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

Transmembrane and coiled-coil domain-containing protein 1

Gene

TMCO1

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

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane and coiled-coil domain-containing protein 1
Alternative name(s):
Transmembrane and coiled-coil domains protein 4
Xenogeneic cross-immune protein PCIA3
Gene namesi
Name:TMCO1
Synonyms:TMCC4
ORF Names:PNAS-10, PNAS-136, UNQ151/PRO177
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18188. TMCO1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence analysisAdd
BLAST
Transmembranei91 – 11121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Craniofacial dysmorphism, skeletal anomalies and mental retardation syndrome (CFSMR)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by craniofacial and skeletal anomalies, associated with mental retardation. Typical craniofacial dysmorphism include brachycephaly, highly arched bushy eyebrows, synophrys, long eyelashes, low-set ears, microdontism of primary teeth, and generalized gingival hyperplasia, whereas Sprengel deformity of scapula, fusion of spine, rib abnormities, pectus excavatum, and pes planus represent skeletal anomalies.
See also OMIM:213980

Keywords - Diseasei

Mental retardation

Organism-specific databases

MalaCardsiTMCO1.
MIMi213980. phenotype.
Orphaneti1394. Cerebro-facio-thoracic dysplasia.
PharmGKBiPA142670792.

Polymorphism and mutation databases

BioMutaiTMCO1.
DMDMi74753399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Transmembrane and coiled-coil domain-containing protein 1PRO_0000244076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601PhosphoserineCombined sources
Modified residuei188 – 1881PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UM00.
MaxQBiQ9UM00.
PaxDbiQ9UM00.
PRIDEiQ9UM00.
TopDownProteomicsiQ9UM00-1. [Q9UM00-1]

PTM databases

iPTMnetiQ9UM00.
PhosphoSiteiQ9UM00.
SwissPalmiQ9UM00.

Expressioni

Tissue specificityi

Widely expressed in adult and fetal tissues, with higher levels in thymus, prostate, testis and small intestine and lower levels in brain, placenta, lung and kidney.2 Publications

Gene expression databases

BgeeiQ9UM00.
CleanExiHS_TMCO1.
ExpressionAtlasiQ9UM00. baseline and differential.
GenevisibleiQ9UM00. HS.

Interactioni

Protein-protein interaction databases

BioGridi119995. 42 interactions.
IntActiQ9UM00. 16 interactions.
STRINGi9606.ENSP00000375975.

Structurei

3D structure databases

ProteinModelPortaliQ9UM00.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili32 – 8958Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi180 – 1834Poly-Pro

Sequence similaritiesi

Belongs to the TMCO1 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3312. Eukaryota.
ENOG410XR8B. LUCA.
GeneTreeiENSGT00390000002659.
HOGENOMiHOG000240371.
HOVERGENiHBG054437.
InParanoidiQ9UM00.
OrthoDBiEOG78WKTD.
PhylomeDBiQ9UM00.
TreeFamiTF315045.

Family and domain databases

InterProiIPR002809. DUF106_TM.
IPR008559. UCP023322_TM_euk.
[Graphical view]
PANTHERiPTHR20917. PTHR20917. 1 hit.
PfamiPF01956. DUF106. 1 hit.
[Graphical view]
PIRSFiPIRSF023322. DUF841_euk. 1 hit.
SMARTiSM01415. DUF106. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UM00-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTMFADTLL IVFISVCTAL LAEGITWVLV YRTDKYKRLK AEVEKQSKKL
60 70 80 90 100
EKKKETITES AGRQQKKKIE RQEEKLKNNN RDLSMVRMKS MFAIGFCFTA
110 120 130 140 150
LMGMFNSIFD GRVVAKLPFT PLSYIQGLSH RNLLGDDTTD CSFIFLYILC
160 170 180
TMSIRQNIQK ILGLAPSRAA TKQAGGFLGP PPPSGKFS
Length:188
Mass (Da):21,175
Last modified:May 1, 2000 - v1
Checksum:iFB77BFC4F0629EB1
GO
Isoform 2 (identifier: Q9UM00-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     64-82: Missing.

Note: No experimental confirmation available.
Show »
Length:169
Mass (Da):18,766
Checksum:i263365EFFEE1C17B
GO

Sequence cautioni

The sequence AAC25388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAK07514.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAK07549.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291S → P in AAK07514 (Ref. 4) Curated
Sequence conflicti129 – 1291S → P in AAK07549 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei64 – 8219Missing in isoform 2. 1 PublicationVSP_019505Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020980 mRNA. Translation: BAA86974.1.
AY763589 mRNA. Translation: AAV34755.1.
AF070626 mRNA. Translation: AAC25388.1. Different initiation.
AF274935 mRNA. Translation: AAK07514.1. Frameshift.
AF277194 mRNA. Translation: AAK07549.1. Frameshift.
AY359027 mRNA. Translation: AAQ89386.1.
AK316610 mRNA. Translation: BAG38197.1.
AL451074 Genomic DNA. Translation: CAH74064.1.
BC000104 mRNA. Translation: AAH00104.1.
RefSeqiNP_061899.2. NM_019026.4.
UniGeneiHs.31498.

