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Q9UIK5

- TEFF2_HUMAN

UniProt

Q9UIK5 - TEFF2_HUMAN

Protein

Tomoregulin-2

Gene

TMEFF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    May be a survival factor for hippocampal and mesencephalic neurons. The shedded form up-regulates cancer cell proliferation, probably by promoting ERK1/2 phosphorylation.2 Publications

    Protein family/group databases

    MEROPSiI01.969.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tomoregulin-2
    Short name:
    TR-2
    Alternative name(s):
    Hyperplastic polyposis protein 1
    Transmembrane protein with EGF-like and two follistatin-like domains
    Gene namesi
    Name:TMEFF2
    Synonyms:HPP1, TENB2, TPEF
    ORF Names:UNQ178/PRO204
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11867. TMEFF2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36568.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 40401 PublicationAdd
    BLAST
    Chaini41 – 374334Tomoregulin-2PRO_0000016587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi204 – 2041N-linked (GlcNAc...) (complex); atypical2 Publications
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi265 ↔ 278By similarity
    Disulfide bondi273 ↔ 289By similarity
    Disulfide bondi291 ↔ 300By similarity

    Post-translational modificationi

    N-glycosylated. Contains chondroitin sulfate glycosaminoglycans.2 Publications
    A soluble form (TMEFF2-ECD) is produced by proteolytic shedding. This shedding can be induced by phorbol ester or proinflammatory cytokines such as TNFalpha, and is mediated by ADAM17.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9UIK5.
    PRIDEiQ9UIK5.

    PTM databases

    PhosphoSiteiQ9UIK5.

    Miscellaneous databases

    PMAP-CutDBQ9UIK5.

    Expressioni

    Tissue specificityi

    Highly expressed in adult and fetal brain, spinal cord and prostate. Expressed in all brain regions except the pituitary gland, with highest levels in amygdala and corpus callosum. Expressed in the pericryptal myofibroblasts and other stromal cells of normal colonic mucosa. Expressed in prostate carcinoma. Down-regulated in colorectal cancer. Present in Alzheimer disease plaques (at protein level). Isoform 3 is expressed weakly in testis and at high levels in normal and cancerous prostate.6 Publications

    Inductioni

    Down-regulated in tumor cell lines in response to a high level of methylation in the 5' region. The CpG island methylation correlates with TMEFF2 silencing in tumor cell lines.2 Publications

    Gene expression databases

    BgeeiQ9UIK5.
    GenevestigatoriQ9UIK5.

    Organism-specific databases

    HPAiHPA015587.

    Interactioni

    Protein-protein interaction databases

    BioGridi117189. 2 interactions.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FMWmodel-A264-301[»]
    ProteinModelPortaliQ9UIK5.
    SMRiQ9UIK5. Positions 88-135, 157-232, 273-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini41 – 320280ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini342 – 37433CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei321 – 34121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 13753Kazal-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini176 – 22954Kazal-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini261 – 30141EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni303 – 32018Required for sheddingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the tomoregulin family.Curated
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 2 Kazal-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG245393.
    HOVERGENiHBG053816.
    InParanoidiQ9UIK5.
    OMAiRGLYIPC.
    OrthoDBiEOG7JT6WK.
    PhylomeDBiQ9UIK5.
    TreeFamiTF330868.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002350. Kazal_dom.
    [Graphical view]
    PfamiPF12661. hEGF. 1 hit.
    PF07648. Kazal_2. 2 hits.
    [Graphical view]
    SMARTiSM00181. EGF. 1 hit.
    SM00280. KAZAL. 2 hits.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS51465. KAZAL_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UIK5-1) [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

    MVLWESPRQC SSWTLCEGFC WLLLLPVMLL IVARPVKLAA FPTSLSDCQT    50
    PTGWNCSGYD DRENDLFLCD TNTCKFDGEC LRIGDTVTCV CQFKCNNDYV 100
    PVCGSNGESY QNECYLRQAA CKQQSEILVV SEGSCATDAG SGSGDGVHEG 150
    SGETSQKETS TCDICQFGAE CDEDAEDVWC VCNIDCSQTN FNPLCASDGK 200
    SYDNACQIKE ASCQKQEKIE VMSLGRCQDN TTTTTKSEDG HYARTDYAEN 250
    ANKLEESARE HHIPCPEHYN GFCMHGKCEH SINMQEPSCR CDAGYTGQHC 300
    EKKDYSVLYV VPGPVRFQYV LIAAVIGTIQ IAVICVVVLC ITRKCPRSNR 350
    IHRQKQNTGH YSSDNTTRAS TRLI 374
    Length:374
    Mass (Da):41,428
    Last modified:May 1, 2000 - v1
    Checksum:i44452F680FEBDCDB
    GO
    Isoform 2 (identifier: Q9UIK5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         344-346: KCP → AKL
         347-374: Missing.

