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Protein

Apolipoprotein B receptor

Gene

APOBR

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

Functioni

Macrophage receptor that binds to the apolipoprotein B48 (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a like domain of APOB in hypertriglyceridemic very low density lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the context of the macrophage. May provide essential lipids to reticuloendothelial cells. Could also be involved in foam cell formation with elevated TRL and remnant lipoprotein (RLP). Mediates the rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein B receptor
Alternative name(s):
Apolipoprotein B-100 receptor
Apolipoprotein B-48 receptor
Short name:
Apolipoprotein B48 receptor
Short name:
apoB-48R
Gene namesi
Name:APOBR
Synonyms:APOB48R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:24087. APOBR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chylomicron, LDL, Membrane, VLDL

Pathology & Biotechi

Keywords - Diseasei

Atherosclerosis

Polymorphism and mutation databases

BioMutaiAPOBR.
DMDMi519668661.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10881088Apolipoprotein B receptorPRO_0000327263Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei449 – 4491PhosphoserineBy similarity
Modified residuei501 – 5011PhosphoserineCombined sources
Modified residuei585 – 5851PhosphoserineBy similarity

Post-translational modificationi

There are 2 forms in macrophages, the membrane-binding proteins 200 kDa (MBP 200) and 235 kDa (MBP 235), that can be reduced into a single active ligand-binding species with intermediate mobility (MBP 200R).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ0VD83.
MaxQBiQ0VD83.
PaxDbiQ0VD83.
PRIDEiQ0VD83.

PTM databases

iPTMnetiQ0VD83.
PhosphoSiteiQ0VD83.

Expressioni

Tissue specificityi

Expressed in peripheral blood leukocytes > bone marrow = spleen > lymph node, and only faintly visible in appendix and thymus. Expressed in the brain, heart, kidney, liver, lung, pancreas, and placenta. Expressed primarily by reticuloendothelial cells: monocytes, macrophages, and endothelial cells. Expressed in atherosclerotic lesion foam cells.2 Publications

Inductioni

Suppressed significantly by PPARA and PPARG in THP-1 and blood-borne monocyte-macrophages. Decreased after pitavastatin treatment in peripheral blood macrophages and remnant lipoprotein (RLP)-induced foam cell formation.2 Publications

Gene expression databases

BgeeiQ0VD83.
GenevisibleiQ0VD83. HS.

Organism-specific databases

HPAiHPA041667.
HPA042093.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiQ0VD83. 2 interactions.
STRINGi9606.ENSP00000457539.

Structurei

3D structure databases

ProteinModelPortaliQ0VD83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi158 – 961804Glu-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410J3HP. Eukaryota.
ENOG410XRQZ. LUCA.
GeneTreeiENSGT00530000065031.
HOVERGENiHBG073497.
InParanoidiQ0VD83.
OMAiRCQEPSA.
OrthoDBiEOG7X6KZS.
PhylomeDBiQ0VD83.
TreeFamiTF337147.

Family and domain databases

InterProiIPR026158. ApolipoprotB_rcpt.
[Graphical view]
PANTHERiPTHR15964. PTHR15964. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q0VD83-1) [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
MDFLRLYLPG LHQALRGALD SLGTFVSYLL GDAVPTVERE AQAAEELGVV
60 70 80 90 100
AVGKTGKIVE EEAQEDLEGL RGSQNEGAGR LRGPGDDRRH EVGSSAVEQT
110 120 130 140 150
WGWGDGSSHG SQAERQDSGA GETAKAARCQ EPSAHLEARK KSKAGSGACQ
160 170 180 190 200
DRSGQAQERQ ESHEQEVNRE ERLRSWEQEE EEEEVRAREP GMARGAESEW
210 220 230 240 250
TWHGETEGKA GAVGPKAAGD NREMEQGVRE ADAGETEEPG AEGAGKGEEV
260 270 280 290 300
VVVEKACEST RAWGTWGPGA EPEDWGILGR EEARTTPGRE EARAILDGEE
310 320 330 340 350
ARTISGGEEA ETASGGEEAE TASGGEEAGT ASGGEEAGIA SGGEAGTASG
360 370 380 390 400
GEEAGTASGG DEAWTTSGKE EADLLGVRQT EYGAVPGERL LEATGKVWVL
410 420 430 440 450
EEEGDEEREA EVSPFPKQPQ VLGTERTEEA AESQTAGREA VGGQEAGESF
460 470 480 490 500
EGQVDLRGKE AEMRQDLGIR ADRARMEELV QAEEAQEERG SSRDPVAELP
510 520 530 540 550
SDGEAEGTAD LEATPEARPE EELTGEESEA AQTSCGLLGV EWGGLTHSVT
560 570 580 590 600
KGQGPELMGG AQTPTKQPEE REAGEVELMG VLALSKEEQE RSLEAGPRHA
610 620 630 640 650
GSVKPEASEA FPGAWENRTR KDMERGNTQE DAADGEQREE EETAGGQTLA
660 670 680 690 700
AEAEGDRESE LSEVPEAGGE GLTTQDAGCG TEEGEASVSE NQELDGSTGA
710 720 730 740 750
DAGPCPSLGE AYARETEDEE AEADRTSRRG WRLQAVAVGL PDREDAQTGS
760 770 780 790 800
VAAGIMGGDV VPHISAAGAG EALEGVLGQG WDSKEKEEAA AGEHAGGQEF
810 820 830 840 850
GLEGSAEEEV TGRGSQVEAF ESREGGPWGG RVEAEESAGA EDSCGLDPAG
860 870 880 890 900
SQTARAEGMG AMVEAGGLLE KWTLLEEEAV GWQEREQRED SEGRCGDYHP
910 920 930 940 950
EGEAPRLLDA EGLMVTGGRR AEAKETEPES LEHVRGQEEQ PTHQAPAEAA
960 970 980 990 1000
PESVGEAETA EAMGSARGGA ANSWSEAPLP GSLLDVSVPR SRVHLSRSSS
1010 1020 1030 1040 1050
QRRSRPSFRR TPAWEQQEEP PAPNPPEEEL SAPEQRPLQL EEPLEPSPLR
1060 1070 1080
HDGTPVPARR RPLGHGFGLA HPGMMQELQA RLGRPKPQ
Length:1,088
Mass (Da):114,874
Last modified:June 26, 2013 - v2
Checksum:i95B2D492E873E624
GO
Isoform 2 (identifier: Q0VD83-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-462: Missing.

