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Protein

Transmembrane protein 2

Gene

Tmem2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be required for the heart morphogenesis.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane protein 2
Gene namesi
Name:Tmem2
Synonyms:Kiaa1412
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1890373. Tmem2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei83 – 10321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13831383Transmembrane protein 2PRO_0000289973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei63 – 631PhosphoserineBy similarity
Glycosylationi282 – 2821N-linked (GlcNAc...); atypical1 Publication
Glycosylationi292 – 2921N-linked (GlcNAc...)2 Publications
Glycosylationi914 – 9141N-linked (GlcNAc...)1 Publication
Glycosylationi1234 – 12341N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ5FWI3.
PaxDbiQ5FWI3.
PeptideAtlasiQ5FWI3.
PRIDEiQ5FWI3.

PTM databases

iPTMnetiQ5FWI3.
PhosphoSiteiQ5FWI3.
SwissPalmiQ5FWI3.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

expressed ubiquitously at early stages of development. Expressed in the endocardial cells lining the ventricles and atria at 9.5 dpc.1 Publication

Gene expression databases

BgeeiQ5FWI3.
CleanExiMM_TMEM2.
GenevisibleiQ5FWI3. MM.

Interactioni

Protein-protein interaction databases

IntActiQ5FWI3. 1 interaction.
MINTiMINT-4119989.
STRINGi10090.ENSMUSP00000025663.

Structurei

3D structure databases

ProteinModelPortaliQ5FWI3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 245125G8PROSITE-ProRule annotationAdd
BLAST
Repeati669 – 69123PbH1 1Add
BLAST
Repeati711 – 73323PbH1 2Add
BLAST
Repeati791 – 81222PbH1 3Add
BLAST

Sequence similaritiesi

Belongs to the TMEM2 family.Curated
Contains 1 G8 domain.PROSITE-ProRule annotation
Contains 3 PbH1 repeats.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFCM. Eukaryota.
ENOG410XQ01. LUCA.
GeneTreeiENSGT00780000121902.
HOVERGENiHBG052198.
InParanoidiQ5FWI3.
OMAiRNYGFQG.
OrthoDBiEOG7PCJG0.
PhylomeDBiQ5FWI3.
TreeFamiTF316575.

