Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UKZ4

- TEN1_HUMAN

UniProt

Q9UKZ4 - TEN1_HUMAN

Protein

Teneurin-1

Gene

TENM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer By similarity.By similarity
    Teneurin C-terminal-associated peptide: Plays a role in the regulation of neuroplasticity in the limbic system. Mediates a rapid reorganization of actin- and tubulin-based cytoskeleton elements with an increase in dendritic arborization and spine density formation of neurons in the hippocampus and amygdala. Induces BDNF transcription inhibition in neurons. Activates the mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK) cascade. Acts also as a bioactive neuroprotective peptide on limbic neurons of the brain and regulates stress-induced behavior: attenuates alkalosis-associated necrotic cell death and the effects of corticotropin-releasing factor (CRF) on c-fos/FOS induction and on the reinstatement of cocaine seeking By similarity.By similarity
    Ten-1 intracellular domain: Induces gene transcription activation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei2595 – 25962CleavageCurated

    GO - Molecular functioni

    1. heparin binding Source: ProtInc
    2. protein heterodimerization activity Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. immune response Source: ProtInc
    2. negative regulation of cell proliferation Source: ProtInc
    3. nervous system development Source: ProtInc
    4. neuropeptide signaling pathway Source: UniProtKB-KW
    5. positive regulation of actin filament polymerization Source: UniProtKB
    6. positive regulation of filopodium assembly Source: UniProtKB
    7. positive regulation of intracellular protein transport Source: UniProtKB
    8. positive regulation of MAP kinase activity Source: UniProtKB
    9. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    10. regulation of transcription from RNA polymerase III promoter Source: UniProtKB
    11. response to stress Source: UniProtKB-KW
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Neuropeptide, Repressor

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiQ9UKZ4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Teneurin-1
    Short name:
    Ten-1
    Alternative name(s):
    Protein Odd Oz/ten-m homolog 1
    Tenascin-M1
    Short name:
    Ten-m1
    Teneurin transmembrane protein 1
    Cleaved into the following 2 chains:
    Ten-1 intracellular domain
    Short name:
    IDten-1
    Short name:
    Ten-1 ICD
    Alternative name(s):
    Ten-1 extracellular domain
    Short name:
    Ten-1 ECD
    Gene namesi
    Name:TENM1
    Synonyms:ODZ1, TNM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8117. TENM1.

    Subcellular locationi

    Cell membrane By similarity; Single-pass membrane protein By similarity
    Chain Ten-1 intracellular domain : Nucleus By similarity. Nucleus speckle By similarity. Nucleus matrix By similarity. Cytoplasmcytoskeleton By similarity
    Chain Teneurin C-terminal-associated peptide : Nucleus By similarity. Cytoplasm By similarity. Cell membrane By similarity
    Note: Colocalizes with the dystroglycan complex at the cell membrane in hippocampal cells. Binds hippocampal cell membranes and is incorporated in the cytoplasm by endocytosis in a caveoli-dependent manner. Upon cell internalization is transported arround and in the nucleus By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. extracellular region Source: ProtInc
    5. Golgi apparatus Source: UniProtKB
    6. integral component of plasma membrane Source: UniProtKB
    7. nuclear matrix Source: UniProtKB
    8. nuclear speck Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27252725Teneurin-1PRO_0000259498Add
    BLAST
    Chaini1 – ?Ten-1 intracellular domainBy similarityPRO_0000421005
    Chaini2596 – 2725130Teneurin C-terminal-associated peptideBy similarityPRO_0000421006Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi532 ↔ 542PROSITE-ProRule annotation
    Disulfide bondi536 ↔ 547PROSITE-ProRule annotation
    Disulfide bondi549 ↔ 558PROSITE-ProRule annotation
    Disulfide bondi567 ↔ 578PROSITE-ProRule annotation
    Disulfide bondi580 ↔ 589PROSITE-ProRule annotation
    Disulfide bondi596 ↔ 607PROSITE-ProRule annotation
    Disulfide bondi601 ↔ 612PROSITE-ProRule annotation
    Disulfide bondi614 ↔ 623PROSITE-ProRule annotation
    Disulfide bondi628 ↔ 639PROSITE-ProRule annotation
    Disulfide bondi633 ↔ 644PROSITE-ProRule annotation
    Disulfide bondi646 ↔ 655PROSITE-ProRule annotation
    Disulfide bondi666 ↔ 679PROSITE-ProRule annotation
    Disulfide bondi681 ↔ 690PROSITE-ProRule annotation
    Disulfide bondi695 ↔ 705PROSITE-ProRule annotation
    Disulfide bondi699 ↔ 710PROSITE-ProRule annotation
    Disulfide bondi712 ↔ 721PROSITE-ProRule annotation
    Disulfide bondi726 ↔ 736PROSITE-ProRule annotation
    Disulfide bondi730 ↔ 741PROSITE-ProRule annotation
    Disulfide bondi743 ↔ 752PROSITE-ProRule annotation
    Disulfide bondi765 ↔ 775PROSITE-ProRule annotation
    Disulfide bondi769 ↔ 784PROSITE-ProRule annotation
    Disulfide bondi786 ↔ 795PROSITE-ProRule annotation
    Glycosylationi905 – 9051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1084 – 10841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1550 – 15501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1567 – 15671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1663 – 16631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1699 – 16991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1757 – 17571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1781 – 17811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1842 – 18421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2145 – 21451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2285 – 22851N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2580 – 25801Phosphoserine1 Publication
    Glycosylationi2602 – 26021N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Teneurin C-terminal-associated peptide: Derives from the plasma membrane form by proteolytic processing. Further proteolytic cleavage may be generated By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9UKZ4.
    PRIDEiQ9UKZ4.

