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O95487

- SC24B_HUMAN

UniProt

O95487 - SC24B_HUMAN

Protein

Protein transport protein Sec24B

Gene

SEC24B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transporter activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    3. cellular protein metabolic process Source: Reactome
    4. COPII vesicle coating Source: Reactome
    5. ER to Golgi vesicle-mediated transport Source: Reactome
    6. intracellular protein transport Source: InterPro
    7. membrane organization Source: Reactome
    8. post-translational protein modification Source: Reactome
    9. protein N-linked glycosylation via asparagine Source: Reactome
    10. small molecule metabolic process Source: Reactome
    11. vesicle-mediated transport Source: ProtInc

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
    REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein transport protein Sec24B
    Alternative name(s):
    SEC24-related protein B
    Gene namesi
    Name:SEC24B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:10704. SEC24B.

    Subcellular locationi

    GO - Cellular componenti

    1. COPII vesicle coat Source: InterPro
    2. cytosol Source: Reactome
    3. endoplasmic reticulum membrane Source: Reactome
    4. ER to Golgi transport vesicle membrane Source: Reactome
    5. Golgi membrane Source: UniProtKB-SubCell
    6. membrane Source: ProtInc
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35627.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 12681267Protein transport protein Sec24BPRO_0000205155Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei1224 – 12241Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95487.
    PaxDbiO95487.
    PRIDEiO95487.

    PTM databases

    PhosphoSiteiO95487.

    Expressioni

    Tissue specificityi

    Expressed in fibroblasts, hepatocytes, and lymphocytes.

    Gene expression databases

    ArrayExpressiO95487.
    BgeeiO95487.
    CleanExiHS_SEC24B.
    GenevestigatoriO95487.

    Organism-specific databases

    HPAiHPA038181.

    Interactioni

    Subunit structurei

    COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and SAR1. SEC24B is capable of forming heterodimers with SEC24A. Interacts with RNF139. Interacts with TMED2 and TMED10.2 Publications

    Protein-protein interaction databases

    BioGridi115696. 11 interactions.
    IntActiO95487. 10 interactions.
    MINTiMINT-6772353.
    STRINGi9606.ENSP00000265175.

    Structurei

    Secondary structure

    1
    1268
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi520 – 5223
    Beta strandi524 – 5263
    Turni527 – 5293
    Helixi548 – 5536
    Turni557 – 5593
    Beta strandi560 – 57011
    Helixi571 – 5777
    Beta strandi582 – 5854
    Turni606 – 6083
    Beta strandi617 – 6259
    Turni627 – 6293
    Beta strandi632 – 6343
    Helixi637 – 6393
    Helixi651 – 6533
    Helixi655 – 6584
    Beta strandi660 – 6667
    Helixi668 – 6703
    Beta strandi672 – 6743
    Beta strandi679 – 6857
    Helixi688 – 6936
    Helixi695 – 70612
    Turni707 – 7093
    Beta strandi717 – 73115
    Beta strandi740 – 7456
    Helixi755 – 7573
    Beta strandi759 – 7613
    Turni762 – 7654
    Helixi766 – 77510
    Helixi776 – 7783
    Helixi790 – 80112
    Turni802 – 8043
    Beta strandi806 – 8127
    Helixi831 – 8344
    Beta strandi835 – 8373
    Helixi847 – 85711
    Beta strandi860 – 8667
    Helixi874 – 8774
    Helixi879 – 8824
    Turni883 – 8853
    Beta strandi888 – 8903
    Turni896 – 8983
    Helixi900 – 91516
    Beta strandi919 – 92810
    Beta strandi932 – 94312
    Beta strandi945 – 95410
    Beta strandi960 – 9689
    Beta strandi974 – 98512
    Beta strandi991 – 100313
    Helixi1006 – 10116
    Helixi1015 – 103218
    Helixi1035 – 105420
    Beta strandi1066 – 10683
    Helixi1069 – 10713
    Helixi1074 – 10829
    Turni1085 – 10873
    Helixi1095 – 110713
    Helixi1110 – 11178
    Beta strandi1120 – 11234
    Beta strandi1133 – 11353
    Beta strandi1138 – 11403
    Helixi1150 – 11523
    Beta strandi1157 – 11626
    Beta strandi1164 – 11718
    Helixi1177 – 11826
    Helixi1189 – 11913
    Beta strandi1194 – 11963
    Helixi1205 – 121915
    Beta strandi1221 – 12233
    Beta strandi1226 – 123611
    Helixi1237 – 12415
    Helixi1255 – 126713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EH1X-ray1.80A518-1268[»]
    ProteinModelPortaliO95487.
    SMRiO95487. Positions 518-1268.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95487.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni605 – 62925Zinc finger-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi379 – 3879Poly-Glu

