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Q9UKZ4

- TEN1_HUMAN

UniProt

Q9UKZ4 - TEN1_HUMAN

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Protein

Teneurin-1

Gene

TENM1

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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 324324CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei325 – 34521HelicalSequence AnalysisAdd
BLAST
Topological domaini346 – 27252380ExtracellularSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

BgeeiQ9UKZ4.
CleanExiHS_ODZ1.
ExpressionAtlasiQ9UKZ4. baseline and differential.
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 531-841, 1364-1391.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119131.
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

        10         20         30         40         50
MEQTDCKPYQ PLPKVKHEMD LAYTSSSDES EDGRKPRQSY NSRETLHEYN
60 70 80 90 100
QELRMNYNSQ SRKRKEVEKS TQEMEFCETS HTLCSGYQTD MHSVSRHGYQ
110 120 130 140 150
LEMGSDVDTE TEGAASPDHA LRMWIRGMKS EHSSCLSSRA NSALSLTDTD
160 170 180 190 200
HERKSDGENG FKFSPVCCDM EAQAGSTQDV QSSPHNQFTF RPLPPPPPPP
210 220 230 240 250
HACTCARKPP PAADSLQRRS MTTRSQPSPA APAPPTSTQD SVHLHNSWVL
260 270 280 290 300
NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF
310 320 330 340 350
SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ
360 370 380 390 400
PVEGELYANG VSKGNRGTES MDTTYSPIGG KVSDKSEKKV FQKGRAIDTG
410 420 430 440 450
EVDIGAQVMQ TIPPGLFWRF QITIHHPIYL KFNISLAKDS LLGIYGRRNI
460 470 480 490 500
PPTHTQFDFV KLMDGKQLVK QDSKGSDDTQ HSPRNLILTS LQETGFIEYM
510 520 530 540 550
DQGPWYLAFY NDGKKMEQVF VLTTAIEIMD DCSTNCNGNG ECISGHCHCF
560 570 580 590 600
PGFLGPDCAR DSCPVLCGGN GEYEKGHCVC RHGWKGPECD VPEEQCIDPT
610 620 630 640 650
CFGHGTCIMG VCICVPGYKG EICEEEDCLD PMCSNHGICV KGECHCSTGW
660 670 680 690 700
GGVNCETPLP VCQEQCSGHG TFLLDAGVCS CDPKWTGSDC STELCTMECG
710 720 730 740 750
SHGVCSRGIC QCEEGWVGPT CEERSCHSHC TEHGQCKDGK CECSPGWEGD
760 770 780 790 800
HCTIAHYLDA VRDGCPGLCF GNGRCTLDQN GWHCVCQVGW SGTGCNVVME
810 820 830 840 850
MLCGDNLDND GDGLTDCVDP DCCQQSNCYI SPLCQGSPDP LDLIQQSQTL
860 870 880 890 900
FSQHTSRLFY DRIKFLIGKD STHVIPPEVS FDSRRACVIR GQVVAIDGTP
910 920 930 940 950
LVGVNVSFLH HSDYGFTISR QDGSFDLVAI GGISVILIFD RSPFLPEKRT
960 970 980 990 1000
LWLPWNQFIV VEKVTMQRVV SDPPSCDISN FISPNPIVLP SPLTSFGGSC
1010 1020 1030 1040 1050
PERGTIVPEL QVVQEEIPIP SSFVRLSYLS SRTPGYKTLL RILLTHSTIP
1060 1070 1080 1090 1100
VGMIKVHLTV AVEGRLTQKW FPAAINLVYT FAWNKTDIYG QKVWGLAEAL
1110 1120 1130 1140 1150
VSVGYEYETC PDFILWEQRT VVLQGFEMDA SNLGGWSLNK HHILNPQSGI
1160 1170 1180 1190 1200
IHKGNGENMF ISQQPPVIST IMGNGHQRSV ACTNCNGPAH NNKLFAPVAL
1210 1220 1230 1240 1250
ASGPDGSVYV GDFNFVRRIF PSGNSVSILE LSTSPAHKYY LAMDPVSESL
1260 1270 1280 1290 1300
