SEC31A

Functionⁱ

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 (By similarity).By similarity1 Publication

GO - Molecular functionⁱ

calcium-dependent protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16957052
- 17196169

GO - Biological processⁱ

antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
COPII vesicle coating Source: Reactome
ER to Golgi vesicle-mediated transport
Source: UniProtKB
Non-traceable author statementⁱ
- 10788476
IRE1-mediated unfolded protein response Source: Reactome
protein transport Source: UniProtKB-KW
response to calcium ion
Source: UniProtKB
Inferred from direct assayⁱ
- 17196169

Complete GO annotation...

Keywords - Biological processⁱ

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

Reactomeⁱ	R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport. R-HSA-2132295. MHC class II antigen presentation. R-HSA-381038. XBP1(S) activates chaperone genes. R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLinkⁱ	O94979.

Protein family/group databases

TCDBⁱ	3.A.5.9.1. the general secretory pathway (sec) family.

TCDBⁱ

3.A.5.9.1. the general secretory pathway (sec) family.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein transport protein Sec31A Alternative name(s): ABP125 ABP130 SEC31-like protein 1 SEC31-related protein A Web1-like protein
Gene namesⁱ	Name:SEC31A Synonyms:KIAA0905, SEC31L1 ORF Names:HSPC275, HSPC334
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

HGNCⁱ	HGNC:17052. SEC31A.

HGNCⁱ

HGNC:17052. SEC31A.

Subcellular locationⁱ

Cytoplasm By similarity
Cytoplasmic vesicle › COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side
Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity

Note:

Associates with membranes in a GTP-dependent manner.By similarity

GO - Cellular componentⁱ

COPII vesicle coat
Source: UniProtKB
Non-traceable author statementⁱ
- 10788476
cytoplasm
Source: UniProtKB
Inferred from direct assayⁱ
- 17196169
cytosol Source: Reactome
endoplasmic reticulum
Source: UniProtKB
Inferred from direct assayⁱ
- 17196169
endoplasmic reticulum exit site
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16957052
endoplasmic reticulum membrane Source: Reactome
ER to Golgi transport vesicle
Source: UniProtKB
Inferred from direct assayⁱ
- 22358839
ER to Golgi transport vesicle membrane Source: Reactome
Golgi membrane Source: GOC
intracellular membrane-bounded organelle Source: HPA
perinuclear region of cytoplasm
Source: UniProtKB
Inferred from direct assayⁱ
- 17196169
- 19401338
vesicle coat
Source: MGI
Inferred from direct assayⁱ
- 22792322

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

A chromosomal aberration involving SEC31A is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;4)(p23;q21) with ALK.

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Mutagenesisⁱ	647 – 647	1	K → R: Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-1217. 1 Publication Manual assertion based on experiment inⁱ Ref.22 "Ubiquitin-dependent regulation of COPII coat size and function." Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M. Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS OF LYS-647 AND LYS-1217, INTERACTION WITH KLHL12.
Mutagenesisⁱ	1217 – 1217	1	K → R: Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-647. 1 Publication Manual assertion based on experiment inⁱ Ref.22 "Ubiquitin-dependent regulation of COPII coat size and function." Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M. Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS OF LYS-647 AND LYS-1217, INTERACTION WITH KLHL12.

Keywords - Diseaseⁱ

Proto-oncogene

Organism-specific databases

PharmGKBⁱ	PA162402737.

PharmGKBⁱ

PA162402737.

Polymorphism and mutation databases

BioMutaⁱ	SEC31A.

BioMutaⁱ

SEC31A.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 1220	1220	Protein transport protein Sec31A		PRO_0000295147	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	527 – 527	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.13 "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-527 AND SER-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.21 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799; THR-1161 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.25 "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-527; SER-799 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	532 – 532	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.13 "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-527 AND SER-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	647 – 647		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment inⁱ Ref.22 "Ubiquitin-dependent regulation of COPII coat size and function." Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M. Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS OF LYS-647 AND LYS-1217, INTERACTION WITH KLHL12.
Modified residueⁱ	799 – 799	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.17 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.19 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND THR-1161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.21 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799; THR-1161 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.25 "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-527; SER-799 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1161 – 1161	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.19 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND THR-1161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799; THR-1161 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1163 – 1163	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.17 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799; THR-1161 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.25 "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-527; SER-799 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	1217 – 1217		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment inⁱ Ref.22 "Ubiquitin-dependent regulation of COPII coat size and function." Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M. Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS OF LYS-647 AND LYS-1217, INTERACTION WITH KLHL12.

