Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trafficking protein particle complex subunit 2

Gene

Trappc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Transcription, Transport

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Trafficking protein particle complex subunit 2
Alternative name(s):
Sedlin
Gene namesi
Name:Trappc2
Synonyms:Sedl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1913476. Trappc2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: MGI
  • TRAPP complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471D → Y: Increased interaction with TRAPPC3. 1 Publication
Mutagenesisi73 – 731S → L: Aberrant protein folding and increased proteasomal degradation. 1 Publication
Mutagenesisi83 – 831F → S: Aberrant protein folding and increased proteasomal degradation. 1 Publication
Mutagenesisi130 – 1301V → D: Aberrant protein folding and increased proteasomal degradation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 140140Trafficking protein particle complex subunit 2PRO_0000211567Add
BLAST

Proteomic databases

EPDiQ9CQP2.
MaxQBiQ9CQP2.
PaxDbiQ9CQP2.
PRIDEiQ9CQP2.

PTM databases

iPTMnetiQ9CQP2.
PhosphoSiteiQ9CQP2.

Expressioni

Tissue specificityi

Expressed in chondrocytes at various stages of differentiation, including proliferating, prehypertrophic and hypertrophic chondrocytes in the distal femoral joint.1 Publication

Gene expression databases

BgeeiQ9CQP2.
ExpressionAtlasiQ9CQP2. baseline and differential.
GenevisibleiQ9CQP2. MM.

Interactioni

Subunit structurei

Part of the multisubunit TRAPP (transport protein particle) complex. Interacts with ENO1, PITX1, SF1 and TRAPPC2L (By similarity). Interacts with TRAPPC3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Spata4Q8K3V13EBI-1172267,EBI-7067375

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211310. 4 interactions.
IntActiQ9CQP2. 9 interactions.
MINTiMINT-4613576.
STRINGi10090.ENSMUSP00000107813.

Structurei

Secondary structure

1
140
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi16 – 227Combined sources
Helixi28 – 303Combined sources
Helixi31 – 5222Combined sources
Helixi53 – 553Combined sources
Beta strandi59 – 679Combined sources
Beta strandi70 – 767Combined sources
Beta strandi82 – 898Combined sources
Helixi92 – 11120Combined sources
Helixi124 – 13714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3QX-ray2.40A1-140[»]
2J3WX-ray2.10A/C1-140[»]
ProteinModelPortaliQ9CQP2.
SMRiQ9CQP2. Positions 1-140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CQP2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3487. Eukaryota.
COG5603. LUCA.
GeneTreeiENSGT00510000047168.
HOGENOMiHOG000214139.
HOVERGENiHBG006717.
InParanoidiQ9CQP2.
OMAiIRFIMLH.
OrthoDBiEOG7JQBQ9.
PhylomeDBiQ9CQP2.
TreeFamiTF314814.

Family and domain databases

InterProiIPR011012. Longin-like_dom.
IPR006722. Sedlin.
[Graphical view]
PANTHERiPTHR12403. PTHR12403. 1 hit.
PfamiPF04628. Sedlin_N. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CQP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSFYFVIV GHHDNPVFEM EFLPPGKAES KDDHRHLNQF IAHAALDLVD
60 70 80 90 100
ENMWLSNNMY LKTVDKFNEW FVSAFVTAGH MRFIMLHDVR QEDGIKNFFT
110 120 130 140
DVYDLYIKFA MNPFYEPNSP IRSSAFDRKV QFLGKKHLLS
Length:140
Mass (Da):16,441
Last modified:June 1, 2001 - v1
Checksum:i6EE89427D223FCB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71F → I in BAB22265 (PubMed:16141072).Curated
Sequence conflicti25 – 251P → A in BAB25114 (PubMed:16141072).Curated
Sequence conflicti25 – 251P → A in BAB22047 (PubMed:16141072).Curated
Sequence conflicti25 – 251P → A in BAB23275 (PubMed:16141072).Curated
Sequence conflicti33 – 331D → E in BAB25114 (PubMed:16141072).Curated
Sequence conflicti33 – 331D → E in BAB22047 (PubMed:16141072).Curated
Sequence conflicti33 – 331D → E in BAB23275 (PubMed:16141072).Curated
Sequence conflicti83 – 831F → L in BAB25114 (PubMed:16141072).Curated
Sequence conflicti83 – 831F → L in BAB22047 (PubMed:16141072).Curated
Sequence conflicti83 – 831F → L in BAB23275 (PubMed:16141072).Curated
Sequence conflicti91 – 911Q → H in BAB25114 (PubMed:16141072).Curated
Sequence conflicti91 – 911Q → H in BAB22047 (PubMed:16141072).Curated
Sequence conflicti91 – 911Q → H in BAB23275 (PubMed:16141072).Curated
Sequence conflicti98 – 981F → L in BAB23284 (PubMed:16141072).Curated
Sequence conflicti122 – 1221R → Q in BAC36921 (PubMed:16141072).Curated
Sequence conflicti127 – 1271D → E in BAB25114 (PubMed:16141072).Curated
Sequence conflicti127 – 1271D → E in BAB22047 (PubMed:16141072).Curated
Sequence conflicti127 – 1271D → E in BAB23275 (PubMed:16141072).Curated
Sequence conflicti140 – 1401S → N in BAB25114 (PubMed:16141072).Curated
Sequence conflicti140 – 1401S → N in BAB22047 (PubMed:16141072).Curated
Sequence conflicti140 – 1401S → N in BAB23275 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008564 mRNA. Translation: BAB25747.1.
AK007889 mRNA. Translation: BAB25332.1.
AK002658 mRNA. Translation: BAB22265.1.
AK004389 mRNA. Translation: BAB23284.1.
AK007568 mRNA. Translation: BAB25114.1.
AK002369 mRNA. Translation: BAB22047.1.
AK004363 mRNA. Translation: BAB23275.1.
AK077643 mRNA. Translation: BAC36921.1.
BC034845 mRNA. Translation: AAH34845.1.
BC061087 mRNA. Translation: AAH61087.1.
CCDSiCCDS41208.1.
RefSeqiNP_001300651.1. NM_001313722.1.
NP_079595.1. NM_025319.2.
NP_079708.2. NM_025432.4.
XP_006533980.1. XM_006533917.2.
XP_006533981.1. XM_006533918.2.
XP_006533982.1. XM_006533919.2.
UniGeneiMm.279752.
Mm.35693.