Family and domain databases

InterProiIPR019316. G8_domain.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF10162. G8. 1 hit.
[Graphical view]
SMARTiSM01225. G8. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 2 hits.
PROSITEiPS51484. G8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5FWI3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYAAGSRGHS PAFLQPQNGN GHRSPGYVPG KVVPLRPAPP PKNHASAKLT
60 70 80 90 100
SRSQDAPATF AFSPEEQRTP SESRKRKRHK NTFICFAITS FSFFVALAVI
110 120 130 140 150
LGISSKYAPD ENCPDQNPRL RNWDPGQDSA KHIVIKEGDL FRLTSDATVD
160 170 180 190 200
SIVIQDGGLL VFGDDKDGSK NITLRTRYIL IQDGGALHIG AEKCRYRSKA
210 220 230 240 250
TITLYGKSDE RESMPIFGKK FIGVEAGGTL ELHGAQRTSW TMLARTLHSS
260 270 280 290 300
GLPFGSYAFE KDFSRGLNVR VIDQDTARVL ENEKFDTHEY HNESRRLQEF
310 320 330 340 350
LRAQEPGRIV AIAVGDSAVK SLLQGTIQMI QDRLGSKLIQ GLGYRQAWAL
360 370 380 390 400
VGVIDGGSSS CNESVRNYEN HSTGGKALAQ GEFYTLDGQK FSVTAYSEWS
410 420 430 440 450
QGISLSGFRV DIADGVKLHL LDDVSTWEAG DRIVVASTDY SMYQAEELTL
460 470 480 490 500
LRCPECSRSQ VKVKEIPQYL HVGEIIDGID MRAEVGLLTR NIVIQGEMED
510 520 530 540 550
SCYAENHCQF FDYDTFGGHV MIEKNFTSVH LSYVELKHMG QQHMGRYPVH
560 570 580 590 600
FHLCGDVDSK GGYSQPASVD GLSVHHSFSR CITVHGTSGL LIKDTIGFDT
610 620 630 640 650
LGHCFFLEDG VEQRNILYHN LGLLTKPGTL LPTDRNSSMC TVMRDGVFGN
660 670 680 690 700
YVPVPTTDCM AVSTFWIAHP NNHLINNAAA GSQDAGIWYL FHKEPTGESS
710 720 730 740 750
GLQLLEKPEL TPLGIFYNNR VHSNFKAGLF VDKGVKTTNA SASDPREYLC
760 770 780 790 800
LDNSARFRPH QDADPEKPRV AAIIDRLIAF KNNDNGAWVR GGDIIVQNSA
810 820 830 840 850
FADNGKGLTF ASDGSFPSDE GSSQEVTESL FVGESRNYGF QGGQNKYMGT
860 870 880 890 900
GGIDQKPRTL PRNRTFPIRG FQIYDGPIHL TKSTFKKYVP TPDRYSSAIG
910 920 930 940 950
FLMKNSWQTT PRNNVSLVKF GPQVSLNVFF GKPGPWFEDC ELDGDKNSIF
960 970 980 990 1000
HDIDGSVTGY KDTYVGRMDN YLIRHPNCVN VTKWNAVICS GTYAQVYVQT
1010 1020 1030 1040 1050
WNTPNLSMII TRDEYPSHPM VLRGINQRAI SPQYQPVVML EKGYTIHWNG
1060 1070 1080 1090 1100
PAPRTTFLYL VNFNKDDWIR VGLCYPANTS FQVTVGFLQR QNGSLSRIED
1110 1120 1130 1140 1150
YEPARSMEEL QKKPSERKFY FDSGTGLLFL YLRAHSHRDG HSYCSSQGCE
1160 1170 1180 1190 1200
RVKIQAATDS KDISNCMAKA YPQYYKKPSA VKRMPAMLTG LCQGCGTHQM
1210 1220 1230 1240 1250
VFTSDPHKSY LPVRFQSPGK AEIQRGDPSI ISVNGTDFTF RSAGALLLIV
1260 1270 1280 1290 1300
DACSVPFRVK EKRMFLSADV SHMEEYFKAS IPPRSIVLLS TRGEIKQLNI
1310 1320 1330 1340 1350
SDSLAVLGLA KPAHLYSKGS VVFLGFSGNF APSWTKLFTS PDEQGLGVLE
1360 1370 1380
QFLPLQMEEY GCSRTGSVHR RDLDLLQQAL KVL
Length:1,383
Mass (Da):153,801
Last modified:March 1, 2005 - v1
Checksum:i7AB8F747A8FC659C
GO

Sequence cautioni

The sequence AAH19745.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651D → G in BAE29013 (PubMed:16141072).Curated
Sequence conflicti1134 – 11341A → S in AAF21349 (PubMed:10767548).Curated
Sequence conflicti1161 – 11611K → R in AAF21349 (PubMed:10767548).Curated
Sequence conflicti1180 – 11801A → G in AAF21349 (PubMed:10767548).Curated
Sequence conflicti1245 – 12451A → V in AAH19745 (PubMed:15489334).Curated
Sequence conflicti1249 – 12491I → V in AAH19745 (PubMed:15489334).Curated
Sequence conflicti1306 – 13061V → L in AAH19745 (PubMed:15489334).Curated
Sequence conflicti1342 – 13421D → N in AAH19745 (PubMed:15489334).Curated
Sequence conflicti1382 – 13821V → L in AAH76570 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC019745 mRNA. Translation: AAH19745.1. Different initiation.
BC076570 mRNA. Translation: AAH76570.1.
BC089353 mRNA. Translation: AAH89353.1.
AK149667 mRNA. Translation: BAE29013.1.
AK149803 mRNA. Translation: BAE29096.1.
AK129352 mRNA. Translation: BAC98162.1.
AF137031 mRNA. Translation: AAF21349.1.
CCDSiCCDS37934.1.
RefSeqiNP_001028931.1. NM_001033759.2.
NP_114386.3. NM_031997.4.
XP_006527549.1. XM_006527486.2.
XP_006527550.1. XM_006527487.2.
UniGeneiMm.329776.