Post-translational modificationⁱ

Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, leading to regulate the size of COPII coats.1 Publication

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	O94979.
MaxQBⁱ	O94979.
PaxDbⁱ	O94979.
PeptideAtlasⁱ	O94979.
PRIDEⁱ	O94979.

PTM databases

iPTMnetⁱ	O94979.
PhosphoSiteⁱ	O94979.
SwissPalmⁱ	O94979.

Expressionⁱ

Tissue specificityⁱ

Abundantly and ubiquitously expressed.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000138674.
ExpressionAtlasⁱ	O94979. baseline and differential.
Genevisibleⁱ	O94979. HS.

Organism-specific databases

HPAⁱ	HPA005457.

Interactionⁱ

Subunit structureⁱ

COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity). Interacts with PDCD6 in a calcium-dependent manner. Interacts with KLHL12.By similarity3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
PDCD6	O75340	6	EBI-1767898,EBI-352915
REL	Q04864	3	EBI-1767898,EBI-307352

With

Entry

#Exp.

IntAct

Notes

PDCD6

O75340

6

EBI-1767898,EBI-352915

REL

Q04864

3

EBI-1767898,EBI-307352

GO - Molecular functionⁱ

calcium-dependent protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16957052
- 17196169

Protein-protein interaction databases

BioGridⁱ	116539. 51 interactions.
DIPⁱ	DIP-40438N.
IntActⁱ	O94979. 35 interactions.
MINTⁱ	MINT-3002555.
STRINGⁱ	9606.ENSP00000347329.

Structureⁱ

Secondary structure

1

1220

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Beta strandⁱ	841 – 843	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3WXA

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3WXA	X-ray	2.36	C/D	837-848	[»]

ProteinModelPortalⁱ

O94979.

SMRⁱ

O94979. Positions 4-770.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Actions
Repeatⁱ	4 – 47	44	WD 1	Add BLAST
Repeatⁱ	68 – 111	44	WD 2	Add BLAST
Repeatⁱ	120 – 160	41	WD 3	Add BLAST
Repeatⁱ	166 – 206	41	WD 4	Add BLAST
Repeatⁱ	209 – 254	46	WD 5	Add BLAST
Repeatⁱ	258 – 298	41	WD 6	Add BLAST
Repeatⁱ	301 – 342	42	WD 7	Add BLAST
Repeatⁱ	397 – 430	34	WD 8; interaction with SEC13PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00221	Add BLAST

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	161 – 471	311	Interaction with SEC13			Add BLAST
Regionⁱ	800 – 1113	314	Interaction with PDCD6			Add BLAST

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Compositional biasⁱ	800 – 1091	292	Pro-rich			Add BLAST

Sequence similaritiesⁱ

Belongs to the WD repeat SEC31 family.Curated

Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat, WD repeat

Phylogenomic databases

eggNOGⁱ	KOG0307. Eukaryota. ENOG410XQ1D. LUCA.
GeneTreeⁱ	ENSGT00390000003175.
HOGENOMⁱ	HOG000230582.
HOVERGENⁱ	HBG055626.
InParanoidⁱ	O94979.
KOⁱ	K14005.
PhylomeDBⁱ	O94979.
TreeFamⁱ	TF313842.

Family and domain databases

Gene3Dⁱ	2.130.10.10. 1 hit.
InterProⁱ	IPR024298. ACE1_Sec16_Sec31. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR017986. WD40_repeat_dom. [Graphical view]
Pfamⁱ	PF12931. Sec16_C. 1 hit. [Graphical view]
SMARTⁱ	SM00320. WD40. 6 hits. [Graphical view]
SUPFAMⁱ	SSF50978. SSF50978. 1 hit.
PROSITEⁱ	PS50082. WD_REPEATS_2. 1 hit. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]

Sequences (10)ⁱ

Sequence statusⁱ: Complete.

