SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UKZ4

- TEN1_HUMAN

UniProt

Q9UKZ4 - TEN1_HUMAN

(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)

Protein
Teneurin-1
Gene
TENM1, ODZ1, TNM1
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.
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.
Ten-1 intracellular domain: Induces gene transcription activation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2595 – 25962Cleavage Inferred

GO - Molecular functioni

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

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 MAP kinase activity Source: UniProtKB
  6. positive regulation of actin filament polymerization Source: UniProtKB
  7. positive regulation of filopodium assembly Source: UniProtKB
  8. positive regulation of intracellular protein transport 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

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 324324Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei325 – 34521Helical; Reviewed prediction
Add
BLAST
Topological domaini346 – 27252380Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. extracellular region Source: ProtInc
  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-1
PRO_0000259498Add
BLAST
Chaini1 – ?Ten-1 intracellular domain By similarityPRO_0000421005
Chaini2596 – 2725130Teneurin C-terminal-associated peptide By similarity
PRO_0000421006Add
BLAST

Amino acid modifications

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

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.

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.

Protein-protein interaction databases

BioGridi115477. 2 interactions.
STRINGi9606.ENSP00000360171.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Contains 8 EGF-like domains.
Contains 5 NHL repeats.
Contains 23 YD repeats.

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

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.
VSP_043356

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611F → S in AAF04723. 1 Publication
Sequence conflicti1135 – 11351G → D in AAF04723. 1 Publication
Sequence conflicti1628 – 16281L → P in AAF04723. 1 Publication
Sequence conflicti1908 – 19081P → S in AAF04723. 1 Publication
Sequence conflicti2133 – 21375MVICD → HGNMC in AAF04723. 1 Publication
Sequence conflicti2179 – 21791N → D in AAF04723. 1 Publication
Sequence conflicti2271 – 22755YADLT → VDATA in AAF04723. 1 Publication
Sequence conflicti2388 – 23892PN → AY in AAF04723. 1 Publication
Sequence conflicti2611 – 26111V → L in AAF04723. 1 Publication

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...

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

« 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: July 9, 2014
This is version 106 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

Similar proteinsi