    Show »
    Length:346
    Mass (Da):38,132
    Checksum:iA2C7231AD4CD43EA
    GO
    Isoform 3 (identifier: Q9UIK5-3) [UniParc]FASTAAdd to Basket

    Also known as: TMEFF2-S

    The sequence of this isoform differs from the canonical sequence as follows:
         147-175: VHEGSGETSQKETSTCDICQFGAECDEDA → GRSCLFTYLKIYWWILLCIFTYVCSISDI
         176-374: Missing.

    Show »
    Length:175
    Mass (Da):19,472
    Checksum:i8CF92F9D9FB171DF
    GO

    Sequence cautioni

    The sequence BAA90820.1 differs from that shown. Reason: Contaminating sequence. Mitochondrial contamination starting in position 361.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281M → V in BAD96411. 1 PublicationCurated
    Sequence conflicti63 – 631E → G in BAC11030. (PubMed:14702039)Curated
    Sequence conflicti222 – 2221M → T in BAD96411. 1 PublicationCurated
    Sequence conflicti339 – 3391L → H in BAD96411. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei147 – 17529VHEGS…CDEDA → GRSCLFTYLKIYWWILLCIF TYVCSISDI in isoform 3. 1 PublicationVSP_024973Add
    BLAST
    Alternative sequencei176 – 374199Missing in isoform 3. 1 PublicationVSP_024974Add
    BLAST
    Alternative sequencei344 – 3463KCP → AKL in isoform 2. 2 PublicationsVSP_014312
    Alternative sequencei347 – 37428Missing in isoform 2. 2 PublicationsVSP_014313Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017269 mRNA. Translation: BAA87897.1.
    AF242221 Genomic DNA. Translation: AAG49451.1.
    AF242222 mRNA. Translation: AAG49452.1.
    AF179274 mRNA. Translation: AAD55776.2.
    DQ133599 mRNA. Translation: AAZ43216.1.
    AY358907 mRNA. Translation: AAQ89266.1.
    AK074507 mRNA. Translation: BAC11030.1.
    CR457390 mRNA. Translation: CAG33671.1.
    AK222691 mRNA. Translation: BAD96411.1.
    AL157430 mRNA. Translation: CAB75654.1.
    AC092644 Genomic DNA. Translation: AAY14874.1.
    AC098617 Genomic DNA. Translation: AAX88893.1.
    BC008973 mRNA. Translation: AAH08973.1.
    AB004064 mRNA. Translation: BAA90820.1. Different termination.
    AF264150 Genomic DNA. Translation: AAF91397.1.
    CCDSiCCDS2314.1. [Q9UIK5-1]
    PIRiT46914.
    RefSeqiNP_057276.2. NM_016192.2. [Q9UIK5-1]
    XP_005246494.1. XM_005246437.1. [Q9UIK5-2]
    UniGeneiHs.144513.

    Genome annotation databases

    EnsembliENST00000272771; ENSP00000272771; ENSG00000144339. [Q9UIK5-1]
    ENST00000392314; ENSP00000376128; ENSG00000144339. [Q9UIK5-2]
    ENST00000409056; ENSP00000386871; ENSG00000144339. [Q9UIK5-3]
    GeneIDi23671.
    KEGGihsa:23671.
    UCSCiuc002utc.3. human. [Q9UIK5-1]
    uc002utd.1. human. [Q9UIK5-3]
    uc031rqm.1. human. [Q9UIK5-2]

    Polymorphism databases

    DMDMi71153590.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017269 mRNA. Translation: BAA87897.1 .
    AF242221 Genomic DNA. Translation: AAG49451.1 .
    AF242222 mRNA. Translation: AAG49452.1 .
    AF179274 mRNA. Translation: AAD55776.2 .
    DQ133599 mRNA. Translation: AAZ43216.1 .
    AY358907 mRNA. Translation: AAQ89266.1 .
    AK074507 mRNA. Translation: BAC11030.1 .
    CR457390 mRNA. Translation: CAG33671.1 .
    AK222691 mRNA. Translation: BAD96411.1 .
    AL157430 mRNA. Translation: CAB75654.1 .
    AC092644 Genomic DNA. Translation: AAY14874.1 .
    AC098617 Genomic DNA. Translation: AAX88893.1 .
    BC008973 mRNA. Translation: AAH08973.1 .
    AB004064 mRNA. Translation: BAA90820.1 . Different termination.
    AF264150 Genomic DNA. Translation: AAF91397.1 .
    CCDSi CCDS2314.1. [Q9UIK5-1 ]
    PIRi T46914.
    RefSeqi NP_057276.2. NM_016192.2. [Q9UIK5-1 ]
    XP_005246494.1. XM_005246437.1. [Q9UIK5-2 ]
    UniGenei Hs.144513.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FMW model - A 264-301 [» ]
    ProteinModelPortali Q9UIK5.
    SMRi Q9UIK5. Positions 88-135, 157-232, 273-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117189. 2 interactions.