This entry describes 10 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Sequence cautionⁱ

The sequence AAF28953 differs from that shown. Reason: Frameshift at positions 857 and 1079. Curated

The sequence AAF29012 differs from that shown. Reason: Frameshift at positions 922, 946, 1029 and 1080. Curated

The sequence CAI45995 differs from that shown. Reason: Erroneous termination at position 221. Translated as Trp.Curated

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	200 – 200	1	K → E in BAA84923 (Ref. 2) Curated
Sequence conflictⁱ	284 – 284	1	K → R in BAC86336 (PubMed:14702039).Curated
Sequence conflictⁱ	854 – 854	1	A → S in BAA84923 (Ref. 2) Curated
Sequence conflictⁱ	854 – 854	1	A → S in BAA84924 (Ref. 2) Curated
Sequence conflictⁱ	1007 – 1007	1	K → R in BAG58628 (PubMed:14702039).Curated

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	263 – 263	1	I → V. Corresponds to variant rs34554214 [ dbSNP \| Ensembl ].	VAR_033225
Natural variantⁱ	456 – 456	1	N → K. Corresponds to variant rs3797036 [ dbSNP \| Ensembl ].	VAR_053414
Natural variantⁱ	841 – 841	1	P → L. Corresponds to variant rs35579207 [ dbSNP \| Ensembl ].	VAR_033226
Natural variantⁱ	1055 – 1055	1	P → T. Corresponds to variant rs35739017 [ dbSNP \| Ensembl ].	VAR_033227

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	1 – 228	228	Missing in isoform 7. 1 Publication Manual assertion based on opinion inⁱ Ref.5 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).	VSP_026742	Add BLAST
Alternative sequenceⁱ	1 – 26	26	MKLKE…IYLAT → MLGESDERCTNAGSGCRRSS P in isoform 9. 1 Publication Manual assertion based on opinion inⁱ Ref.5 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).	VSP_044602	Add BLAST
Alternative sequenceⁱ	229 – 260	32	MVLAS…LENHA → MVKLVLLSIVLLKVTVPKLS NYLLQLDFMPIH in isoform 7. 1 Publication Manual assertion based on opinion inⁱ Ref.5 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).	VSP_026743	Add BLAST
Alternative sequenceⁱ	504 – 542	39	Missing in isoform 4, isoform 6, isoform 7 and isoform 10. 4 Publications Manual assertion based on opinion inⁱ Ref.2 "The yeast web1-like human protein that has WD repeat domain." Noguchi J., Shibata M. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). Ref.5 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9). Ref.6 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Ref.9 "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 2; 3; 5 AND 10).	VSP_026744	Add BLAST
Alternative sequenceⁱ	504 – 509	6	IALALN → VNFWES in isoform 5. 1 Publication Manual assertion based on opinion inⁱ Ref.9 "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 2; 3; 5 AND 10).	VSP_026745
Alternative sequenceⁱ	510 – 1220	711	Missing in isoform 5. 1 Publication Manual assertion based on opinion inⁱ Ref.9 "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 2; 3; 5 AND 10).	VSP_026746	Add BLAST
Alternative sequenceⁱ	834 – 834	1	H → HVRIAPTVTTWSNKTPTALP SHPPAASPSDTQ in isoform 7. 1 Publication Manual assertion based on opinion inⁱ Ref.5 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).	VSP_026747
Alternative sequenceⁱ	876 – 876	1	P → R in isoform 3 and isoform 6. 2 Publications Manual assertion based on opinion inⁱ Ref.6 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Ref.9 "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 2; 3; 5 AND 10).	VSP_026748
Alternative sequenceⁱ	877 – 990	114	Missing in isoform 3 and isoform 6. 2 Publications Manual assertion based on opinion inⁱ Ref.6 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Ref.9 "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 2; 3; 5 AND 10).	VSP_026749	Add BLAST
Alternative sequenceⁱ	974 – 988	15	Missing in isoform 2, isoform 7, isoform 9 and isoform 10. 2 Publications Manual assertion based on opinion inⁱ Ref.5 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9). Ref.9 "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 2; 3; 5 AND 10).	VSP_026750	Add BLAST
Alternative sequenceⁱ	989 – 989	1	T → TENQSIQDQAPMLE in isoform 8. 1 Publication Manual assertion based on opinion inⁱ Ref.11 "Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 852-1220 (ISOFORM 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 899-1220 (ISOFORM 1).	VSP_026751

