYEQH
1910 1920 1930 1940 1950
GSRSGQSSRG EQHGSSSGSS SSYGQHGSGS RQSLGHGQHG SGSGQSPSPS
1960 1970 1980 1990 2000
RGRHGSGSGQ SSSYGPYGSG SGWSSSRGPY ESGSGHSSGL GHRESRSGQS
2010 2020 2030 2040 2050
SGYGQHGSSS GHSSTHGQHG SASGQSSSCG QHGASSGQSS SHGQHGSGSS
2060 2070 2080 2090 2100
QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS YGRHGSGSGR SSSSGQHGPG
2110 2120 2130 2140 2150
LGESSGFGHH ESSSGQSSSY SQHGSGSGHS SGYGQHGSRS GQSSRGERHG
2160 2170 2180 2190 2200
SSSGSSSRYG QHGSGSRQSS GHGRQGSGSG HSPSRGRHGS GSGHSSSHGQ
2210 2220 2230 2240 2250
HGSGSGRSSS RGPYESRSGH SSVFGQHESG SGHSSAYSQH GSGSGHFCSQ
2260 2270 2280 2290 2300
GQHGSTSGQS STFDQEGSST GQSSSHGQHG SGSSQSSSYG QQGSGSGQSP
2310 2320 2330 2340 2350
SRGRHGSGSG HSSSYGQHGS GSGWSSSSGR HGSGSGQSSG FGHHESSSWQ
2360 2370 2380 2390 2400
SSGYTQHGSG SGHSSSYEQH GSRSGQSSRG ERHGSSSGSS SSYGQHGSGS
2410 2420 2430 2440 2450
RQSLGHGQHG SGSGQSPSPS RGRHGSGSGQ SSSYSPYGSG SGWSSSRGPY
2460 2470 2480 2490 2500
ESGSGHSSGL GHRESRSGQS SGYGQHGSSS GHSSTHGQHG STSGQSSSCG
2510 2520 2530 2540 2550
QHGASSGQSS SHGQHGSGSS QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS
2560 2570 2580 2590 2600
YGRHGSGSGR SSSSGQHGSG LGESSGFGHH ESSSGQSSSY SQHGSGSGHS
2610 2620 2630 2640 2650
SGYGQHGSRS GQSSRGERHG SSSGSSSHYG QHGSGSRQSS GHGRQGSGSG
2660 2670 2680 2690 2700
QSPSRGRHGS GLGHSSSHGQ HGSGSGRSSS RGPYESRLGH SSVFGQHESG
2710 2720 2730 2740 2750
SGHSSAYSQH GSGSGHFCSQ GQHGSTSGQS STFDQEGSST GQSSSYGHRG
2760 2770 2780 2790 2800
SGSSQSSGYG RHGAGSGQSL SHGRHGSGSG QSSSYGQHGS GSGQSSGYSQ
2810 2820 2830 2840 2850
HGSGSGQDGY SYCKGGSNHD GGSSGSYFLS FPSSTSPYEY VQEQRCYFYQ
Length:2,850
Mass (Da):282,390
Last modified:March 15, 2004 - v2
Checksum:iF25D8028C5AB6701
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711E → D in AAR91619 (Ref. 2) Curated
Sequence conflicti2382 – 23821R → Q in BAC57496 (PubMed:15507446).Curated
Sequence conflicti2539 – 25391G → S in BAC57496 (PubMed:15507446).Curated
Sequence conflicti2688 – 26881L → S in BAC57496 (PubMed:15507446).Curated
Sequence conflicti2837 – 28371P → T in AAR91619 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851R → H.1 Publication
Corresponds to variant rs11204937 [ dbSNP | Ensembl ].
VAR_048494
Natural varianti122 – 1221R → W.
Corresponds to variant rs57277761 [ dbSNP | Ensembl ].
VAR_061053
Natural varianti167 – 1671G → D.
Corresponds to variant rs12741518 [ dbSNP | Ensembl ].
VAR_048495
Natural varianti273 – 2731H → Q.
Corresponds to variant rs7545406 [ dbSNP | Ensembl ].
VAR_059174
Natural varianti376 – 3761Q → R.
Corresponds to variant rs6587649 [ dbSNP | Ensembl ].
VAR_061054
Natural varianti427 – 4271G → D.
Corresponds to variant rs6666097 [ dbSNP | Ensembl ].
VAR_061055
Natural varianti473 – 4731E → G.
Corresponds to variant rs6587648 [ dbSNP | Ensembl ].
VAR_048496
Natural varianti492 – 4921G → R.
Corresponds to variant rs6587647 [ dbSNP | Ensembl ].
VAR_048497
Natural varianti517 – 5171Y → C.
Corresponds to variant rs41266134 [ dbSNP | Ensembl ].
VAR_061056
Natural varianti664 – 6641R → Q.
Corresponds to variant rs7520249 [ dbSNP | Ensembl ].
VAR_048498
Natural varianti799 – 7991S → T.
Corresponds to variant rs6662450 [ dbSNP | Ensembl ].
VAR_048499
Natural varianti2435 – 24351S → G.
Corresponds to variant rs4248393 [ dbSNP | Ensembl ].
VAR_059175
Natural varianti2461 – 24611G → S.
Corresponds to variant rs6659183 [ dbSNP | Ensembl ].
VAR_059176

