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Protein

Protein transport protein Sec24C

Gene

SEC24C

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.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein Sec24C
Alternative name(s):
SEC24-related protein C
Gene namesi
Name:SEC24C
Synonyms:KIAA0079
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:10705. SEC24C.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35628.

Polymorphism and mutation databases

BioMutaiSEC24C.
DMDMi257051070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10941094Protein transport protein Sec24CPRO_0000205156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei214 – 2141PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP53992.
MaxQBiP53992.
PaxDbiP53992.
PRIDEiP53992.

PTM databases

iPTMnetiP53992.
PhosphoSiteiP53992.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP53992.
CleanExiHS_SEC24C.
ExpressionAtlasiP53992. baseline and differential.
GenevisibleiP53992. HS.

Organism-specific databases

HPAiHPA040196.
HPA040213.

Interactioni

Subunit structurei

Interacts with SLC6A4 (By similarity). COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1. SEC24C is capable of forming heterodimers with SEC24A. Interacts with TMED2 and TMED10.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MOSP005403EBI-81134,EBI-1757866
SEC23AQ154365EBI-81134,EBI-81088
WIPF1O435163EBI-81134,EBI-346356

Protein-protein interaction databases

BioGridi114991. 67 interactions.
DIPiDIP-30981N.
IntActiP53992. 34 interactions.
MINTiMINT-4998997.
STRINGi9606.ENSP00000321845.

Structurei

Secondary structure

1
1094
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi331 – 34010Combined sources
Beta strandi343 – 3464Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi366 – 3683Combined sources
Turni371 – 3733Combined sources
Beta strandi374 – 38411Combined sources
Helixi385 – 3917Combined sources
Beta strandi395 – 3995Combined sources
Beta strandi413 – 4153Combined sources
Helixi418 – 4203Combined sources
Turni426 – 4283Combined sources
Beta strandi437 – 4393Combined sources
Helixi440 – 4423Combined sources
Beta strandi444 – 4463Combined sources
Turni448 – 4503Combined sources
Beta strandi453 – 4553Combined sources
Turni458 – 4614Combined sources
Helixi462 – 4665Combined sources
Beta strandi467 – 4693Combined sources
Helixi477 – 4804Combined sources
Beta strandi482 – 4876Combined sources
Helixi490 – 4923Combined sources
Helixi494 – 4963Combined sources
Beta strandi503 – 5097Combined sources
Helixi512 – 5165Combined sources
Helixi519 – 53012Combined sources
Helixi531 – 5333Combined sources
Beta strandi546 – 56015Combined sources
Beta strandi569 – 5735Combined sources
Turni576 – 5783Combined sources
Beta strandi587 – 5893Combined sources
Turni591 – 5944Combined sources
Helixi595 – 60915Combined sources
Helixi620 – 63213Combined sources
Beta strandi637 – 6437Combined sources
Beta strandi649 – 6513Combined sources
Helixi661 – 6633Combined sources
Helixi669 – 6724Combined sources
Helixi679 – 68911Combined sources
Beta strandi692 – 6987Combined sources
Helixi706 – 7094Combined sources
Helixi711 – 7155Combined sources
Beta strandi720 – 7223Combined sources
Helixi728 – 74417Combined sources
Beta strandi747 – 75711Combined sources
Beta strandi761 – 7699Combined sources
Beta strandi773 – 7764Combined sources
Beta strandi778 – 7847Combined sources
Beta strandi789 – 7979Combined sources
Turni801 – 8033Combined sources
Beta strandi805 – 81410Combined sources
Beta strandi820 – 83415Combined sources
Helixi835 – 8406Combined sources
Helixi844 – 85815Combined sources
Turni859 – 8613Combined sources
Helixi864 – 88522Combined sources
Helixi899 – 9013Combined sources
Helixi904 – 9129Combined sources
Turni915 – 9173Combined sources
Helixi925 – 93713Combined sources
Helixi940 – 9478Combined sources
Beta strandi950 – 9534Combined sources
Helixi972 – 9743Combined sources
Beta strandi980 – 9845Combined sources
Beta strandi986 – 9938Combined sources
Helixi999 – 10068Combined sources
Helixi1011 – 10133Combined sources
Helixi1027 – 104014Combined sources
Beta strandi1043 – 10453Combined sources
Beta strandi1048 – 10569Combined sources
Helixi1059 – 10635Combined sources
Turni1072 – 10743Combined sources
Helixi1078 – 109215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EH2X-ray2.35A/B/C329-1094[»]
ProteinModelPortaliP53992.
SMRiP53992. Positions 329-1094.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53992.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 45026Zinc finger-likeAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1985. Eukaryota.
COG5028. LUCA.
GeneTreeiENSGT00590000082962.
HOGENOMiHOG000196365.
HOVERGENiHBG062229.
InParanoidiP53992.
KOiK14007.
OMAiVYKYASF.
PhylomeDBiP53992.
TreeFamiTF300464.