    PTM databases

    PhosphoSiteiQ9UKZ4.

    Expressioni

    Tissue specificityi

    Expressed in fetal brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9UKZ4.
    BgeeiQ9UKZ4.
    CleanExiHS_ODZ1.
    GenevestigatoriQ9UKZ4.

    Organism-specific databases

    HPAiHPA002848.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Heterodimer with either TENM2 or TENM3. May also form heterodimer with TENM4. Ten-1 ICD interacts with SORBS1 (via third SH3 domain). Interacts with MBD1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi115477. 2 interactions.
    STRINGi9606.ENSP00000360171.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKZ4.
    SMRiQ9UKZ4. Positions 504-841, 1305-1334, 1364-1391.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 324324CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini346 – 27252380ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei325 – 34521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 318318Teneurin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 55932EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini560 – 59132EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 62433EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini625 – 65733EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini658 – 69134EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini692 – 72130EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini722 – 75332EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini761 – 79636EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Repeati1194 – 121926NHL 1Add
    BLAST
    Repeati1292 – 133645NHL 2Add
    BLAST
    Repeati1351 – 140252NHL 3Add
    BLAST
    Repeati1414 – 145845NHL 4Add
    BLAST
    Repeati1481 – 152444NHL 5Add
    BLAST
    Repeati1534 – 155320YD 1Add
    BLAST
    Repeati1570 – 159021YD 2Add
    BLAST
    Repeati1608 – 163225YD 3Add
    BLAST
    Repeati1633 – 165422YD 4Add
    BLAST
    Repeati1655 – 167521YD 5Add
    BLAST
    Repeati1845 – 186420YD 6Add
    BLAST
    Repeati1865 – 188521YD 7Add
    BLAST
    Repeati1886 – 190419YD 8Add
    BLAST
    Repeati1905 – 192521YD 9Add
    BLAST
    Repeati1933 – 194917YD 10Add
    BLAST
    Repeati1950 – 196920YD 11Add
    BLAST
    Repeati1970 – 198920YD 12Add
    BLAST
    Repeati1992 – 201221YD 13Add
    BLAST
    Repeati2015 – 203521YD 14Add
    BLAST
    Repeati2085 – 210521YD 15Add
    BLAST
    Repeati2113 – 213321YD 16Add
    BLAST
    Repeati2153 – 217321YD 17Add
    BLAST
    Repeati2174 – 219421YD 18Add
    BLAST
    Repeati2196 – 221621YD 19Add
    BLAST
    Repeati2228 – 224821YD 20Add
    BLAST
    Repeati2250 – 227021YD 21Add
    BLAST
    Repeati2296 – 231318YD 22Add
    BLAST
    Repeati2314 – 233724YD 23Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi62 – 654Nuclear localization signal (NLS)By similarity
    Motifi290 – 2978Required for interaction with SORBS1 (Ten-1 ICD form)By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 2009Poly-Pro

    Domaini

    EGF-like domains 2 and 5 which have an odd number of cysteines might enable the formation of intermolecular disulfide bonds.
    Cytoplasmic proline-rich regions could serve as docking domains for intracellular SH3-containing proteins.