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB104446 mRNA. Translation: BAC57496.1.
BR000036 mRNA. Translation: FAA00004.1.
AY396741 mRNA. Translation: AAR91619.1.
AL589986 Genomic DNA. Translation: CAH70026.1.
CCDSiCCDS30859.1.
RefSeqiNP_001009931.1. NM_001009931.2.
UniGeneiHs.490162.

Genome annotation databases

EnsembliENST00000368801; ENSP00000357791; ENSG00000197915.
GeneIDi388697.
KEGGihsa:388697.
UCSCiuc001ezt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB104446 mRNA. Translation: BAC57496.1.
BR000036 mRNA. Translation: FAA00004.1.
AY396741 mRNA. Translation: AAR91619.1.
AL589986 Genomic DNA. Translation: CAH70026.1.
CCDSiCCDS30859.1.
RefSeqiNP_001009931.1. NM_001009931.2.
UniGeneiHs.490162.

3D structure databases

ProteinModelPortaliQ86YZ3.
SMRiQ86YZ3. Positions 4-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi132814. 22 interactions.
IntActiQ86YZ3. 11 interactions.
MINTiMINT-2809380.
STRINGi9606.ENSP00000357791.

PTM databases

iPTMnetiQ86YZ3.
PhosphoSiteiQ86YZ3.

Polymorphism and mutation databases

DMDMi45476906.

2D gel databases

UCD-2DPAGEQ86YZ3.

Proteomic databases

EPDiQ86YZ3.
MaxQBiQ86YZ3.
PaxDbiQ86YZ3.
PRIDEiQ86YZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368801; ENSP00000357791; ENSG00000197915.
GeneIDi388697.
KEGGihsa:388697.
UCSCiuc001ezt.3. human.

Organism-specific databases

CTDi388697.
GeneCardsiHRNR.
H-InvDBHIX0200013.
HGNCiHGNC:20846. HRNR.
HPAiHPA031469.
MIMi616293. gene.
neXtProtiNX_Q86YZ3.
PharmGKBiPA134936141.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IX7U. Eukaryota.
ENOG410ZH9F. LUCA.
GeneTreeiENSGT00530000063634.
HOGENOMiHOG000112590.
InParanoidiQ86YZ3.
OMAiSHHESSQ.
OrthoDBiEOG7QC7VH.
TreeFamiTF338665.

Miscellaneous databases

GenomeRNAii388697.
NextBioi102292.
PROiQ86YZ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ86YZ3.
CleanExiHS_HRNR.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR033201. HRNR.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR22571:SF25. PTHR22571:SF25. 2 hits.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of human hornerin and its expression in regenerating and psoriatic skin."
    Takaishi M., Makino T., Morohashi M., Huh N.-H.
    J. Biol. Chem. 280:4696-4703(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Skin.
  2. "Human intermediate filament-associated protein family."
    Wu Z., Bartels J., Schroeder J.M.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-85.
    Tissue: Skin.
  3. "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.
    , 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].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION, TRANSGLUTAMINATION, TISSUE SPECIFICITY.
  9. "Ultraviolet B irradiation induces the expression of hornerin in xenotransplanted human skin."
    Makino T., Yamakoshi T., Mizawa M., Shimizu T.
    Acta Histochem. 116:20-24(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY UV-B.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659; SER-661; SER-993; SER-1008; SER-1463; SER-1478; SER-1712; SER-1714; SER-1829; SER-1831; SER-1933; SER-1948; SER-2299; SER-2301; SER-2403; SER-2418; SER-2652 AND SER-2654, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHORN_HUMAN
AccessioniPrimary (citable) accession number: Q86YZ3
Secondary accession number(s): Q5DT20, Q5U1F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: May 11, 2016
This is version 117 of the entry and version 2 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 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.