YLSDTNTRKV YKLKSLVETK DLSKNFEVVA GTGDQCLPFD QSHCGDGGRA
1310 1320 1330 1340 1350
SEASLNSPRG ITVDRHGFIY FVDGTMIRKI DENAVITTVI GSNGLTSTQP
1360 1370 1380 1390 1400
LSCDSGMDIT QVRLEWPTDL AVNPMDNSLY VLDNNIVLQI SENRRVRIIA
1410 1420 1430 1440 1450
GRPIHCQVPG IDHFLVSKVA IHSTLESARA ISVSHSGLLF IAETDERKVN
1460 1470 1480 1490 1500
RIQQVTTNGE IYIIAGAPTD CDCKIDPNCD CFSGDGGYAK DAKMKAPSSL
1510 1520 1530 1540 1550
AVSPDGTLYV ADLGNVRIRT ISRNQAHLND MNIYEIASPA DQELYQFTVN
1560 1570 1580 1590 1600
GTHLHTLNLI TRDYVYNFTY NSEGDLGAIT SSNGNSVHIR RDAGGMPLWL
1610 1620 1630 1640 1650
VVPGGQVYWL TISSNGVLKR VSAQGYNLAL MTYPGNTGLL ATKSNENGWT
1660 1670 1680 1690 1700
TVYEYDPEGH LTNATFPTGE VSSFHSDLEK LTKVELDTSN RENVLMSTNL
1710 1720 1730 1740 1750
TATSTIYILK QENTQSTYRV NPDGSLRVTF ASGMEIGLSS EPHILAGAVN
1760 1770 1780 1790 1800
PTLGKCNISL PGEHNANLIE WRQRKEQNKG NVSAFERRLR AHNRNLLSID
1810 1820 1830 1840 1850
FDHITRTGKI YDDHRKFTLR ILYDQTGRPI LWSPVSRYNE VNITYSPSGL
1860 1870 1880 1890 1900
VTFIQRGTWN EKMEYDQSGK IISRTWADGK IWSYTYLEKS VMLLLHSQRR
1910 1920 1930 1940 1950
YIFEYDQPDC LLSVTMPSMV RHSLQTMLSV GYYRNIYTPP DSSTSFIQDY
1960 1970 1980 1990 2000
SRDGRLLQTL HLGTGRRVLY KYTKQARLSE VLYDTTQVTL TYEESSGVIK
2010 2020 2030 2040 2050
TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD YSYNNFRVTS
2060 2070 2080 2090 2100
MQAVINETPL PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK
2110 2120 2130 2140 2150
IFSANGQVIE VQYEILKAIA YWMTIQYDNV GRMVICDIRV GVDANITRYF
2160 2170 2180 2190 2200
YEYDADGQLQ TVSVNDKTQW RYSYDLNGNI NLLSHGKSAR LTPLRYDLRD
2210 2220 2230 2240 2250
RITRLGEIQY KMDEDGFLRQ RGNDIFEYNS NGLLQKAYNK ASGWTVQYYY
2260 2270 2280 2290 2300
DGLGRRVASK SSLGQHLQFF YADLTNPIRV THLYNHTSSE ITSLYYDLQG
2310 2320 2330 2340 2350
HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT PYGDIYHDTY
2360 2370 2380 2390 2400
PDFQVIIGFH GGLYDFLTKL VHLGQRDYDV VAGRWTTPNH HIWKQLNLLP
2410 2420 2430 2440 2450
KPFNLYSFEN NYPVGKIQDV AKYTTDIRSW LELFGFQLHN VLPGFPKPEL
2460 2470 2480 2490 2500
ENLELTYELL RLQTKTQEWD PGKTILGIQC ELQKQLRNFI SLDQLPMTPR
2510 2520 2530 2540 2550
YNDGRCLEGG KQPRFAAVPS VFGKGIKFAI KDGIVTADII GVANEDSRRL
2560 2570 2580 2590 2600
AAILNNAHYL ENLHFTIEGR DTHYFIKLGS LEEDLVLIGN TGGRRILENG
2610 2620 2630 2640 2650
VNVTVSQMTS VLNGRTRRFA DIQLQHGALC FNIRYGTTVE EEKNHVLEIA
2660 2670 2680 2690 2700
RQRAVAQAWT KEQRRLQEGE EGIRAWTEGE KQQLLSTGRV QGYDGYFVLS
2710 2720
VEQYLELSDS ANNIHFMRQS EIGRR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 531-841, 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.
GeneTreei ENSGT00760000119131.
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

Bgeei Q9UKZ4.
CleanExi HS_ODZ1.
ExpressionAtlasi Q9UKZ4. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 109 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