    Sequence similaritiesi

    Belongs to the tenascin family. Teneurin subfamily.Curated
    Contains 8 EGF-like domains.PROSITE-ProRule annotation
    Contains 5 NHL repeats.Curated
    Contains 1 teneurin N-terminal domain.PROSITE-ProRule annotation
    Contains 23 YD repeats.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG323120.
    HOGENOMiHOG000231701.
    HOVERGENiHBG080306.
    InParanoidiQ9UKZ4.
    OMAiIAYWMTI.
    OrthoDBiEOG7H791C.
    PhylomeDBiQ9UKZ4.
    TreeFamiTF316833.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009471. Ten_N.
    IPR027688. TENM1.
    IPR028916. Tox-GHH_dom.
    IPR006530. YD.
    [Graphical view]
    PANTHERiPTHR11219:SF7. PTHR11219:SF7. 1 hit.
    PfamiPF12661. hEGF. 1 hit.
    PF06484. Ten_N. 2 hits.
    PF15636. Tox-GHH. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 6 hits.
    [Graphical view]
    TIGRFAMsiTIGR01643. YD_repeat_2x. 3 hits.
    PROSITEiPS00022. EGF_1. 8 hits.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 5 hits.
    PS51361. TENEURIN_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKZ4-1) [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

    MEQTDCKPYQ PLPKVKHEMD LAYTSSSDES EDGRKPRQSY NSRETLHEYN     50
    QELRMNYNSQ SRKRKEVEKS TQEMEFCETS HTLCSGYQTD MHSVSRHGYQ 100
    LEMGSDVDTE TEGAASPDHA LRMWIRGMKS EHSSCLSSRA NSALSLTDTD 150
    HERKSDGENG FKFSPVCCDM EAQAGSTQDV QSSPHNQFTF RPLPPPPPPP 200
    HACTCARKPP PAADSLQRRS MTTRSQPSPA APAPPTSTQD SVHLHNSWVL 250
    NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF 300
    SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ 350
    PVEGELYANG VSKGNRGTES MDTTYSPIGG KVSDKSEKKV FQKGRAIDTG 400
    EVDIGAQVMQ TIPPGLFWRF QITIHHPIYL KFNISLAKDS LLGIYGRRNI 450
    PPTHTQFDFV KLMDGKQLVK QDSKGSDDTQ HSPRNLILTS LQETGFIEYM 500
    DQGPWYLAFY NDGKKMEQVF VLTTAIEIMD DCSTNCNGNG ECISGHCHCF 550
    PGFLGPDCAR DSCPVLCGGN GEYEKGHCVC RHGWKGPECD VPEEQCIDPT 600
    CFGHGTCIMG VCICVPGYKG EICEEEDCLD PMCSNHGICV KGECHCSTGW 650
    GGVNCETPLP VCQEQCSGHG TFLLDAGVCS CDPKWTGSDC STELCTMECG 700
    SHGVCSRGIC QCEEGWVGPT CEERSCHSHC TEHGQCKDGK CECSPGWEGD 750
    HCTIAHYLDA VRDGCPGLCF GNGRCTLDQN GWHCVCQVGW SGTGCNVVME 800
    MLCGDNLDND GDGLTDCVDP DCCQQSNCYI SPLCQGSPDP LDLIQQSQTL 850
    FSQHTSRLFY DRIKFLIGKD STHVIPPEVS FDSRRACVIR GQVVAIDGTP 900
    LVGVNVSFLH HSDYGFTISR QDGSFDLVAI GGISVILIFD RSPFLPEKRT 950
    LWLPWNQFIV VEKVTMQRVV SDPPSCDISN FISPNPIVLP SPLTSFGGSC 1000
    PERGTIVPEL QVVQEEIPIP SSFVRLSYLS SRTPGYKTLL RILLTHSTIP 1050
