Q9UKZ4 (TEN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Teneurin-1
Short name=Ten-1

Alternative name(s):
Protein Odd Oz/ten-m homolog 1
Tenascin-M1
Short name=Ten-m1

Gene names

Name:	ODZ1
Synonyms:	TNM1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2725 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as a cellular signal transducer.
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Membrane; Single-pass type II membrane protein Probable.
Tissue specificity	Expressed in fetal brain. Ref.3
Domain	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 similarities	Belongs to the tenascin family. Teneurin subfamily. Contains 8 EGF-like domains. Contains 5 NHL repeats. Contains 1 teneurin N-terminal domain. Contains 23 YD repeats.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	immune response Traceable author statement. Source: ProtInc negative regulation of cell proliferation Traceable author statement. Source: ProtInc nervous system development Traceable author statement. Source: ProtInc signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Traceable author statement. Source: ProtInc integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	heparin binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2725	2725	Teneurin-1		PRO_0000259498
Regions
	Topological domain	1 – 324	324	Cytoplasmic Potential
	Transmembrane	325 – 345	21	Helical; Potential
	Topological domain	346 – 2725	2380	Extracellular Potential
	Domain	1 – 318	318	Teneurin N-terminal
	Domain	528 – 559	32	EGF-like 1
	Domain	560 – 591	32	EGF-like 2
	Domain	592 – 624	33	EGF-like 3
	Domain	625 – 657	33	EGF-like 4
	Domain	658 – 691	34	EGF-like 5
	Domain	692 – 721	30	EGF-like 6
	Domain	722 – 753	32	EGF-like 7
	Domain	761 – 796	36	EGF-like 8
	Repeat	1194 – 1219	26	NHL 1
	Repeat	1292 – 1336	45	NHL 2
	Repeat	1351 – 1402	52	NHL 3
	Repeat	1414 – 1458	45	NHL 4
	Repeat	1481 – 1524	44	NHL 5
	Repeat	1534 – 1553	20	YD 1
	Repeat	1570 – 1590	21	YD 2
	Repeat	1608 – 1632	25	YD 3
	Repeat	1633 – 1654	22	YD 4
	Repeat	1655 – 1675	21	YD 5
	Repeat	1845 – 1864	20	YD 6
	Repeat	1865 – 1885	21	YD 7
	Repeat	1886 – 1904	19	YD 8
	Repeat	1905 – 1925	21	YD 9
	Repeat	1933 – 1949	17	YD 10
	Repeat	1950 – 1969	20	YD 11
	Repeat	1970 – 1989	20	YD 12
	Repeat	1992 – 2012	21	YD 13
	Repeat	2015 – 2035	21	YD 14
	Repeat	2085 – 2105	21	YD 15
	Repeat	2113 – 2133	21	YD 16
	Repeat	2153 – 2173	21	YD 17
	Repeat	2174 – 2194	21	YD 18
	Repeat	2196 – 2216	21	YD 19
	Repeat	2228 – 2248	21	YD 20
	Repeat	2250 – 2270	21	YD 21
	Repeat	2296 – 2313	18	YD 22
	Repeat	2314 – 2337	24	YD 23
	Compositional bias	192 – 200	9	Poly-Pro
Amino acid modifications
	Modified residue	2580	1	Phosphoserine Ref.4
	Glycosylation	433	1	N-linked (GlcNAc...) Potential
	Glycosylation	905	1	N-linked (GlcNAc...) Potential
	Glycosylation	1084	1	N-linked (GlcNAc...) Potential
	Glycosylation	1550	1	N-linked (GlcNAc...) Potential
	Glycosylation	1567	1	N-linked (GlcNAc...) Potential
	Glycosylation	1663	1	N-linked (GlcNAc...) Potential
	Glycosylation	1699	1	N-linked (GlcNAc...) Potential