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.
SSF82754. SSF82754. 1 hit.
SSF82919. SSF82919. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P53992-1) [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
MNVNQSVPPV PPFGQPQPIY PGYHQSSYGG QSGSTAPAIP YGAYNGPVPG
60 70 80 90 100
YQQTPPQGMS RAPPSSGAPP ASTAQAPCGQ AAYGQFGQGD VQNGPSSTVQ
110 120 130 140 150
MQRLPGSQPF GSPLAPVGNQ PPVLQPYGPP PTSAQVATQL SGMQISGAVA
160 170 180 190 200
PAPPSSGLGF GPPTSLASAS GSFPNSGLYG SYPQGQAPPL SQAQGHPGIQ
210 220 230 240 250
TPQRSAPSQA SSFTPPASGG PRLPSMTGPL LPGQSFGGPS VSQPNHVSSP
260 270 280 290 300
PQALPPGTQM TGPLGPLPPM HSPQQPGYQP QQNGSFGPAR GPQSNYGGPY
310 320 330 340 350
PAAPTFGSQP GPPQPLPPKR LDPDAIPSPI QVIEDDRNNR GTEPFVTGVR
360 370 380 390 400
GQVPPLVTTN FLVKDQGNAS PRYIRCTSYN IPCTSDMAKQ AQVPLAAVIK
410 420 430 440 450
PLARLPPEEA SPYVVDHGES GPLRCNRCKA YMCPFMQFIE GGRRFQCCFC
460 470 480 490 500
SCINDVPPQY FQHLDHTGKR VDAYDRPELS LGSYEFLATV DYCKNNKFPS
510 520 530 540 550
PPAFIFMIDV SYNAIRTGLV RLLCEELKSL LDFLPREGGA EESAIRVGFV
560 570 580 590 600
TYNKVLHFYN VKSSLAQPQM MVVSDVADMF VPLLDGFLVN VNESRAVITS
610 620 630 640 650
LLDQIPEMFA DTRETETVFV PVIQAGMEAL KAAECAGKLF LFHTSLPIAE
660 670 680 690 700
APGKLKNRDD RKLINTDKEK TLFQPQTGAY QTLAKECVAQ GCCVDLFLFP
710 720 730 740 750
NQYVDVATLS VVPQLTGGSV YKYASFQVEN DQERFLSDLR RDVQKVVGFD
760 770 780 790 800
AVMRVRTSTG IRAVDFFGAF YMSNTTDVEL AGLDGDKTVT VEFKHDDRLN
810 820 830 840 850
EESGALLQCA LLYTSCAGQR RLRIHNLALN CCTQLADLYR NCETDTLINY
860 870 880 890 900
MAKFAYRGVL NSPVKAVRDT LITQCAQILA CYRKNCASPS SAGQLILPEC
910 920 930 940 950
MKLLPVYLNC VLKSDVLQPG AEVTTDDRAY VRQLVTSMDV TETNVFFYPR
960 970 980 990 1000
LLPLTKSPVE STTEPPAVRA SEERLSNGDI YLLENGLNLF LWVGASVQQG
1010 1020 1030 1040 1050
VVQSLFSVSS FSQITSGLSV LPVLDNPLSK KVRGLIDSLR AQRSRYMKLT
1060 1070 1080 1090
VVKQEDKMEM LFKHFLVEDK SLSGGASYVD FLCHMHKEIR QLLS
Length:1,094
Mass (Da):118,325
Last modified:September 1, 2009 - v3
Checksum:i5E308E4B8E596ECE
GO
Isoform 2 (identifier: P53992-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-752: Missing.