    VGMIKVHLTV AVEGRLTQKW FPAAINLVYT FAWNKTDIYG QKVWGLAEAL 1100
    VSVGYEYETC PDFILWEQRT VVLQGFEMDA SNLGGWSLNK HHILNPQSGI 1150
    IHKGNGENMF ISQQPPVIST IMGNGHQRSV ACTNCNGPAH NNKLFAPVAL 1200
    ASGPDGSVYV GDFNFVRRIF PSGNSVSILE LSTSPAHKYY LAMDPVSESL 1250
    YLSDTNTRKV YKLKSLVETK DLSKNFEVVA GTGDQCLPFD QSHCGDGGRA 1300
    SEASLNSPRG ITVDRHGFIY FVDGTMIRKI DENAVITTVI GSNGLTSTQP 1350
    LSCDSGMDIT QVRLEWPTDL AVNPMDNSLY VLDNNIVLQI SENRRVRIIA 1400
    GRPIHCQVPG IDHFLVSKVA IHSTLESARA ISVSHSGLLF IAETDERKVN 1450
    RIQQVTTNGE IYIIAGAPTD CDCKIDPNCD CFSGDGGYAK DAKMKAPSSL 1500
    AVSPDGTLYV ADLGNVRIRT ISRNQAHLND MNIYEIASPA DQELYQFTVN 1550
    GTHLHTLNLI TRDYVYNFTY NSEGDLGAIT SSNGNSVHIR RDAGGMPLWL 1600
    VVPGGQVYWL TISSNGVLKR VSAQGYNLAL MTYPGNTGLL ATKSNENGWT 1650
    TVYEYDPEGH LTNATFPTGE VSSFHSDLEK LTKVELDTSN RENVLMSTNL 1700
    TATSTIYILK QENTQSTYRV NPDGSLRVTF ASGMEIGLSS EPHILAGAVN 1750
    PTLGKCNISL PGEHNANLIE WRQRKEQNKG NVSAFERRLR AHNRNLLSID 1800
    FDHITRTGKI YDDHRKFTLR ILYDQTGRPI LWSPVSRYNE VNITYSPSGL 1850
    VTFIQRGTWN EKMEYDQSGK IISRTWADGK IWSYTYLEKS VMLLLHSQRR 1900
    YIFEYDQPDC LLSVTMPSMV RHSLQTMLSV GYYRNIYTPP DSSTSFIQDY 1950
    SRDGRLLQTL HLGTGRRVLY KYTKQARLSE VLYDTTQVTL TYEESSGVIK 2000
    TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD YSYNNFRVTS 2050
    MQAVINETPL PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK 2100
    IFSANGQVIE VQYEILKAIA YWMTIQYDNV GRMVICDIRV GVDANITRYF 2150
    YEYDADGQLQ TVSVNDKTQW RYSYDLNGNI NLLSHGKSAR LTPLRYDLRD 2200
    RITRLGEIQY KMDEDGFLRQ RGNDIFEYNS NGLLQKAYNK ASGWTVQYYY 2250
    DGLGRRVASK SSLGQHLQFF YADLTNPIRV THLYNHTSSE ITSLYYDLQG 2300
    HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT PYGDIYHDTY 2350
    PDFQVIIGFH GGLYDFLTKL VHLGQRDYDV VAGRWTTPNH HIWKQLNLLP 2400
    KPFNLYSFEN NYPVGKIQDV AKYTTDIRSW LELFGFQLHN VLPGFPKPEL 2450
    ENLELTYELL RLQTKTQEWD PGKTILGIQC ELQKQLRNFI SLDQLPMTPR 2500
    YNDGRCLEGG KQPRFAAVPS VFGKGIKFAI KDGIVTADII GVANEDSRRL 2550
    AAILNNAHYL ENLHFTIEGR DTHYFIKLGS LEEDLVLIGN TGGRRILENG 2600
    VNVTVSQMTS VLNGRTRRFA DIQLQHGALC FNIRYGTTVE EEKNHVLEIA 2650
    RQRAVAQAWT KEQRRLQEGE EGIRAWTEGE KQQLLSTGRV QGYDGYFVLS 2700
    VEQYLELSDS ANNIHFMRQS EIGRR 2725
    Length:2,725
    Mass (Da):305,011
    Last modified:October 31, 2006 - v2
    Checksum:i70F5C22BF33B5BB7
    GO
    Isoform 2 (identifier: Q9UKZ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1231-1231: L → LRNRDTRH

    Note: No experimental confirmation available.