	Glycosylation	1757	1	N-linked (GlcNAc...) Potential
	Glycosylation	1781	1	N-linked (GlcNAc...) Potential
	Glycosylation	1842	1	N-linked (GlcNAc...) Potential
	Glycosylation	2145	1	N-linked (GlcNAc...) Potential
	Glycosylation	2285	1	N-linked (GlcNAc...) Potential
	Glycosylation	2602	1	N-linked (GlcNAc...) Potential
	Disulfide bond	532 ↔ 542		By similarity
	Disulfide bond	536 ↔ 547		By similarity
	Disulfide bond	549 ↔ 558		By similarity
	Disulfide bond	567 ↔ 578		By similarity
	Disulfide bond	580 ↔ 589		By similarity
	Disulfide bond	596 ↔ 607		By similarity
	Disulfide bond	601 ↔ 612		By similarity
	Disulfide bond	614 ↔ 623		By similarity
	Disulfide bond	628 ↔ 639		By similarity
	Disulfide bond	633 ↔ 644		By similarity
	Disulfide bond	646 ↔ 655		By similarity
	Disulfide bond	666 ↔ 679		By similarity
	Disulfide bond	681 ↔ 690		By similarity
	Disulfide bond	695 ↔ 705		By similarity
	Disulfide bond	699 ↔ 710		By similarity
	Disulfide bond	712 ↔ 721		By similarity
	Disulfide bond	726 ↔ 736		By similarity
	Disulfide bond	730 ↔ 741		By similarity
	Disulfide bond	743 ↔ 752		By similarity
	Disulfide bond	765 ↔ 775		By similarity
	Disulfide bond	769 ↔ 784		By similarity
	Disulfide bond	786 ↔ 795		By similarity
Natural variations
	Natural variant	40	1	Y → H. Corresponds to variant rs36065191 [ dbSNP | Ensembl ].		VAR_053792
	Natural variant	342	1	L → F in a breast cancer sample; somatic mutation. Ref.5		VAR_036596
	Natural variant	371	1	M → T. Corresponds to variant rs2213591 [ dbSNP | Ensembl ].		VAR_053793
	Natural variant	632	1	M → V. Corresponds to variant rs16999334 [ dbSNP | Ensembl ].		VAR_053794
	Natural variant	641	1	K → E. Corresponds to variant rs6649271 [ dbSNP | Ensembl ].		VAR_053795
	Natural variant	1216	1	V → I in a breast cancer sample; somatic mutation. Ref.5		VAR_036597
	Natural variant	1482	1	F → V in a colorectal cancer sample; somatic mutation. Ref.5		VAR_036598
	Natural variant	2235	1	Q → H in a breast cancer sample; somatic mutation. Ref.5		VAR_036599
	Natural variant	2396	1	L → F in a colorectal cancer sample; somatic mutation. Ref.5		VAR_036600
Experimental info
	Sequence conflict	261	1	F → S in AAF04723. Ref.1
	Sequence conflict	1135	1	G → D in AAF04723. Ref.1
	Sequence conflict	1628	1	L → P in AAF04723. Ref.1
	Sequence conflict	1908	1	P → S in AAF04723. Ref.1
	Sequence conflict	2133 – 2137	5	MVICD → HGNMC in AAF04723. Ref.1
	Sequence conflict	2179	1	N → D in AAF04723. Ref.1
	Sequence conflict	2271 – 2275	5	YADLT → VDATA in AAF04723. Ref.1
	Sequence conflict	2388 – 2389	2	PN → AY in AAF04723. Ref.1
	Sequence conflict	2611	1	V → L in AAF04723. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UKZ4 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 70F5C22BF33B5BB7	FASTA	2,725	305,011