Note: No experimental confirmation available.
Show »
Length:342
Mass (Da):38,181
Checksum:i9FE10EE8578DBE79
GO

Sequence cautioni

The sequence BAA07558.2 differs from that shown. Reason: Frameshift at position 1041. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091P → S.1 Publication
Corresponds to variant rs17851695 [ dbSNP | Ensembl ].
VAR_058690
Natural varianti934 – 9341L → P.
Corresponds to variant rs16930872 [ dbSNP | Ensembl ].
VAR_057174

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 752752Missing in isoform 2. 1 PublicationVSP_056516Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38555 mRNA. Translation: BAA07558.2. Sequence problems.
AK303085 mRNA. Translation: BAG64196.1.
AC022400 Genomic DNA. No translation available.
BC018928 mRNA. Translation: AAH18928.1.
CCDSiCCDS7332.1. [P53992-1]
RefSeqiNP_004913.2. NM_004922.3. [P53992-1]
NP_940999.1. NM_198597.2. [P53992-1]
UniGeneiHs.81964.

Genome annotation databases

EnsembliENST00000339365; ENSP00000343405; ENSG00000176986. [P53992-1]
ENST00000345254; ENSP00000321845; ENSG00000176986. [P53992-1]
GeneIDi9632.
KEGGihsa:9632.
UCSCiuc001juw.4. human. [P53992-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38555 mRNA. Translation: BAA07558.2. Sequence problems.
AK303085 mRNA. Translation: BAG64196.1.
AC022400 Genomic DNA. No translation available.
BC018928 mRNA. Translation: AAH18928.1.
CCDSiCCDS7332.1. [P53992-1]
RefSeqiNP_004913.2. NM_004922.3. [P53992-1]
NP_940999.1. NM_198597.2. [P53992-1]
UniGeneiHs.81964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EH2X-ray2.35A/B/C329-1094[»]
ProteinModelPortaliP53992.
SMRiP53992. Positions 329-1094.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114991. 67 interactions.
DIPiDIP-30981N.
IntActiP53992. 34 interactions.
MINTiMINT-4998997.
STRINGi9606.ENSP00000321845.

PTM databases

iPTMnetiP53992.
PhosphoSiteiP53992.

Polymorphism and mutation databases

BioMutaiSEC24C.
DMDMi257051070.

Proteomic databases

EPDiP53992.
MaxQBiP53992.
PaxDbiP53992.
PRIDEiP53992.

Protocols and materials databases

DNASUi9632.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339365; ENSP00000343405; ENSG00000176986. [P53992-1]
ENST00000345254; ENSP00000321845; ENSG00000176986. [P53992-1]
GeneIDi9632.
KEGGihsa:9632.
UCSCiuc001juw.4. human. [P53992-1]

Organism-specific databases

CTDi9632.
GeneCardsiSEC24C.
H-InvDBHIX0008930.
HGNCiHGNC:10705. SEC24C.
HPAiHPA040196.
HPA040213.
MIMi607185. gene.
neXtProtiNX_P53992.
PharmGKBiPA35628.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1985. Eukaryota.
COG5028. LUCA.
GeneTreeiENSGT00590000082962.
HOGENOMiHOG000196365.
HOVERGENiHBG062229.
InParanoidiP53992.
KOiK14007.
OMAiVYKYASF.
PhylomeDBiP53992.
TreeFamiTF300464.

Enzyme and pathway databases

ReactomeiR-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiSEC24C. human.
EvolutionaryTraceiP53992.
GeneWikiiSEC24C.
GenomeRNAii9632.
PROiP53992.
SOURCEiSearch...

Gene expression databases

BgeeiP53992.
CleanExiHS_SEC24C.
ExpressionAtlasiP53992. baseline and differential.
GenevisibleiP53992. 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.
SSF82754. SSF82754. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "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] (ISOFORM 2).
    Tissue: Thymus.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1), VARIANT SER-109.
    Tissue: Muscle.
  5. "Hypothetical protein KIAA0079 is a mammalian homologue of yeast Sec24p."
    Tani K., Oyama Y., Hatsuzawa K., Tagaya M.
    FEBS Lett. 447:247-250(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSC24C_HUMAN
AccessioniPrimary (citable) accession number: P53992
Secondary accession number(s): B4DZT4, Q8WV25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 1, 2009
Last modified: June 8, 2016
This is version 161 of the entry and version 3 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 10
    Human chromosome 10: 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

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.