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Protein

Protein transport protein Sec24B

Gene

SEC24B

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

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

  • transporter activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10704. SEC24B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35627.

Polymorphism and mutation databases

BioMutaiSEC24B.

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 – 12241Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95487.
PaxDbiO95487.
PRIDEiO95487.

PTM databases

PhosphoSiteiO95487.

Expressioni

Tissue specificityi

Expressed in fibroblasts, hepatocytes, and lymphocytes.

Gene expression databases

BgeeiO95487.
CleanExiHS_SEC24B.
GenevisibleiO95487. HS.

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. Interacts with CNIH4 (PubMed:24405750).3 Publications

Protein-protein interaction databases

BioGridi115696. 12 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 – 5223Combined sources
Beta strandi524 – 5263Combined sources
Turni527 – 5293Combined sources
Helixi548 – 5536Combined sources
Turni557 – 5593Combined sources
Beta strandi560 – 57011Combined sources
Helixi571 – 5777Combined sources
Beta strandi582 – 5854Combined sources
Turni606 – 6083Combined sources
Beta strandi617 – 6259Combined sources
Turni627 – 6293Combined sources
Beta strandi632 – 6343Combined sources
Helixi637 – 6393Combined sources
Helixi651 – 6533Combined sources
Helixi655 – 6584Combined sources
Beta strandi660 – 6667Combined sources
Helixi668 – 6703Combined sources
Beta strandi672 – 6743Combined sources
Beta strandi679 – 6857Combined sources
Helixi688 – 6936Combined sources
Helixi695 – 70612Combined sources
Turni707 – 7093Combined sources
Beta strandi717 – 73115Combined sources
Beta strandi740 – 7456Combined sources
Helixi755 – 7573Combined sources
Beta strandi759 – 7613Combined sources
Turni762 – 7654Combined sources
Helixi766 – 77510Combined sources
Helixi776 – 7783Combined sources
Helixi790 – 80112Combined sources
Turni802 – 8043Combined sources
Beta strandi806 – 8127Combined sources
Helixi831 – 8344Combined sources
Beta strandi835 – 8373Combined sources
Helixi847 – 85711Combined sources
Beta strandi860 – 8667Combined sources
Helixi874 – 8774Combined sources
Helixi879 – 8824Combined sources
Turni883 – 8853Combined sources
Beta strandi888 – 8903Combined sources
Turni896 – 8983Combined sources
Helixi900 – 91516Combined sources
Beta strandi919 – 92810Combined sources
Beta strandi932 – 94312Combined sources
Beta strandi945 – 95410Combined sources
Beta strandi960 – 9689Combined sources
Beta strandi974 – 98512Combined sources
Beta strandi991 – 100313Combined sources
Helixi1006 – 10116Combined sources
Helixi1015 – 103218Combined sources
Helixi1035 – 105420Combined sources
Beta strandi1066 – 10683Combined sources
Helixi1069 – 10713Combined sources
Helixi1074 – 10829Combined sources
Turni1085 – 10873Combined sources
Helixi1095 – 110713Combined sources
Helixi1110 – 11178Combined sources
Beta strandi1120 – 11234Combined sources
Beta strandi1133 – 11353Combined sources
Beta strandi1138 – 11403Combined sources
Helixi1150 – 11523Combined sources
Beta strandi1157 – 11626Combined sources
Beta strandi1164 – 11718Combined sources
Helixi1177 – 11826Combined sources
Helixi1189 – 11913Combined sources
Beta strandi1194 – 11963Combined sources
Helixi1205 – 121915Combined sources
Beta strandi1221 – 12233Combined sources
Beta strandi1226 – 123611Combined sources
Helixi1237 – 12415Combined sources
Helixi1255 – 126713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00590000082962.
HOGENOMiHOG000196365.
HOVERGENiHBG054850.
InParanoidiO95487.
KOiK14007.
OMAiNILPMTP.
OrthoDBiEOG7R56RS.
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. AlignAdd to basket