Note: No experimental confirmation available.
Show »
Length:626
Mass (Da):66,335
Checksum:iCD3C36057E9603F5
GO
Isoform 3 (identifier: Q0VD83-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1047-1088: SPLRHDGTPVPARRRPLGHGFGLAHPGMMQELQARLGRPKPQ → RWEDRLRPGVRDQPGQHSKIPIF

Note: No experimental confirmation available.
Show »
Length:1,069
Mass (Da):113,041
Checksum:i904BB04262416644
GO
Isoform 4 (identifier: Q0VD83-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     343-343: G → GEAGTASGGE

Note: Gene prediction based on EST data.
Show »
Length:1,097
Mass (Da):115,634
Checksum:i55BADDAD96EB16E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti340 – 3401A → S in AAF76255 (PubMed:10852956).Curated
Sequence conflicti340 – 3401A → S in AAF76256 (PubMed:10852956).Curated
Sequence conflicti381 – 3811E → Q in AAF76255 (PubMed:10852956).Curated
Sequence conflicti381 – 3811E → Q in AAF76256 (PubMed:10852956).Curated
Sequence conflicti776 – 7761V → A in AAF76255 (PubMed:10852956).Curated
Sequence conflicti776 – 7761V → A in AAF76256 (PubMed:10852956).Curated
Sequence conflicti776 – 7761V → A in AAI19787 (PubMed:15489334).Curated
Sequence conflicti776 – 7761V → A in AAI19789 (PubMed:15489334).Curated
Sequence conflicti776 – 7761V → A in AK075085 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti419 – 4191P → A.3 Publications
Corresponds to variant rs180743 [ dbSNP | Ensembl ].
VAR_042432

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 462462Missing in isoform 2. 1 PublicationVSP_032733Add
BLAST
Alternative sequencei343 – 3431G → GEAGTASGGE in isoform 4. CuratedVSP_047051
Alternative sequencei1047 – 108842SPLRH…RPKPQ → RWEDRLRPGVRDQPGQHSKI PIF in isoform 3. 1 PublicationVSP_032734Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF141332 mRNA. Translation: AAF76255.1.
AF141333 Genomic DNA. Translation: AAF76256.1.
AC138894 Genomic DNA. No translation available.
BC119786 mRNA. Translation: AAI19787.1.
BC119788 mRNA. Translation: AAI19789.1.
AK075085 mRNA. No translation available.
CCDSiCCDS58442.1. [Q0VD83-4]
RefSeqiNP_061160.3. NM_018690.3. [Q0VD83-4]
UniGeneiHs.200333.

Genome annotation databases

EnsembliENST00000431282; ENSP00000416094; ENSG00000184730. [Q0VD83-1]
ENST00000564831; ENSP00000457539; ENSG00000184730. [Q0VD83-4]
GeneIDi55911.
KEGGihsa:55911.
UCSCiuc002dqb.2. human. [Q0VD83-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF141332 mRNA. Translation: AAF76255.1.
AF141333 Genomic DNA. Translation: AAF76256.1.
AC138894 Genomic DNA. No translation available.
BC119786 mRNA. Translation: AAI19787.1.
BC119788 mRNA. Translation: AAI19789.1.
AK075085 mRNA. No translation available.
CCDSiCCDS58442.1. [Q0VD83-4]
RefSeqiNP_061160.3. NM_018690.3. [Q0VD83-4]
UniGeneiHs.200333.