Genome annotation databases

EnsembliENSMUST00000112194; ENSMUSP00000107813; ENSMUSG00000079317.
ENSMUST00000116495; ENSMUSP00000112195; ENSMUSG00000079317.
GeneIDi66050.
66226.
KEGGimmu:66050.
mmu:66226.
UCSCiuc009uws.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008564 mRNA. Translation: BAB25747.1.
AK007889 mRNA. Translation: BAB25332.1.
AK002658 mRNA. Translation: BAB22265.1.
AK004389 mRNA. Translation: BAB23284.1.
AK007568 mRNA. Translation: BAB25114.1.
AK002369 mRNA. Translation: BAB22047.1.
AK004363 mRNA. Translation: BAB23275.1.
AK077643 mRNA. Translation: BAC36921.1.
BC034845 mRNA. Translation: AAH34845.1.
BC061087 mRNA. Translation: AAH61087.1.
CCDSiCCDS41208.1.
RefSeqiNP_001300651.1. NM_001313722.1.
NP_079595.1. NM_025319.2.
NP_079708.2. NM_025432.4.
XP_006533980.1. XM_006533917.2.
XP_006533981.1. XM_006533918.2.
XP_006533982.1. XM_006533919.2.
UniGeneiMm.279752.
Mm.35693.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3QX-ray2.40A1-140[»]
2J3WX-ray2.10A/C1-140[»]
ProteinModelPortaliQ9CQP2.
SMRiQ9CQP2. Positions 1-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211310. 4 interactions.
IntActiQ9CQP2. 9 interactions.
MINTiMINT-4613576.
STRINGi10090.ENSMUSP00000107813.

PTM databases

iPTMnetiQ9CQP2.
PhosphoSiteiQ9CQP2.

Proteomic databases

EPDiQ9CQP2.
MaxQBiQ9CQP2.
PaxDbiQ9CQP2.
PRIDEiQ9CQP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112194; ENSMUSP00000107813; ENSMUSG00000079317.
ENSMUST00000116495; ENSMUSP00000112195; ENSMUSG00000079317.
GeneIDi66050.
66226.
KEGGimmu:66050.
mmu:66226.
UCSCiuc009uws.1. mouse.

Organism-specific databases

CTDi6399.
MGIiMGI:1913476. Trappc2.

Phylogenomic databases

eggNOGiKOG3487. Eukaryota.
COG5603. LUCA.
GeneTreeiENSGT00510000047168.
HOGENOMiHOG000214139.
HOVERGENiHBG006717.
InParanoidiQ9CQP2.
OMAiIRFIMLH.
OrthoDBiEOG7JQBQ9.
PhylomeDBiQ9CQP2.
TreeFamiTF314814.

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.

Miscellaneous databases

EvolutionaryTraceiQ9CQP2.
PROiQ9CQP2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQP2.
ExpressionAtlasiQ9CQP2. baseline and differential.
GenevisibleiQ9CQP2. MM.

Family and domain databases

InterProiIPR011012. Longin-like_dom.
IPR006722. Sedlin.
[Graphical view]
PANTHERiPTHR12403. PTHR12403. 1 hit.
PfamiPF04628. Sedlin_N. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Kidney, Pancreas and Small intestine.
  2. "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].
    Tissue: Brain and Mammary gland.
  3. "Biochemical consequences of sedlin mutations that cause spondyloepiphyseal dysplasia tarda."
    Choi M.Y., Chan C.C.Y., Chan D., Luk K.D.K., Cheah K.S.E., Tanner J.A.
    Biochem. J. 423:233-242(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAPPC3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-47; SER-73; PHE-83 AND VAL-130.
  4. "Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda."
    Jang S.B., Kim Y.-G., Cho Y.-S., Suh P.-G., Kim K.-H., Oh B.-H.
    J. Biol. Chem. 277:49863-49869(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiTPPC2_MOUSE
AccessioniPrimary (citable) accession number: Q9CQP2
Secondary accession number(s): Q8BP61
, Q9CQF5, Q9D0V3, Q9DCM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.