	10 20 30 40 50 60 MEQTDCKPYQ PLPKVKHEMD LAYTSSSDES EDGRKPRQSY NSRETLHEYN QELRMNYNSQ 70 80 90 100 110 120 SRKRKEVEKS TQEMEFCETS HTLCSGYQTD MHSVSRHGYQ LEMGSDVDTE TEGAASPDHA 130 140 150 160 170 180 LRMWIRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGENG FKFSPVCCDM EAQAGSTQDV 190 200 210 220 230 240 QSSPHNQFTF RPLPPPPPPP HACTCARKPP PAADSLQRRS MTTRSQPSPA APAPPTSTQD 250 260 270 280 290 300 SVHLHNSWVL NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF 310 320 330 340 350 360 SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ PVEGELYANG 370 380 390 400 410 420 VSKGNRGTES MDTTYSPIGG KVSDKSEKKV FQKGRAIDTG EVDIGAQVMQ TIPPGLFWRF 430 440 450 460 470 480 QITIHHPIYL KFNISLAKDS LLGIYGRRNI PPTHTQFDFV KLMDGKQLVK QDSKGSDDTQ 490 500 510 520 530 540 HSPRNLILTS LQETGFIEYM DQGPWYLAFY NDGKKMEQVF VLTTAIEIMD DCSTNCNGNG 550 560 570 580 590 600 ECISGHCHCF PGFLGPDCAR DSCPVLCGGN GEYEKGHCVC RHGWKGPECD VPEEQCIDPT 610 620 630 640 650 660 CFGHGTCIMG VCICVPGYKG EICEEEDCLD PMCSNHGICV KGECHCSTGW GGVNCETPLP 670 680 690 700 710 720 VCQEQCSGHG TFLLDAGVCS CDPKWTGSDC STELCTMECG SHGVCSRGIC QCEEGWVGPT 730 740 750 760 770 780 CEERSCHSHC TEHGQCKDGK CECSPGWEGD HCTIAHYLDA VRDGCPGLCF GNGRCTLDQN 790 800 810 820 830 840 GWHCVCQVGW SGTGCNVVME MLCGDNLDND GDGLTDCVDP DCCQQSNCYI SPLCQGSPDP 850 860 870 880 890 900 LDLIQQSQTL FSQHTSRLFY DRIKFLIGKD STHVIPPEVS FDSRRACVIR GQVVAIDGTP 910 920 930 940 950 960 LVGVNVSFLH HSDYGFTISR QDGSFDLVAI GGISVILIFD RSPFLPEKRT LWLPWNQFIV 970 980 990 1000 1010 1020 VEKVTMQRVV SDPPSCDISN FISPNPIVLP SPLTSFGGSC PERGTIVPEL QVVQEEIPIP 1030 1040 1050 1060 1070 1080 SSFVRLSYLS SRTPGYKTLL RILLTHSTIP VGMIKVHLTV AVEGRLTQKW FPAAINLVYT 1090 1100 1110 1120 1130 1140 FAWNKTDIYG QKVWGLAEAL VSVGYEYETC PDFILWEQRT VVLQGFEMDA SNLGGWSLNK 1150 1160 1170 1180 1190 1200 HHILNPQSGI IHKGNGENMF ISQQPPVIST IMGNGHQRSV ACTNCNGPAH NNKLFAPVAL 1210 1220 1230 1240 1250 1260 ASGPDGSVYV GDFNFVRRIF PSGNSVSILE LSTSPAHKYY LAMDPVSESL YLSDTNTRKV 1270 1280 1290 1300 1310 1320 YKLKSLVETK DLSKNFEVVA GTGDQCLPFD QSHCGDGGRA SEASLNSPRG ITVDRHGFIY 1330 1340 1350 1360 1370 1380 FVDGTMIRKI DENAVITTVI GSNGLTSTQP LSCDSGMDIT QVRLEWPTDL AVNPMDNSLY 1390 1400 1410 1420 1430 1440 VLDNNIVLQI SENRRVRIIA GRPIHCQVPG IDHFLVSKVA IHSTLESARA ISVSHSGLLF 1450 1460 1470 1480 1490 1500 IAETDERKVN RIQQVTTNGE IYIIAGAPTD CDCKIDPNCD CFSGDGGYAK DAKMKAPSSL 1510 1520 1530 1540 1550 1560 AVSPDGTLYV ADLGNVRIRT ISRNQAHLND MNIYEIASPA DQELYQFTVN GTHLHTLNLI 1570 1580 1590 1600 1610 1620 TRDYVYNFTY NSEGDLGAIT SSNGNSVHIR RDAGGMPLWL VVPGGQVYWL TISSNGVLKR 1630 1640 1650 1660 1670 1680 VSAQGYNLAL MTYPGNTGLL ATKSNENGWT TVYEYDPEGH LTNATFPTGE VSSFHSDLEK 1690 1700 1710 1720 1730 1740 LTKVELDTSN RENVLMSTNL TATSTIYILK QENTQSTYRV NPDGSLRVTF ASGMEIGLSS 1750 1760 1770 1780 1790 1800 EPHILAGAVN PTLGKCNISL PGEHNANLIE WRQRKEQNKG NVSAFERRLR AHNRNLLSID 1810 1820 1830 1840 1850 1860 FDHITRTGKI YDDHRKFTLR ILYDQTGRPI LWSPVSRYNE VNITYSPSGL VTFIQRGTWN 1870 1880 1890 1900 1910 1920 EKMEYDQSGK IISRTWADGK IWSYTYLEKS VMLLLHSQRR YIFEYDQPDC LLSVTMPSMV 1930 1940 1950 1960 1970 1980 RHSLQTMLSV GYYRNIYTPP DSSTSFIQDY SRDGRLLQTL HLGTGRRVLY KYTKQARLSE 1990 2000 2010 2020 2030 2040 VLYDTTQVTL TYEESSGVIK TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD 2050 2060 2070 2080 2090 2100 YSYNNFRVTS MQAVINETPL PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK 2110 2120 2130 2140 2150 2160 IFSANGQVIE VQYEILKAIA YWMTIQYDNV GRMVICDIRV GVDANITRYF