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O95487

- SC24B_HUMAN

UniProt

O95487 - SC24B_HUMAN

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Protein
Protein transport protein Sec24B
Gene
SEC24B
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

GO - Biological processi

  1. COPII vesicle coating Source: Reactome
  2. ER to Golgi vesicle-mediated transport Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. cellular protein metabolic process 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
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: Chromosome 4

Organism-specific databases

HGNCiHGNC:10704. SEC24B.

Subcellular locationi

GO - Cellular componenti

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

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 Sec24B
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiO95487.

Family & Domainsi

Region

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

Compositional bias

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

Sequence similaritiesi

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.

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.
VSP_054432
Alternative sequencei354 – 38835Missing in isoform 2.
VSP_035987Add
BLAST
Alternative sequencei496 – 4961Missing in isoform 3.
VSP_054433

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231A → S in CAA10335. 1 Publication

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.
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 .
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

« 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].

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: September 3, 2014
This is version 123 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