    Show »
    Length:2,732
    Mass (Da):305,947
    Checksum:i7EA5C0EC5B692B15
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611F → S in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti1135 – 11351G → D in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti1628 – 16281L → P in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti1908 – 19081P → S in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti2133 – 21375MVICD → HGNMC in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti2179 – 21791N → D in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti2271 – 22755YADLT → VDATA in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti2388 – 23892PN → AY in AAF04723. (PubMed:10556288)Curated
    Sequence conflicti2611 – 26111V → L in AAF04723. (PubMed:10556288)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401Y → H.
    Corresponds to variant rs36065191 [ dbSNP | Ensembl ].
    VAR_053792
    Natural varianti342 – 3421L → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036596
    Natural varianti371 – 3711M → T.
    Corresponds to variant rs2213591 [ dbSNP | Ensembl ].
    VAR_053793
    Natural varianti632 – 6321M → V.
    Corresponds to variant rs16999334 [ dbSNP | Ensembl ].
    VAR_053794
    Natural varianti641 – 6411K → E.
    Corresponds to variant rs6649271 [ dbSNP | Ensembl ].
    VAR_053795
    Natural varianti1216 – 12161V → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036597
    Natural varianti1482 – 14821F → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036598
    Natural varianti2235 – 22351Q → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036599
    Natural varianti2396 – 23961L → F in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036600

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1231 – 12311L → LRNRDTRH in isoform 2. 1 PublicationVSP_043356

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF100772 mRNA. Translation: AAF04723.1.
    AL022718
    , AL023878, AL031075, Z81008, Z83823, Z85995 Genomic DNA. Translation: CAI42154.1.
    AL023878
    , AL022718, AL031075, Z81008, Z83823, Z85995 Genomic DNA. Translation: CAI42975.1.
    AL031075
    , AL022718, AL023878, Z81008, Z83823, Z85995 Genomic DNA. Translation: CAI43065.1.
    Z81008
    , Z83823, Z85995, AL022718, AL023878, AL031075 Genomic DNA. Translation: CAI42710.1.
    Z83823
    , Z81008, Z85995, AL022718, AL023878, AL031075 Genomic DNA. Translation: CAI42742.1.
    Z85995
    , Z81008, Z83823, AL022718, AL023878, AL031075 Genomic DNA. Translation: CAI42721.1.
    BC140783 mRNA. Translation: AAI40784.1.
    CCDSiCCDS14609.1. [Q9UKZ4-1]
    CCDS55488.1. [Q9UKZ4-2]
    RefSeqiNP_001156750.1. NM_001163278.1. [Q9UKZ4-2]
    NP_001156751.1. NM_001163279.1.
    NP_055068.2. NM_014253.3. [Q9UKZ4-1]
    UniGeneiHs.23796.
    Hs.744536.

    Genome annotation databases

    EnsembliENST00000371130; ENSP00000360171; ENSG00000009694. [Q9UKZ4-1]
    ENST00000422452; ENSP00000403954; ENSG00000009694. [Q9UKZ4-2]
    GeneIDi10178.
    KEGGihsa:10178.
    UCSCiuc004euj.3. human. [Q9UKZ4-1]
    uc010nqy.3. human. [Q9UKZ4-2]

    Polymorphism databases

    DMDMi117949792.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF100772 mRNA. Translation: AAF04723.1 .
    AL022718
    , AL023878 , AL031075 , Z81008 , Z83823 , Z85995 Genomic DNA. Translation: CAI42154.1 .
    AL023878
    , AL022718 , AL031075 , Z81008 , Z83823 , Z85995 Genomic DNA. Translation: CAI42975.1 .
    AL031075
    , AL022718 , AL023878 , Z81008 , Z83823 , Z85995 Genomic DNA. Translation: CAI43065.1 .
    Z81008
    , Z83823 , Z85995 , AL022718 , AL023878 , AL031075 Genomic DNA. Translation: CAI42710.1 .
    Z83823
    , Z81008 , Z85995 , AL022718 , AL023878 , AL031075 Genomic DNA. Translation: CAI42742.1 .
    Z85995
    , Z81008 , Z83823 , AL022718 , AL023878 , AL031075 Genomic DNA. Translation: CAI42721.1 .
    BC140783 mRNA. Translation: AAI40784.1 .
    CCDSi CCDS14609.1. [Q9UKZ4-1 ]
    CCDS55488.1. [Q9UKZ4-2 ]
    RefSeqi NP_001156750.1. NM_001163278.1. [Q9UKZ4-2 ]
    NP_001156751.1. NM_001163279.1.
    NP_055068.2. NM_014253.3. [Q9UKZ4-1 ]
    UniGenei Hs.23796.
    Hs.744536.