YEYDADGQLQ 2170 2180 2190 2200 2210 2220 TVSVNDKTQW RYSYDLNGNI NLLSHGKSAR LTPLRYDLRD RITRLGEIQY KMDEDGFLRQ 2230 2240 2250 2260 2270 2280 RGNDIFEYNS NGLLQKAYNK ASGWTVQYYY DGLGRRVASK SSLGQHLQFF YADLTNPIRV 2290 2300 2310 2320 2330 2340 THLYNHTSSE ITSLYYDLQG HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT 2350 2360 2370 2380 2390 2400 PYGDIYHDTY PDFQVIIGFH GGLYDFLTKL VHLGQRDYDV VAGRWTTPNH HIWKQLNLLP 2410 2420 2430 2440 2450 2460 KPFNLYSFEN NYPVGKIQDV AKYTTDIRSW LELFGFQLHN VLPGFPKPEL ENLELTYELL 2470 2480 2490 2500 2510 2520 RLQTKTQEWD PGKTILGIQC ELQKQLRNFI SLDQLPMTPR YNDGRCLEGG KQPRFAAVPS 2530 2540 2550 2560 2570 2580 VFGKGIKFAI KDGIVTADII GVANEDSRRL AAILNNAHYL ENLHFTIEGR DTHYFIKLGS 2590 2600 2610 2620 2630 2640 LEEDLVLIGN TGGRRILENG VNVTVSQMTS VLNGRTRRFA DIQLQHGALC FNIRYGTTVE 2650 2660 2670 2680 2690 2700 EEKNHVLEIA RQRAVAQAWT KEQRRLQEGE EGIRAWTEGE KQQLLSTGRV QGYDGYFVLS 2710 2720 VEQYLELSDS ANNIHFMRQS EIGRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10556288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 10341219] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2580, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-342; ILE-1216; VAL-1482; HIS-2235 AND PHE-2396.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00942033.
RefSeq	NP_001156750.1. NM_001163278.1. NP_001156751.1. NM_001163279.1. NP_055068.2. NM_014253.3.
UniGene	Hs.23796. Hs.727607.
3D structure databases
HSSP	HSSP built from PDB template 1MOX based on UniProtKB P01135.
ProteinModelPortal	Q9UKZ4.
SMR	Q9UKZ4. Positions 287-312, 531-834, 1192-1394, 1425-1460, 1491-1522.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UKZ4.
PTM databases
PhosphoSite	Q9UKZ4.
Polymorphism databases
DMDM	117949792.
Proteomic databases
PRIDE	Q9UKZ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371130; ENSP00000360171; ENSG00000009694.
GeneID	10178.
KEGG	hsa:10178.
UCSC	uc004euj.1. human.
Organism-specific databases
CTD	10178.
GeneCards	GC0XM123509.
H-InvDB	HIX0056136.
HGNC	HGNC:8117. ODZ1.
HPA	HPA002848.
MIM	300588. gene.
neXtProt	NX_Q9UKZ4.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09184.
GeneTree	ENSGT00580000081247.
HOVERGEN	HBG080306.
InParanoid	Q9UKZ4.
OrthoDB	EOG498TZV.
Gene expression databases
ArrayExpress	Q9UKZ4.
Bgee	Q9UKZ4.
CleanEx	HS_ODZ1.
Genevestigator	Q9UKZ4.
GermOnline	ENSG00000009694. Homo sapiens.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR013111. EGF_extracell. IPR009471. Ten_N. IPR006530. YD. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 2 hits.
Pfam	PF07974. EGF_2. 2 hits. PF06484. Ten_N. 2 hits. [Graphical view]
SMART	SM00181. EGF. 6 hits. [Graphical view]
TIGRFAMs	TIGR01643. YD_repeat_2x. 3 hits.
PROSITE	PS00022. EGF_1. 8 hits. PS01186. EGF_2. 7 hits. PS50026. EGF_3. 5 hits. PS51125. NHL. False negative. PS51361. TENEURIN_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	38530.
SOURCE	Search...

Entry information

Entry name

TEN1_HUMAN

Accession

Primary (citable) accession number: Q9UKZ4
Secondary accession number(s): Q5JZ17

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.