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Protein

Translocating chain-associated membrane protein 2

Gene

TRAM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for collagen type I synthesis. May couple the activity of the ER Ca2+ pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca2+ concentration at the site of collagen synthesis, and a high Ca2+ concentration may be necessary for the function of molecular chaperones involved in collagen folding.1 Publication

GO - Biological processi

  • collagen biosynthetic process Source: UniProtKB
  • cotranslational protein targeting to membrane Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Translocating chain-associated membrane protein 2
Gene namesi
Name:TRAM2
Synonyms:KIAA0057
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:16855. TRAM2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4321HelicalSequence analysisAdd
BLAST
Transmembranei76 – 9621HelicalSequence analysisAdd
BLAST
Transmembranei120 – 14021HelicalSequence analysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence analysisAdd
BLAST
Transmembranei199 – 21921HelicalSequence analysisAdd
BLAST
Transmembranei251 – 27121HelicalSequence analysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394555.

Polymorphism and mutation databases

BioMutaiTRAM2.
DMDMi18202502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Translocating chain-associated membrane protein 2PRO_0000185532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ15035.
MaxQBiQ15035.
PaxDbiQ15035.
PRIDEiQ15035.

PTM databases

iPTMnetiQ15035.
PhosphoSiteiQ15035.
SwissPalmiQ15035.

Expressioni

Gene expression databases

BgeeiQ15035.
CleanExiHS_TRAM2.
ExpressionAtlasiQ15035. baseline and differential.
GenevisibleiQ15035. HS.

Organism-specific databases

HPAiHPA035092.
HPA057925.

Interactioni

Subunit structurei

Interacts with SERCA2B and COL1A1.1 Publication

Protein-protein interaction databases

BioGridi115049. 2 interactions.
STRINGi9606.ENSP00000182527.

Structurei

3D structure databases

ProteinModelPortaliQ15035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 321210TLCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAM family.Curated
Contains 1 TLC (TRAM/LAG1/CLN8) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1608. Eukaryota.
ENOG410XSB3. LUCA.
GeneTreeiENSGT00510000046470.
HOGENOMiHOG000007494.
HOVERGENiHBG054402.
InParanoidiQ15035.
OMAiLFNAWAA.
OrthoDBiEOG7ZPNKC.
PhylomeDBiQ15035.
TreeFamiTF314319.

Family and domain databases

InterProiIPR006634. TLC-dom.
IPR013599. TRAM1.
IPR016447. Translocation_assoc_membrane.
[Graphical view]
PfamiPF08390. TRAM1. 1 hit.
PF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
PIRSFiPIRSF005449. Translocation_assoc_membrane. 1 hit.
SMARTiSM00724. TLC. 1 hit.
[Graphical view]
PROSITEiPS50922. TLC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFRRRTKSY PLFSQEFVIH NHADIGFCLV LCVLIGLMFE VTAKTAFLFI
60 70 80 90 100
LPQYNISVPT ADSETVHYHY GPKDLVTILF YIFITIILHA VVQEYILDKI
110 120 130 140 150
SKRLHLSKVK HSKFNESGQL VVFHFTSVIW CFYVVVTEGY LTNPRSLWED
160 170 180 190 200
YPHVHLPFQV KFFYLCQLAY WLHALPELYF QKVRKEEIPR QLQYICLYLV
210 220 230 240 250
HIAGAYLLNL SRLGLILLLL QYSTEFLFHT ARLFYFADEN NEKLFSAWAA
260 270 280 290 300
VFGVTRLFIL TLAVLAIGFG LARMENQAFD PEKGNFNTLF CRLCVLLLVC
310 320 330 340 350
AAQAWLMWRF IHSQLRHWRE YWNEQSAKRR VPATPRLPAR LIKRESGYHE
360 370
NGVVKAENGT SPRTKKLKSP
Length:370
Mass (Da):43,328
Last modified:November 1, 1996 - v1
Checksum:i9B5183F1A3D45366
GO

Sequence cautioni

The sequence BAA06540.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31762 mRNA. Translation: BAA06540.2. Different initiation.
AK291751 mRNA. Translation: BAF84440.1.
AL049611 Genomic DNA. Translation: CAB71119.1.
CH471081 Genomic DNA. Translation: EAX04373.1.
BC028121 mRNA. Translation: AAH28121.1.
CCDSiCCDS34477.1.
RefSeqiNP_036420.1. NM_012288.3.
UniGeneiHs.520182.

Genome annotation databases

EnsembliENST00000182527; ENSP00000182527; ENSG00000065308.
GeneIDi9697.
KEGGihsa:9697.
UCSCiuc003paq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31762 mRNA. Translation: BAA06540.2. Different initiation.
AK291751 mRNA. Translation: BAF84440.1.
AL049611 Genomic DNA. Translation: CAB71119.1.
CH471081 Genomic DNA. Translation: EAX04373.1.
BC028121 mRNA. Translation: AAH28121.1.
CCDSiCCDS34477.1.
RefSeqiNP_036420.1. NM_012288.3.
UniGeneiHs.520182.

3D structure databases

ProteinModelPortaliQ15035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115049. 2 interactions.
STRINGi9606.ENSP00000182527.

PTM databases

iPTMnetiQ15035.
PhosphoSiteiQ15035.
SwissPalmiQ15035.

Polymorphism and mutation databases

BioMutaiTRAM2.
DMDMi18202502.

Proteomic databases

EPDiQ15035.
MaxQBiQ15035.
PaxDbiQ15035.
PRIDEiQ15035.

Protocols and materials databases

DNASUi9697.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000182527; ENSP00000182527; ENSG00000065308.
GeneIDi9697.
KEGGihsa:9697.
UCSCiuc003paq.4. human.

Organism-specific databases

CTDi9697.
GeneCardsiTRAM2.
HGNCiHGNC:16855. TRAM2.
HPAiHPA035092.
HPA057925.
MIMi608485. gene.
neXtProtiNX_Q15035.
PharmGKBiPA128394555.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1608. Eukaryota.
ENOG410XSB3. LUCA.
GeneTreeiENSGT00510000046470.
HOGENOMiHOG000007494.
HOVERGENiHBG054402.
InParanoidiQ15035.
OMAiLFNAWAA.
OrthoDBiEOG7ZPNKC.
PhylomeDBiQ15035.
TreeFamiTF314319.

Miscellaneous databases

ChiTaRSiTRAM2. human.
GeneWikiiTRAM2.
GenomeRNAii9697.
PROiQ15035.
SOURCEiSearch...

Gene expression databases

BgeeiQ15035.
CleanExiHS_TRAM2.
ExpressionAtlasiQ15035. baseline and differential.
GenevisibleiQ15035. HS.

Family and domain databases

InterProiIPR006634. TLC-dom.
IPR013599. TRAM1.
IPR016447. Translocation_assoc_membrane.
[Graphical view]
PfamiPF08390. TRAM1. 1 hit.
PF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
PIRSFiPIRSF005449. Translocation_assoc_membrane. 1 hit.
SMARTiSM00724. TLC. 1 hit.
[Graphical view]
PROSITEiPS50922. TLC. 1 hit.
[Graphical view]
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].
    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].
    Tissue: Placenta.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis."
    Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.
    Mol. Cell. Biol. 24:1758-1768(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SERCA2B AND COL1A1.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRAM2_HUMAN
AccessioniPrimary (citable) accession number: Q15035
Secondary accession number(s): A8K6T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 127 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.