    3D structure databases

    ProteinModelPortali Q9UKZ4.
    SMRi Q9UKZ4. Positions 504-841, 1305-1334, 1364-1391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115477. 2 interactions.
    STRINGi 9606.ENSP00000360171.

    PTM databases

    PhosphoSitei Q9UKZ4.

    Polymorphism databases

    DMDMi 117949792.

    Proteomic databases

    PaxDbi Q9UKZ4.
    PRIDEi Q9UKZ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371130 ; ENSP00000360171 ; ENSG00000009694 . [Q9UKZ4-1 ]
    ENST00000422452 ; ENSP00000403954 ; ENSG00000009694 . [Q9UKZ4-2 ]
    GeneIDi 10178.
    KEGGi hsa:10178.
    UCSCi uc004euj.3. human. [Q9UKZ4-1 ]
    uc010nqy.3. human. [Q9UKZ4-2 ]

    Organism-specific databases

    CTDi 10178.
    GeneCardsi GC0XM123511.
    HGNCi HGNC:8117. TENM1.
    HPAi HPA002848.
    MIMi 300588. gene.
    neXtProti NX_Q9UKZ4.
    PharmGKBi PA31904.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323120.
    HOGENOMi HOG000231701.
    HOVERGENi HBG080306.
    InParanoidi Q9UKZ4.
    OMAi IAYWMTI.
    OrthoDBi EOG7H791C.
    PhylomeDBi Q9UKZ4.
    TreeFami TF316833.

    Enzyme and pathway databases

    SignaLinki Q9UKZ4.

    Miscellaneous databases

    GeneWikii ODZ1.
    GenomeRNAii 10178.
    NextBioi 38530.
    PROi Q9UKZ4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKZ4.
    Bgeei Q9UKZ4.
    CleanExi HS_ODZ1.
    Genevestigatori Q9UKZ4.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009471. Ten_N.
    IPR027688. TENM1.
    IPR028916. Tox-GHH_dom.
    IPR006530. YD.
    [Graphical view ]
    PANTHERi PTHR11219:SF7. PTHR11219:SF7. 1 hit.
    Pfami PF12661. hEGF. 1 hit.
    PF06484. Ten_N. 2 hits.
    PF15636. Tox-GHH. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 6 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01643. YD_repeat_2x. 3 hits.
    PROSITEi PS00022. EGF_1. 8 hits.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 5 hits.
    PS51361. TENEURIN_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Epstein-Barr virus-negative boys with non-Hodgkin lymphoma are mutated in the SH2D1A gene, as are patients with X-linked lymphoproliferative disease (XLP)."
      Brandau O., Schuster V., Weiss M., Hellebrand H., Fink F.M., Kreczy A., Friedrich W., Strahm B., Niemeyer C., Belohradsky B.H., Meindl A.
      Hum. Mol. Genet. 8:2407-2413(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 2).
      Tissue: Brain.
    4. "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain."
      Minet A.D., Rubin B.P., Tucker R.P., Baumgartner S., Chiquet-Ehrismann R.
      J. Cell Sci. 112:2019-2032(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-342; ILE-1216; VAL-1482; HIS-2235 AND PHE-2396.

    Entry informationi

    Entry nameiTEN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKZ4
    Secondary accession number(s): B2RTR5, Q5JZ17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 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

    Miscellaneous

    Teneurin C-terminal-associated peptide: Binds to the plasma membrane and may be internalized by a receptor- and caveolae-mediated endocytosis manner to reach cytosolic compartments in a dynamin-dependent manner.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3