P40482 (SEC24_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein transport protein SEC24

Alternative name(s):
Abnormal nuclear morphology 1

Gene names

Name:	SEC24
Synonyms:	ANU1
Ordered Locus Names:	YIL109C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	926 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter. Ref.5 Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.27 Ref.28 Ref.31 Ref.32
Subunit structure	The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1. Ref.4 Ref.6 Ref.7 Ref.9 Ref.11 Ref.13 Ref.16 Ref.19 Ref.20 Ref.21 Ref.27 Ref.30 Ref.32 Ref.33 Ref.36
Subcellular location	Cytoplasm. Cytoplasmic vesicle › COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Potential Ref.5 Ref.9 Ref.14 Ref.16 Ref.17 Ref.18 Ref.25 Ref.29.
Sequence similarities	Belongs to the SEC23/SEC24 family. SEC24 subfamily.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cargo loading into COPII-coated vesicle Inferred from direct assay Ref.27Ref.31PubMed 15665868. Source: SGD intracellular protein transport Inferred from electronic annotation. Source: InterPro
Cellular_component	COPII vesicle coat Inferred from direct assay PubMed 8004676. Source: SGD Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	signal sequence binding Inferred from mutant phenotype Ref.27. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRH1	Q04410	3	EBI-16592,EBI-32083
SEC23	P15303	4	EBI-16592,EBI-16584
SEC31	P38968	4	EBI-16592,EBI-20524

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 926

926

Protein transport protein SEC24

PRO_0000205150

Regions

Region

231 – 256

26

Zinc finger-like

Compositional bias

110 – 114

5

Poly-Gln

Compositional bias

157 – 160

4

Poly-Pro

Sites

Metal binding

231

1

Zinc

Metal binding

234

1

Zinc

Metal binding

253

1

Zinc

Metal binding

256

1

Zinc

Amino acid modifications

Modified residue

175

1

Phosphoserine Ref.22

Modified residue

178

1

Phosphoserine Ref.22 Ref.34

Experimental info

Mutagenesis

230

1

R → A: Abolishes binding to and packaging of cargo protein BET1. Ref.27

Mutagenesis

231

1

C → S: Lethal. Ref.4

Mutagenesis

235

1

R → A: Abolishes binding to and packaging of cargo protein BET1. Ref.27

Mutagenesis

559

1

R → M: Abolishes binding to and packaging of cargo protein BET1. Ref.27

Mutagenesis

561

1

R → M: Abolishes binding to and packaging of cargo protein BET1. Ref.27

Mutagenesis

616

1

L → W: Abolishes binding to and packaging of cargo protein BET1. Ref.27

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

926

Helix Strand Turn

Details...