    Protein family/group databases

    MEROPSi I01.969.

    PTM databases

    PhosphoSitei Q9UIK5.

    Polymorphism databases

    DMDMi 71153590.

    Proteomic databases

    PaxDbi Q9UIK5.
    PRIDEi Q9UIK5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272771 ; ENSP00000272771 ; ENSG00000144339 . [Q9UIK5-1 ]
    ENST00000392314 ; ENSP00000376128 ; ENSG00000144339 . [Q9UIK5-2 ]
    ENST00000409056 ; ENSP00000386871 ; ENSG00000144339 . [Q9UIK5-3 ]
    GeneIDi 23671.
    KEGGi hsa:23671.
    UCSCi uc002utc.3. human. [Q9UIK5-1 ]
    uc002utd.1. human. [Q9UIK5-3 ]
    uc031rqm.1. human. [Q9UIK5-2 ]

    Organism-specific databases

    CTDi 23671.
    GeneCardsi GC02M192777.
    HGNCi HGNC:11867. TMEFF2.
    HPAi HPA015587.
    MIMi 605734. gene.
    neXtProti NX_Q9UIK5.
    PharmGKBi PA36568.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245393.
    HOVERGENi HBG053816.
    InParanoidi Q9UIK5.
    OMAi RGLYIPC.
    OrthoDBi EOG7JT6WK.
    PhylomeDBi Q9UIK5.
    TreeFami TF330868.

    Miscellaneous databases

    GeneWikii TMEFF2.
    GenomeRNAii 23671.
    NextBioi 46527.
    PMAP-CutDB Q9UIK5.
    PROi Q9UIK5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UIK5.
    Genevestigatori Q9UIK5.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002350. Kazal_dom.
    [Graphical view ]
    Pfami PF12661. hEGF. 1 hit.
    PF07648. Kazal_2. 2 hits.
    [Graphical view ]
    SMARTi SM00181. EGF. 1 hit.
    SM00280. KAZAL. 2 hits.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS51465. KAZAL_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of TMEFF2, a novel survival factor for hippocampal and mesencephalic neurons."
      Horie M., Mitsumoto Y., Kyushiki H., Kanemoto N., Watanabe A., Taniguchi Y., Nishino N., Okamoto T., Kondo M., Mori T., Noguchi K., Nakamura Y., Takahashi E., Tanigami A.
      Genomics 67:146-152(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "The gene for a novel transmembrane protein containing epidermal growth factor and follistatin domains is frequently hypermethylated in human tumor cells."
      Liang G., Robertson K.D., Talmadge C., Sumegi J., Jones P.A.
      Cancer Res. 60:4907-4912(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, INDUCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "TENB2, a proteoglycan identified in prostate cancer that is associated with disease progression and androgen independence."
      Glynne-Jones E., Harper M.E., Seery L.T., James R., Anglin I., Morgan H.E., Taylor K.M., Gee J.M., Nicholson R.I.
      Int. J. Cancer 94:178-184(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, TISSUE SPECIFICITY.
      Tissue: Prostatic carcinoma.
    4. "A truncated isoform of TMEFF2 encodes a secreted protein in prostate cancer cells."
      Quayle S.N., Sadar M.D.
      Genomics 87:633-637(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    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: Embryo.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    10. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Brain.
    12. "A novel epidermal growth factor-like molecule containing two follistatin modules stimulates tyrosine phosphorylation of erbB-4 in MKN28 gastric cancer cells."
      Uchida T., Wada K., Akamatsu T., Yonezawa M., Noguchi H., Mizoguchi A., Kasuga M., Sakamoto C.
      Biochem. Biophys. Res. Commun. 266:593-602(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-360.
    13. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, TISSUE SPECIFICITY, INDUCTION.
      Tissue: Colon.
    14. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-55.
    15. "Tomoregulin-2 is found extensively in plaques in Alzheimer's disease brain."
      Siegel D.A., Davies P., Dobrenis K., Huang M.
      J. Neurochem. 98:34-44(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. "Phorbol ester-induced shedding of the prostate cancer marker transmembrane protein with epidermal growth factor and two follistatin motifs 2 is mediated by the disintegrin and metalloproteinase-17."
      Ali N., Knaeuper V.
      J. Biol. Chem. 282:37378-37388(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE, FUNCTION.
    17. Cited for: GLYCOSYLATION AT ASN-204.

    Entry informationi

    Entry nameiTEFF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIK5
    Secondary accession number(s): Q2FA44
    , Q4ZFW4, Q53H90, Q53RE1, Q8N2R5, Q9NR15, Q9NSS5, Q9P2Y9, Q9UK65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3