Genome annotation databases

EnsembliENST00000392129; ENSP00000375975; ENSG00000143183. [Q9UM00-1]
GeneIDi54499.
KEGGihsa:54499.
UCSCiuc057mzb.1. human. [Q9UM00-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020980 mRNA. Translation: BAA86974.1.
AY763589 mRNA. Translation: AAV34755.1.
AF070626 mRNA. Translation: AAC25388.1. Different initiation.
AF274935 mRNA. Translation: AAK07514.1. Frameshift.
AF277194 mRNA. Translation: AAK07549.1. Frameshift.
AY359027 mRNA. Translation: AAQ89386.1.
AK316610 mRNA. Translation: BAG38197.1.
AL451074 Genomic DNA. Translation: CAH74064.1.
BC000104 mRNA. Translation: AAH00104.1.
RefSeqiNP_061899.2. NM_019026.4.
UniGeneiHs.31498.

3D structure databases

ProteinModelPortaliQ9UM00.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119995. 42 interactions.
IntActiQ9UM00. 16 interactions.
STRINGi9606.ENSP00000375975.

PTM databases

iPTMnetiQ9UM00.
PhosphoSiteiQ9UM00.
SwissPalmiQ9UM00.

Polymorphism and mutation databases

BioMutaiTMCO1.
DMDMi74753399.

Proteomic databases

EPDiQ9UM00.
MaxQBiQ9UM00.
PaxDbiQ9UM00.
PRIDEiQ9UM00.
TopDownProteomicsiQ9UM00-1. [Q9UM00-1]

Protocols and materials databases

DNASUi54499.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392129; ENSP00000375975; ENSG00000143183. [Q9UM00-1]
GeneIDi54499.
KEGGihsa:54499.
UCSCiuc057mzb.1. human. [Q9UM00-1]

Organism-specific databases

CTDi54499.
GeneCardsiTMCO1.
HGNCiHGNC:18188. TMCO1.
MalaCardsiTMCO1.
MIMi213980. phenotype.
614123. gene.
neXtProtiNX_Q9UM00.
Orphaneti1394. Cerebro-facio-thoracic dysplasia.
PharmGKBiPA142670792.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3312. Eukaryota.
ENOG410XR8B. LUCA.
GeneTreeiENSGT00390000002659.
HOGENOMiHOG000240371.
HOVERGENiHBG054437.
InParanoidiQ9UM00.
OrthoDBiEOG78WKTD.
PhylomeDBiQ9UM00.
TreeFamiTF315045.

Miscellaneous databases

ChiTaRSiTMCO1. human.
GeneWikiiTMCO1.
GenomeRNAii54499.
PROiQ9UM00.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UM00.
CleanExiHS_TMCO1.
ExpressionAtlasiQ9UM00. baseline and differential.
GenevisibleiQ9UM00. HS.

Family and domain databases

InterProiIPR002809. DUF106_TM.
IPR008559. UCP023322_TM_euk.
[Graphical view]
PANTHERiPTHR20917. PTHR20917. 1 hit.
PfamiPF01956. DUF106. 1 hit.
[Graphical view]
PIRSFiPIRSF023322. DUF841_euk. 1 hit.
SMARTiSM01415. DUF106. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multi-ubiquitination of a nascent membrane protein produced in a rabbit reticulocyte lysate."
    Iwamuro S., Saeki M., Kato S.
    J. Biochem. 126:48-53(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Gastric adenocarcinoma.
  2. "Identification of angiogenesis-related genes from placenta by xenogeneic antibody screening."
    Deng H.-X., Wei Y.-Q., Zhao X., Yang H.-S., Wang R., Yang J.-L.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Human acute promyelocytic leukemia cell line NB4's apoptosis/differentiation related genes."
    Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Promyelocytic leukemia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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] (ISOFORM 1).
    Tissue: Trachea.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Placenta.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Homozygous frameshift mutation in TMCO1 causes a syndrome with craniofacial dysmorphism, skeletal anomalies, and mental retardation."
    Xin B., Puffenberger E.G., Turben S., Tan H., Zhou A., Wang H.
    Proc. Natl. Acad. Sci. U.S.A. 107:258-263(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CFSMR, TISSUE SPECIFICITY.
  13. "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-60 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTMCO1_HUMAN
AccessioniPrimary (citable) accession number: Q9UM00
Secondary accession number(s): B2REA0
, O75545, Q9BZS3, Q9BZU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 129 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 1
    Human chromosome 1: 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.