3D structure databases

ProteinModelPortaliQ0VD83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ0VD83. 2 interactions.
STRINGi9606.ENSP00000457539.

PTM databases

iPTMnetiQ0VD83.
PhosphoSiteiQ0VD83.

Polymorphism and mutation databases

BioMutaiAPOBR.
DMDMi519668661.

Proteomic databases

EPDiQ0VD83.
MaxQBiQ0VD83.
PaxDbiQ0VD83.
PRIDEiQ0VD83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000431282; ENSP00000416094; ENSG00000184730. [Q0VD83-1]
ENST00000564831; ENSP00000457539; ENSG00000184730. [Q0VD83-4]
GeneIDi55911.
KEGGihsa:55911.
UCSCiuc002dqb.2. human. [Q0VD83-1]

Organism-specific databases

CTDi55911.
GeneCardsiAPOBR.
HGNCiHGNC:24087. APOBR.
HPAiHPA041667.
HPA042093.
MIMi605220. gene.
neXtProtiNX_Q0VD83.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J3HP. Eukaryota.
ENOG410XRQZ. LUCA.
GeneTreeiENSGT00530000065031.
HOVERGENiHBG073497.
InParanoidiQ0VD83.
OMAiRCQEPSA.
OrthoDBiEOG7X6KZS.
PhylomeDBiQ0VD83.
TreeFamiTF337147.

Miscellaneous databases

GenomeRNAii55911.
NextBioi13609695.
PROiQ0VD83.
SOURCEiSearch...

Gene expression databases

BgeeiQ0VD83.
GenevisibleiQ0VD83. HS.

Family and domain databases

InterProiIPR026158. ApolipoprotB_rcpt.
[Graphical view]
PANTHERiPTHR15964. PTHR15964. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 814-821; 857-868 AND 910-919, FUNCTION, TISSUE SPECIFICITY, VARIANT ALA-419.
    Tissue: Monocytic leukemia and Placenta.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2), VARIANT ALA-419.
  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] OF 756-1088 (ISOFORM 3).
    Tissue: Placenta.
  5. "Antipeptide antibodies reveal interrelationships of MBP 200 and MBP 235: unique apoB-specific receptors for triglyceride-rich lipoproteins on human monocyte-macrophages."
    Bradley W.A., Brown M.L., Ramprasad M.P., Li R., Song R., Gianturco S.H.
    J. Lipid Res. 40:744-752(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 910-919, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POST-TRANSLATIONAL MODIFICATION.
  6. "Human THP-1 monocyte-macrophage membrane binding proteins: distinct receptor(s) for triglyceride-rich lipoproteins."
    Ramprasad M.P., Li R., Bradley W.A., Gianturco S.H.
    Biochemistry 34:9126-9135(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Apolipoprotein B-48 or its apolipoprotein B-100 equivalent mediates the binding of triglyceride-rich lipoproteins to their unique human monocyte-macrophage receptor."
    Gianturco S.H., Ramprasad M.P., Song R., Li R., Brown M.L., Bradley W.A.
    Arterioscler. Thromb. Vasc. Biol. 18:968-976(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "PPAR(alpha) and PPAR(gamma) activators suppress the monocyte-macrophage apoB-48 receptor."
    Haraguchi G., Kobayashi Y., Brown M.L., Tanaka A., Isobe M., Gianturco S.H., Bradley W.A.
    J. Lipid Res. 44:1224-1231(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Pitavastatin inhibits remnant lipoprotein-induced macrophage foam cell formation through ApoB48 receptor-dependent mechanism."
    Kawakami A., Tani M., Chiba T., Yui K., Shinozaki S., Nakajima K., Tanaka A., Shimokado K., Yoshida M.
    Arterioscler. Thromb. Vasc. Biol. 25:424-429(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  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-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Association of nucleotide variations in the apolipoprotein B48 receptor gene (APOB48R) with hypercholesterolemia."
    Fujita Y., Ezura Y., Bujo H., Nakajima T., Takahashi K., Kamimura K., Iino Y., Katayama Y., Saito Y., Emi M.
    J. Hum. Genet. 50:203-209(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-419.

Entry informationi

Entry nameiAPOBR_HUMAN
AccessioniPrimary (citable) accession number: Q0VD83
Secondary accession number(s): H3BU97
, Q0VD81, Q8NC15, Q9NPJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 26, 2013
Last modified: March 16, 2016
This is version 77 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

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.