    Sequence similaritiesi

    Belongs to the SEC23/SEC24 family. SEC24 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5028.
    HOGENOMiHOG000196365.
    HOVERGENiHBG054850.
    KOiK14007.
    PhylomeDBiO95487.
    TreeFamiTF354244.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR006900. Sec23/24_helical_dom.
    IPR006896. Sec23/24_trunk_dom.
    IPR012990. Sec23_24_beta_S.
    IPR002035. VWF_A.
    IPR006895. Znf_Sec23_Sec24.
    [Graphical view]
    PfamiPF00626. Gelsolin. 1 hit.
    PF08033. Sec23_BS. 1 hit.
    PF04815. Sec23_helical. 1 hit.
    PF04811. Sec23_trunk. 1 hit.
    PF04810. zf-Sec23_Sec24. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    SSF81811. SSF81811. 1 hit.
    SSF82919. SSF82919. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95487-1) [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

    MSAPAGSSHP AASARIPPKF GGAAVSGAAA PAGPGAGPAP HQQNGPAQNQ     50
    MQVPSGYGLH HQNYIAPSGH YSQGPGKMTS LPLDTQCGDY YSALYTVPTQ 100
    NVTPNTVNQQ PGAQQLYSRG PPAPHIVGST LGSFQGAASS ASHLHTSASQ 150
    PYSSFVNHYN SPAMYSASSS VASQGFPSTC GHYAMSTVSN AAYPSVSYPS 200
    LPAGDTYGQM FTSQNAPTVR PVKDNSFSGQ NTAISHPSPL PPLPSQQHHQ 250
    QQSLSGYSTL TWSSPGLPST QDNLIRNHTG SLAVANNNPT ITVADSLSCP 300
    VMQNVQPPKS SPVVSTVLSG SSGSSSTRTP PTANHPVEPV TSVTQPSELL 350
    QQKGVQYGEY VNNQASSAPT PLSSTSDDEE EEEEDEEAGV DSSSTTSSAS 400
    PMPNSYDALE GGSYPDMLSS SASSPAPDPA PEPDPASAPA PASAPAPVVP 450
    QPSKMAKPFG YGYPTLQPGY QNATAPLISG VQPSNPVYSG FQQYPQQYPG 500
    VNQLSSSIGG LSLQSSPQPE SLRPVNLTQE RNILPMTPVW APVPNLNADL 550
    KKLNCSPDSF RCTLTNIPQT QALLNKAKLP LGLLLHPFRD LTQLPVITSN 600
    TIVRCRSCRT YINPFVSFID QRRWKCNLCY RVNDVPEEFM YNPLTRSYGE 650
    PHKRPEVQNS TVEFIASSDY MLRPPQPAVY LFVLDVSHNA VEAGYLTILC 700
    QSLLENLDKL PGDSRTRIGF MTFDSTIHFY NLQEGLSQPQ MLIVSDIDDV 750
    FLPTPDSLLV NLYESKELIK DLLNALPNMF TNTRETHSAL GPALQAAFKL 800
    MSPTGGRVSV FQTQLPSLGA GLLQSREDPN QRSSTKVVQH LGPATDFYKK 850
    LALDCSGQQT AVDLFLLSSQ YSDLASLACM SKYSAGCIYY YPSFHYTHNP 900
    SQAEKLQKDL KRYLTRKIGF EAVMRIRCTK GLSMHTFHGN FFVRSTDLLS 950
    LANINPDAGF AVQLSIEESL TDTSLVCFQT ALLYTSSKGE RRIRVHTLCL 1000
    PVVSSLADVY AGVDVQAAIC LLANMAVDRS VSSSLSDARD ALVNAVVDSL 1050
    SAYGSTVSNL QHSALMAPSS LKLFPLYVLA LLKQKAFRTG TSTRLDDRVY 1100
    AMCQIKSQPL VHLMKMIHPN LYRIDRLTDE GAVHVNDRIV PQPPLQKLSA 1150
    EKLTREGAFL MDCGSVFYIW VGKGCDNNFI EDVLGYTNFA SIPQKMTHLP 1200
    ELDTLSSERA RSFITWLRDS RPLSPILHIV KDESPAKAEF FQHLIEDRTE 1250
    AAFSYYEFLL HVQQQICK 1268
    Length:1,268
    Mass (Da):137,418
    Last modified:December 16, 2008 - v2
    Checksum:i0E08B982D0982F84
    GO
    Isoform 2 (identifier: O95487-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         354-388: Missing.

    Show »
    Length:1,233
    Mass (Da):133,629
    Checksum:i95EEBB976F613B6B
    GO
    Isoform 3 (identifier: O95487-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         44-44: N → NETGFHHVAQASLELLDPSNLPASASQIAGST
         496-496: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,298
    Mass (Da):140,421
    Checksum:i3B649E12AEF0F17C
    GO

    Sequence cautioni

    The sequence CAA10335.1 differs from that shown. Reason: Frameshift at positions 459 and 483.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231A → S in CAA10335. (PubMed:10075675)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti456 – 4561A → G.
    Corresponds to variant rs35705351 [ dbSNP | Ensembl ].
    VAR_047934

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei44 – 441N → NETGFHHVAQASLELLDPSN LPASASQIAGST in isoform 3. 1 PublicationVSP_054432
    Alternative sequencei354 – 38835Missing in isoform 2. 1 PublicationVSP_035987Add
    BLAST
    Alternative sequencei496 – 4961Missing in isoform 3. 1 PublicationVSP_054433