Genome annotation databases

EnsembliENSMUST00000025663; ENSMUSP00000025663; ENSMUSG00000024754.
ENSMUST00000096194; ENSMUSP00000093908; ENSMUSG00000024754.
GeneIDi83921.
KEGGimmu:83921.
UCSCiuc008gzg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC019745 mRNA. Translation: AAH19745.1. Different initiation.
BC076570 mRNA. Translation: AAH76570.1.
BC089353 mRNA. Translation: AAH89353.1.
AK149667 mRNA. Translation: BAE29013.1.
AK149803 mRNA. Translation: BAE29096.1.
AK129352 mRNA. Translation: BAC98162.1.
AF137031 mRNA. Translation: AAF21349.1.
CCDSiCCDS37934.1.
RefSeqiNP_001028931.1. NM_001033759.2.
NP_114386.3. NM_031997.4.
XP_006527549.1. XM_006527486.2.
XP_006527550.1. XM_006527487.2.
UniGeneiMm.329776.

3D structure databases

ProteinModelPortaliQ5FWI3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5FWI3. 1 interaction.
MINTiMINT-4119989.
STRINGi10090.ENSMUSP00000025663.

PTM databases

iPTMnetiQ5FWI3.
PhosphoSiteiQ5FWI3.
SwissPalmiQ5FWI3.

Proteomic databases

MaxQBiQ5FWI3.
PaxDbiQ5FWI3.
PeptideAtlasiQ5FWI3.
PRIDEiQ5FWI3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025663; ENSMUSP00000025663; ENSMUSG00000024754.
ENSMUST00000096194; ENSMUSP00000093908; ENSMUSG00000024754.
GeneIDi83921.
KEGGimmu:83921.
UCSCiuc008gzg.2. mouse.

Organism-specific databases

CTDi23670.
MGIiMGI:1890373. Tmem2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IFCM. Eukaryota.
ENOG410XQ01. LUCA.
GeneTreeiENSGT00780000121902.
HOVERGENiHBG052198.
InParanoidiQ5FWI3.
OMAiRNYGFQG.
OrthoDBiEOG7PCJG0.
PhylomeDBiQ5FWI3.
TreeFamiTF316575.

Miscellaneous databases

ChiTaRSiTmem2. mouse.
PROiQ5FWI3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5FWI3.
CleanExiMM_TMEM2.
GenevisibleiQ5FWI3. MM.

Family and domain databases

InterProiIPR019316. G8_domain.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF10162. G8. 1 hit.
[Graphical view]
SMARTiSM01225. G8. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 2 hits.
PROSITEiPS51484. G8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J and Czech II.
    Tissue: Brain and Mammary tumor.
  2. "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] OF 1-235.
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 415-1383.
    Tissue: Embryonic tail.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1033-1383, TISSUE SPECIFICITY.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-292 AND ASN-914.
    Tissue: Myoblast.
  7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-282; ASN-292 AND ASN-1234.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung and Spleen.
  9. "Transmembrane protein 2 (Tmem2) is required to regionally restrict atrioventricular canal boundary and endocardial cushion development."
    Smith K.A., Lagendijk A.K., Courtney A.D., Chen H., Paterson S., Hogan B.M., Wicking C., Bakkers J.
    Development 138:4193-4198(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiTMEM2_MOUSE
AccessioniPrimary (citable) accession number: Q5FWI3
Secondary accession number(s): Q3UE15
, Q3UE98, Q6DFZ0, Q6ZPR7, Q8VE53, Q9QY22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: March 1, 2005
Last modified: July 6, 2016
This is version 87 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.