Helix

64 – 72

9

Beta strand

140 – 142

3

Helix

143 – 145

3

Helix

151 – 155

5

Helix

165 – 167

3

Beta strand

168 – 170

3

Helix

173 – 175

3

Turn

179 – 181

3

Beta strand

182 – 192

11

Helix

193 – 199

7

Beta strand

204 – 207

4

Beta strand

212 – 214

3

Turn

232 – 234

3

Beta strand

243 – 245

3

Turn

246 – 249

4

Beta strand

250 – 252

3

Turn

254 – 256

3

Beta strand

259 – 261

3

Helix

264 – 267

4

Helix

277 – 279

3

Helix

281 – 284

4

Beta strand

286 – 291

6

Helix

294 – 296

3

Beta strand

305 – 311

7

Helix

314 – 319

6

Helix

321 – 332

12

Turn

333 – 335

3

Beta strand

344 – 358

15

Helix

362 – 364

3

Beta strand

374 – 376

3

Turn

390 – 392

3

Beta strand

393 – 395

3

Turn

396 – 399

4

Helix

400 – 413

14

Turn

414 – 416

3

Helix

424 – 435

12

Turn

436 – 438

3

Beta strand

440 – 448

9

Helix

471 – 475

5

Helix

482 – 492

11

Beta strand

495 – 505

11

Helix

509 – 517

9

Turn

518 – 520

3

Beta strand

523 – 527

5

Helix

534 – 549

16

Beta strand

554 – 562

9

Beta strand

566 – 576

11

Beta strand

578 – 587

10

Beta strand

594 – 600

7

Beta strand

606 – 618

13

Turn

620 – 622

3

Beta strand

624 – 637

14

Helix

639 – 644

6

Helix

648 – 665

18

Helix

668 – 689

22

Beta strand

696 – 699

4

Beta strand

702 – 704

3

Helix

705 – 707

3

Helix

710 – 718

9

Turn

721 – 723

3

Helix

730 – 742

13

Helix

745 – 752

8

Beta strand

755 – 758

4

Turn

759 – 761

3

Helix

791 – 793

3

Beta strand

799 – 803

5

Beta strand

805 – 812

8

Helix

818 – 825

8

Helix

830 – 832

3

Helix

847 – 860

14

Beta strand

870 – 875

6

Helix

885 – 899

15

Helix

913 – 923

11

Sequences

	Sequence		Length	Mass (Da)
	P40482 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 35E2BDD24CC75899	FASTA	926	103,636
	10 20 30 40 50 60 MSHHKKRVYP QAQLQYGQNA TPLQQPAQFM PPQDPAAAGM SYGQMGMPPQ GAVPSMGQQQ 70 80 90 100 110 120 FLTPAQEQLH QQIDQATTSM NDMHLHNVPL VDPNAYMQPQ VPVQMGTPLQ QQQQPMAAPA 130 140 150 160 170 180 YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP ITDLTLPPPP LVIPPERMLV PSELSNASPD 190 200 210 220 230 240 YIRSTLNAVP KNSSLLKKSK LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP 250 260 270 280 290 300 FVTFIEQGRR WRCNFCRLAN DVPMQMDQSD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ 310 320 330 340 350 360 PPPATYCFLI DVSQSSIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV DNAIHYFKIP 370 380 390 400 410 420 LDSENNEESA DQINMMDIAD LEEPFLPRPN SMVVSLKACR QNIETLLTKI PQIFQSNLIT 430 440 450 460 470 480 NFALGPALKS AYHLIGGVGG KIIVVSGTLP NLGIGKLQRR NESGVVNTSK ETAQLLSCQD 490 500 510 520 530 540 SFYKNFTIDC SKVQITVDLF LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF 550 560 570 580 590 600 STEFAKHISM DFCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV 610 620 630 640 650 660 DESIMADYCY VQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA IASFYNSKAV 670 680 690 700 710 720 EKALNSSLDD ARVLINKSVQ DILATYKKEI VVSNTAGGAP LRLCANLRMF PLLMHSLTKH 730 740 750 760 770 780 MAFRSGIVPS DHRASALNNL ESLPLKYLIK NIYPDVYSLH DMADEAGLPV QTEDGEATGT 790 800 810 820 830 840 IVLPQPINAT SSLFERYGLY LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI 850 860 870 880 890 900 PVVENSEFNQ RVRNIINQLR NHDDVITYQS LYIVRGASLS EPVNHASARE VATLRLWASS 910 920 TLVEDKILNN ESYREFLQIM KARISK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles." Peng R., Grabowski R., De Antoni A., Gallwitz D. Proc. Natl. Acad. Sci. U.S.A. 96:3751-3756(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 731-740 AND 774-793, INTERACTION WITH SED5, MUTAGENESIS OF CYS-231.
[5]	"COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast." Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R.W., Orci L. Cell 83:1183-1196(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p." Gimeno R.E., Espenshade P.J., Kaiser C.A. Mol. Biol. Cell 7:1815-1823(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEC16.
[7]	"COPII subunit interactions in the assembly of the vesicle coat." Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A. J. Biol. Chem. 272:25413-25416(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE COPII COAT, INTERACTION WITH SEC16.
[8]	"Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles." Campbell J.L., Schekman R.W. Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes." Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R.W., Yeung T. Cell 93:263-275(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[10]	"COPII-cargo interactions direct protein sorting into ER-derived transport vesicles." Kuehn M.J., Herrmann J.M., Schekman R.W. Nature 391:187-190(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
[11]	"Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs." Springer S., Schekman R.W. Science 281:698-700(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BET1; BOS1; SAR1 AND SEC23.
[12]	"Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter." Penalver E., Lucero P., Moreno E., Lagunas R. J. Bacteriol. 181:2555-2563(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
[13]	"Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles." Gilstring C.F., Melin-Larsson M., Ljungdahl P.O. Mol. Biol. Cell 10:3549-3565(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHR3.
[14]	"Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members." Peng R., De Antoni A., Gallwitz D. J. Biol. Chem. 275:11521-11528(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum." Higashio H., Kimata Y., Kiriyama T., Hirata A., Kohno K. J. Biol. Chem. 275:17900-17908(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae." Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L., Schekman R.W. J. Cell Biol. 151:973-984(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PMA1.
[17]	"The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting." Matsuoka K., Schekman R.W. Methods 20:417-428(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]	"Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae." Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W., Yoshihisa T. Mol. Biol. Cell 11:983-998(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]	"An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export." Votsmeier C., Gallwitz D. EMBO J. 20:6742-6750(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYS1.
[20]	"Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex." Belden W.J., Barlowe C. J. Biol. Chem. 276:43040-43048(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EMP24 AND ERV25.
[21]	"Dynamics of the COPII coat with GTP and stable analogues." Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W. Nat. Cell Biol. 3:531-537(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE COPII COAT.
[22]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-178, MASS SPECTROMETRY.
[23]	"Structure of the Sec23p/24p and Sec13p/31p complexes of COPII." Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S., Schekman R.W., Walz T., Kirchhausen T. Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
[24]	"Surface structure of the COPII-coated vesicle." Matsuoka K., Schekman R.W., Orci L., Heuser J.E. Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
[25]	"Sec16p potentiates the action of COPII proteins to bud transport vesicles." Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W. J. Cell Biol. 158:1029-1038(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[26]	"Self-assembly of minimal COPII cages." Antonny B., Gounon P., Schekman R.W., Orci L. EMBO Rep. 4:419-424(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF THE COPII COMPLEX.
[27]	"Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles." Miller E.A., Beilharz T.H., Malkus P.N., Lee M.C.S., Hamamoto S., Orci L., Schekman R.W. Cell 114:497-509(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BET1 AND SYS1, MUTAGENESIS OF ARG-230; ARG-235; ARG-559; ARG-561 AND LEU-616.
[28]	"The early secretory pathway contributes to autophagy in yeast." Hamasaki M., Noda T., Ohsumi Y. Cell Struct. Funct. 28:49-54(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[29]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[30]	"Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23." Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C. Nat. Cell Biol. 5:661-667(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEC23.
[31]	"Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting." Sato K., Nakano A. J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract] Cited for: COPII COMPLEX ASSEMBLY, FUNCTION OF THE COPII COMPLEX.
[32]	"Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile." Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A., Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S., Krogan N.J. Cell 123:507-519(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GRH1.
[33]	"The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic." Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S. J. Cell Biol. 176:255-261(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GHR1.
[34]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, MASS SPECTROMETRY. Strain: ADR376.
[35]	"Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat." Bi X., Corpina R.A., Goldberg J. Nature 419:271-277(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SEC23 AND ZINC.
[36]	"SNARE selectivity of the COPII coat." Mossessova E., Bickford L.C., Goldberg J. Cell 114:483-495(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 117-926 IN COMPLEX WITH SED5; SYS1; BET1 AND ZINC, INTERACTION WITH SEC22.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z38125 Genomic DNA. Translation: CAA86271.1.
AY692888 Genomic DNA. Translation: AAT92907.1.
BK006942 Genomic DNA. Translation: DAA08444.1.