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

        10         20         30         40         50
MSAPAGSSHP AASARIPPKF GGAAVSGAAA PAGPGAGPAP HQQNGPAQNQ
60 70 80 90 100
MQVPSGYGLH HQNYIAPSGH YSQGPGKMTS LPLDTQCGDY YSALYTVPTQ
110 120 130 140 150
NVTPNTVNQQ PGAQQLYSRG PPAPHIVGST LGSFQGAASS ASHLHTSASQ
160 170 180 190 200
PYSSFVNHYN SPAMYSASSS VASQGFPSTC GHYAMSTVSN AAYPSVSYPS
210 220 230 240 250
LPAGDTYGQM FTSQNAPTVR PVKDNSFSGQ NTAISHPSPL PPLPSQQHHQ
260 270 280 290 300
QQSLSGYSTL TWSSPGLPST QDNLIRNHTG SLAVANNNPT ITVADSLSCP
310 320 330 340 350
VMQNVQPPKS SPVVSTVLSG SSGSSSTRTP PTANHPVEPV TSVTQPSELL
360 370 380 390 400
QQKGVQYGEY VNNQASSAPT PLSSTSDDEE EEEEDEEAGV DSSSTTSSAS
410 420 430 440 450
PMPNSYDALE GGSYPDMLSS SASSPAPDPA PEPDPASAPA PASAPAPVVP
460 470 480 490 500
QPSKMAKPFG YGYPTLQPGY QNATAPLISG VQPSNPVYSG FQQYPQQYPG
510 520 530 540 550
VNQLSSSIGG LSLQSSPQPE SLRPVNLTQE RNILPMTPVW APVPNLNADL
560 570 580 590 600
KKLNCSPDSF RCTLTNIPQT QALLNKAKLP LGLLLHPFRD LTQLPVITSN
610 620 630 640 650
TIVRCRSCRT YINPFVSFID QRRWKCNLCY RVNDVPEEFM YNPLTRSYGE
660 670 680 690 700
PHKRPEVQNS TVEFIASSDY MLRPPQPAVY LFVLDVSHNA VEAGYLTILC
710 720 730 740 750
QSLLENLDKL PGDSRTRIGF MTFDSTIHFY NLQEGLSQPQ MLIVSDIDDV
760 770 780 790 800
FLPTPDSLLV NLYESKELIK DLLNALPNMF TNTRETHSAL GPALQAAFKL
810 820 830 840 850
MSPTGGRVSV FQTQLPSLGA GLLQSREDPN QRSSTKVVQH LGPATDFYKK
860 870 880 890 900
LALDCSGQQT AVDLFLLSSQ YSDLASLACM SKYSAGCIYY YPSFHYTHNP
910 920 930 940 950
SQAEKLQKDL KRYLTRKIGF EAVMRIRCTK GLSMHTFHGN FFVRSTDLLS
960 970 980 990 1000
LANINPDAGF AVQLSIEESL TDTSLVCFQT ALLYTSSKGE RRIRVHTLCL
1010 1020 1030 1040 1050
PVVSSLADVY AGVDVQAAIC LLANMAVDRS VSSSLSDARD ALVNAVVDSL
1060 1070 1080 1090 1100
SAYGSTVSNL QHSALMAPSS LKLFPLYVLA LLKQKAFRTG TSTRLDDRVY
1110 1120 1130 1140 1150
AMCQIKSQPL VHLMKMIHPN LYRIDRLTDE GAVHVNDRIV PQPPLQKLSA
1160 1170 1180 1190 1200
EKLTREGAFL MDCGSVFYIW VGKGCDNNFI EDVLGYTNFA SIPQKMTHLP
1210 1220 1230 1240 1250
ELDTLSSERA RSFITWLRDS RPLSPILHIV KDESPAKAEF FQHLIEDRTE
1260
AAFSYYEFLL HVQQQICK
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. Contains a phosphoserine at position 55.1 Publication
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS75179.1. [O95487-3]
RefSeqiNP_001036199.1. NM_001042734.2. [O95487-2]
NP_001287742.1. NM_001300813.1. [O95487-3]
NP_006314.2. NM_006323.3. [O95487-1]
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]
uc011cfp.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS75179.1. [O95487-3]
RefSeqiNP_001036199.1. NM_001042734.2. [O95487-2]
NP_001287742.1. NM_001300813.1. [O95487-3]
NP_006314.2. NM_006323.3. [O95487-1]
UniGeneiHs.292472.

3D structure databases

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

Protein-protein interaction databases

BioGridi115696. 12 interactions.
IntActiO95487. 10 interactions.
MINTiMINT-6772353.
STRINGi9606.ENSP00000265175.

PTM databases

PhosphoSiteiO95487.

Polymorphism and mutation databases

BioMutaiSEC24B.

Proteomic databases

MaxQBiO95487.
PaxDbiO95487.
PRIDEiO95487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
uc011cfp.2. human.

Organism-specific databases

CTDi10427.
GeneCardsiGC04P110354.
HGNCiHGNC:10704. SEC24B.
HPAiHPA038181.
MIMi607184. gene.
neXtProtiNX_O95487.
PharmGKBiPA35627.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5028.
GeneTreeiENSGT00590000082962.
HOGENOMiHOG000196365.
HOVERGENiHBG054850.
InParanoidiO95487.
KOiK14007.
OMAiNILPMTP.
OrthoDBiEOG7R56RS.
PhylomeDBiO95487.
TreeFamiTF354244.

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.

Miscellaneous databases

ChiTaRSiSEC24B. human.
EvolutionaryTraceiO95487.
GeneWikiiSEC24B.
GenomeRNAii10427.
NextBioi35481162.
PROiO95487.
SOURCEiSearch...

Gene expression databases

BgeeiO95487.
CleanExiHS_SEC24B.
GenevisibleiO95487. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  11. "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-1224, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "CNIH4 interacts with newly synthesized GPCR and controls their export from the endoplasmic reticulum."
    Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y., Simpson J.C., Pepperkok R., Bouvier M.
    Traffic 15:383-400(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNIH4.

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: June 24, 2015
This is version 132 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

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 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.