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131245 mRNA. Translation: CAA10335.1. Frameshift.
    AC105314 Genomic DNA. No translation available.
    AC138782 Genomic DNA. No translation available.
    BC040137 mRNA. Translation: AAH40137.1.
    BC117135 mRNA. Translation: AAI17136.1.
    BC143268 mRNA. Translation: AAI43269.1.
    BC143276 mRNA. Translation: AAI43277.1.
    CCDSiCCDS43260.1. [O95487-2]
    CCDS47124.1. [O95487-1]
    RefSeqiNP_001036199.1. NM_001042734.1. [O95487-2]
    NP_006314.2. NM_006323.2. [O95487-1]
    XP_005262746.1. XM_005262689.1. [O95487-3]
    UniGeneiHs.292472.

    Genome annotation databases

    EnsembliENST00000265175; ENSP00000265175; ENSG00000138802. [O95487-1]
    ENST00000399100; ENSP00000382051; ENSG00000138802. [O95487-2]
    ENST00000504968; ENSP00000428564; ENSG00000138802. [O95487-3]
    GeneIDi10427.
    KEGGihsa:10427.
    UCSCiuc003hzk.3. human. [O95487-1]
    uc003hzl.3. human. [O95487-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131245 mRNA. Translation: CAA10335.1 . Frameshift.
    AC105314 Genomic DNA. No translation available.
    AC138782 Genomic DNA. No translation available.
    BC040137 mRNA. Translation: AAH40137.1 .
    BC117135 mRNA. Translation: AAI17136.1 .
    BC143268 mRNA. Translation: AAI43269.1 .
    BC143276 mRNA. Translation: AAI43277.1 .
    CCDSi CCDS43260.1. [O95487-2 ]
    CCDS47124.1. [O95487-1 ]
    RefSeqi NP_001036199.1. NM_001042734.1. [O95487-2 ]
    NP_006314.2. NM_006323.2. [O95487-1 ]
    XP_005262746.1. XM_005262689.1. [O95487-3 ]
    UniGenei Hs.292472.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EH1 X-ray 1.80 A 518-1268 [» ]
    ProteinModelPortali O95487.
    SMRi O95487. Positions 518-1268.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115696. 11 interactions.
    IntActi O95487. 10 interactions.
    MINTi MINT-6772353.
    STRINGi 9606.ENSP00000265175.

    PTM databases

    PhosphoSitei O95487.

    Proteomic databases

    MaxQBi O95487.
    PaxDbi O95487.
    PRIDEi O95487.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265175 ; ENSP00000265175 ; ENSG00000138802 . [O95487-1 ]
    ENST00000399100 ; ENSP00000382051 ; ENSG00000138802 . [O95487-2 ]
    ENST00000504968 ; ENSP00000428564 ; ENSG00000138802 . [O95487-3 ]
    GeneIDi 10427.
    KEGGi hsa:10427.
    UCSCi uc003hzk.3. human. [O95487-1 ]
    uc003hzl.3. human. [O95487-2 ]

    Organism-specific databases

    CTDi 10427.
    GeneCardsi GC04P110354.
    HGNCi HGNC:10704. SEC24B.
    HPAi HPA038181.
    MIMi 607184. gene.
    neXtProti NX_O95487.
    PharmGKBi PA35627.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5028.
    HOGENOMi HOG000196365.
    HOVERGENi HBG054850.
    KOi K14007.
    PhylomeDBi O95487.
    TreeFami TF354244.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
    REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Miscellaneous databases

    ChiTaRSi SEC24B. human.
    EvolutionaryTracei O95487.
    GeneWikii SEC24B.
    GenomeRNAii 10427.
    NextBioi 35481162.
    PROi O95487.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95487.
    Bgeei O95487.
    CleanExi HS_SEC24B.
    Genevestigatori O95487.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR006900. Sec23/24_helical_dom.
    IPR006896. Sec23/24_trunk_dom.
    IPR012990. Sec23_24_beta_S.
    IPR002035. VWF_A.
    IPR006895. Znf_Sec23_Sec24.
    [Graphical view ]
    Pfami PF00626. Gelsolin. 1 hit.
    PF08033. Sec23_BS. 1 hit.
    PF04815. Sec23_helical. 1 hit.
    PF04811. Sec23_trunk. 1 hit.
    PF04810. zf-Sec23_Sec24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    SSF81811. SSF81811. 1 hit.
    SSF82919. SSF82919. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: B-cell.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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; 2 AND 3).
      Tissue: Brain and Eye.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. "The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage."
      Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.
      J. Biol. Chem. 284:28995-29004(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF139.
    8. "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.
    9. "Selective export of human GPI-anchored proteins from the endoplasmic reticulum."
      Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.
      J. Cell Sci. 123:1705-1715(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMED2 AND TMED10.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSC24B_HUMAN
    AccessioniPrimary (citable) accession number: O95487
    Secondary accession number(s): B7ZKM8, B7ZKN4, Q0VG08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 124 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3