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF139184 mRNA. Translation: AAF67836.1. AB018358 mRNA. Translation: BAA84923.1. AB018359 mRNA. Translation: BAA84924.1. AB020712 mRNA. Translation: BAA74928.2. AK125897 mRNA. Translation: BAC86336.1. AK295810 mRNA. Translation: BAG58628.1. AL049463 mRNA. Translation: CAH56418.1. CR933696 mRNA. Translation: CAI45995.1. Sequence problems. AC021105 Genomic DNA. No translation available. AC108469 Genomic DNA. No translation available. CH471057 Genomic DNA. Translation: EAX05908.1. BC047883 mRNA. Translation: AAH47883.1. BC084583 mRNA. Translation: AAH84583.1. BC117221 mRNA. Translation: AAI17222.1. BC143489 mRNA. Translation: AAI43490.1. BC143491 mRNA. Translation: AAI43492.1. BC143492 mRNA. Translation: AAI43493.1. AY137583 mRNA. Translation: AAN15221.1. AF161393 mRNA. Translation: AAF28953.1. Frameshift. AF161452 mRNA. Translation: AAF29012.1. Frameshift.
CCDSⁱ	CCDS3596.1. [O94979-1] CCDS3597.1. [O94979-4] CCDS43244.1. [O94979-3] CCDS47088.1. [O94979-2] CCDS54773.1. [O94979-9] CCDS75155.1. [O94979-6] CCDS75156.1. [O94979-10]
RefSeqⁱ	NP_001070674.1. NM_001077206.3. [O94979-3] NP_001070675.1. NM_001077207.3. [O94979-1] NP_001070676.1. NM_001077208.3. [O94979-2] NP_001177978.1. NM_001191049.2. [O94979-9] NP_001287673.1. NM_001300744.2. [O94979-6] NP_001287674.1. NM_001300745.2. [O94979-10] NP_001305048.1. NM_001318119.1. [O94979-2] NP_001305049.1. NM_001318120.1. [O94979-1] NP_057295.2. NM_016211.4. [O94979-4]
UniGeneⁱ	Hs.370024. Hs.617723. Hs.728916.

Genome annotation databases

Ensemblⁱ	ENST00000311785; ENSP00000309070; ENSG00000138674. [O94979-3] ENST00000348405; ENSP00000337602; ENSG00000138674. [O94979-4] ENST00000355196; ENSP00000347329; ENSG00000138674. [O94979-1] ENST00000395310; ENSP00000378721; ENSG00000138674. [O94979-1] ENST00000443462; ENSP00000408027; ENSG00000138674. [O94979-9] ENST00000448323; ENSP00000400926; ENSG00000138674. [O94979-1] ENST00000500777; ENSP00000421464; ENSG00000138674. [O94979-6] ENST00000505984; ENSP00000424451; ENSG00000138674. [O94979-10] ENST00000508502; ENSP00000424635; ENSG00000138674. [O94979-2] ENST00000509142; ENSP00000426569; ENSG00000138674. [O94979-3] ENST00000513858; ENSP00000426886; ENSG00000138674. [O94979-6]
GeneIDⁱ	22872.
KEGGⁱ	hsa:22872.
UCSCⁱ	uc003hnf.3. human. [O94979-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF139184 mRNA. Translation: AAF67836.1. AB018358 mRNA. Translation: BAA84923.1. AB018359 mRNA. Translation: BAA84924.1. AB020712 mRNA. Translation: BAA74928.2. AK125897 mRNA. Translation: BAC86336.1. AK295810 mRNA. Translation: BAG58628.1. AL049463 mRNA. Translation: CAH56418.1. CR933696 mRNA. Translation: CAI45995.1. Sequence problems. AC021105 Genomic DNA. No translation available. AC108469 Genomic DNA. No translation available. CH471057 Genomic DNA. Translation: EAX05908.1. BC047883 mRNA. Translation: AAH47883.1. BC084583 mRNA. Translation: AAH84583.1. BC117221 mRNA. Translation: AAI17222.1. BC143489 mRNA. Translation: AAI43490.1. BC143491 mRNA. Translation: AAI43492.1. BC143492 mRNA. Translation: AAI43493.1. AY137583 mRNA. Translation: AAN15221.1. AF161393 mRNA. Translation: AAF28953.1. Frameshift. AF161452 mRNA. Translation: AAF29012.1. Frameshift.
CCDSⁱ	CCDS3596.1. [O94979-1] CCDS3597.1. [O94979-4] CCDS43244.1. [O94979-3] CCDS47088.1. [O94979-2] CCDS54773.1. [O94979-9] CCDS75155.1. [O94979-6] CCDS75156.1. [O94979-10]
RefSeqⁱ	NP_001070674.1. NM_001077206.3. [O94979-3] NP_001070675.1. NM_001077207.3. [O94979-1] NP_001070676.1. NM_001077208.3. [O94979-2] NP_001177978.1. NM_001191049.2. [O94979-9] NP_001287673.1. NM_001300744.2. [O94979-6] NP_001287674.1. NM_001300745.2. [O94979-10] NP_001305048.1. NM_001318119.1. [O94979-2] NP_001305049.1. NM_001318120.1. [O94979-1] NP_057295.2. NM_016211.4. [O94979-4]
UniGeneⁱ	Hs.370024. Hs.617723. Hs.728916.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3WXA	X-ray	2.36	C/D	837-848	[»]

ProteinModelPortalⁱ

O94979.