PIR

S48463.

RefSeq

NP_012157.3. NM_001179457.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M2V	X-ray	2.75	B	1-926	[»]
1PCX	X-ray	2.50	A	117-926	[»]
1PD0	X-ray	2.60	A	117-926	[»]
1PD1	X-ray	2.60	A	117-926	[»]

ProteinModelPortal

P40482.

SMR

P40482. Positions 133-926.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2233N.

IntAct

P40482. 22 interactions.

MINT

MINT-476513.

STRING

4932.YIL109C.

Proteomic databases

PaxDb

P40482.

PeptideAtlas

P40482.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL109C; YIL109C; YIL109C.

GeneID

854697.

KEGG

sce:YIL109C.

Organism-specific databases

CYGD

YIL109c.

SGD

S000001371. SEC24.

Phylogenomic databases

eggNOG

COG5028.

GeneTree

ENSGT00590000082962.

HOGENOM

HOG000196365.

KO

K14007.

OMA

NNEESAD.

OrthoDB

EOG47Q1F9.

Enzyme and pathway databases

BioCyc

YEAST:G3O-31364-MONOMER.

Gene expression databases

Genevestigator

P40482.

GermOnline

YIL109C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.50.410. 1 hit.

InterPro

IPR007123. Gelsolin_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]

Pfam

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]

SUPFAM

SSF81811. Sec23_helical. 1 hit.
SSF82919. Znf_Sec23_Sec24. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P40482.

NextBio

977337.

Entry information

Entry name

SEC24_YEAST

Accession

Primary (citable) accession number: P40482
Secondary accession number(s): D6VVH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program