SMRⁱ

O94979. Positions 4-770.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	116539. 51 interactions.
DIPⁱ	DIP-40438N.
IntActⁱ	O94979. 35 interactions.
MINTⁱ	MINT-3002555.
STRINGⁱ	9606.ENSP00000347329.

Protein family/group databases

TCDBⁱ	3.A.5.9.1. the general secretory pathway (sec) family.

TCDBⁱ

3.A.5.9.1. the general secretory pathway (sec) family.

PTM databases

iPTMnetⁱ	O94979.
PhosphoSiteⁱ	O94979.
SwissPalmⁱ	O94979.

Polymorphism and mutation databases

BioMutaⁱ	SEC31A.

BioMutaⁱ

SEC31A.

Proteomic databases

EPDⁱ	O94979.
MaxQBⁱ	O94979.
PaxDbⁱ	O94979.
PeptideAtlasⁱ	O94979.
PRIDEⁱ	O94979.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000311785; ENSP00000309070; ENSG00000138674. [O94979-3] ENST00000348405; ENSP00000337602; ENSG00000138674. [O94979-4] ENST00000355196; ENSP00000347329; ENSG00000138674. [O94979-1] ENST00000395310; ENSP00000378721; ENSG00000138674. [O94979-1] ENST00000443462; ENSP00000408027; ENSG00000138674. [O94979-9] ENST00000448323; ENSP00000400926; ENSG00000138674. [O94979-1] ENST00000500777; ENSP00000421464; ENSG00000138674. [O94979-6] ENST00000505984; ENSP00000424451; ENSG00000138674. [O94979-10] ENST00000508502; ENSP00000424635; ENSG00000138674. [O94979-2] ENST00000509142; ENSP00000426569; ENSG00000138674. [O94979-3] ENST00000513858; ENSP00000426886; ENSG00000138674. [O94979-6]
GeneIDⁱ	22872.
KEGGⁱ	hsa:22872.
UCSCⁱ	uc003hnf.3. human. [O94979-1]

Organism-specific databases

CTDⁱ	22872.
GeneCardsⁱ	SEC31A.
HGNCⁱ	HGNC:17052. SEC31A.
HPAⁱ	HPA005457.
MIMⁱ	610257. gene.
neXtProtⁱ	NX_O94979.
PharmGKBⁱ	PA162402737.
HUGEⁱ	Search...
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0307. Eukaryota. ENOG410XQ1D. LUCA.
GeneTreeⁱ	ENSGT00390000003175.
HOGENOMⁱ	HOG000230582.
HOVERGENⁱ	HBG055626.
InParanoidⁱ	O94979.
KOⁱ	K14005.
PhylomeDBⁱ	O94979.
TreeFamⁱ	TF313842.

Enzyme and pathway databases

Reactomeⁱ	R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport. R-HSA-2132295. MHC class II antigen presentation. R-HSA-381038. XBP1(S) activates chaperone genes. R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLinkⁱ	O94979.

Miscellaneous databases

ChiTaRSⁱ	SEC31A. human.
GeneWikiⁱ	SEC31A.
GenomeRNAiⁱ	22872.
PROⁱ	O94979.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000138674.
ExpressionAtlasⁱ	O94979. baseline and differential.
Genevisibleⁱ	O94979. HS.

Family and domain databases

Gene3Dⁱ	2.130.10.10. 1 hit.
InterProⁱ	IPR024298. ACE1_Sec16_Sec31. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR017986. WD40_repeat_dom. [Graphical view]
Pfamⁱ	PF12931. Sec16_C. 1 hit. [Graphical view]
SMARTⁱ	SM00320. WD40. 6 hits. [Graphical view]
SUPFAMⁱ	SSF50978. SSF50978. 1 hit.
PROSITEⁱ	PS50082. WD_REPEATS_2. 1 hit. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

SC31A_HUMAN

Accessionⁱ

Primary (citable) accession number: O94979
Secondary accession number(s): B4DIW6

Q9UM06

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	July 10, 2007
Last modified:	September 7, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - O94979 (SC31A_HUMAN)

UniProt

O94979 - SC31A_HUMAN

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Protein transport protein Sec31A

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (10)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (10)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