Q92752 (TENR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tenascin-R
Short name=TN-R

Alternative name(s):
Janusin
Restrictin

Gene names

Name:

TNR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance By similarity.
Subunit structure	Forms oligomers. Interacts with CNTN1, TNC, and FN1. Interacts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix.
Tissue specificity	Brain specific. Ref.1
Domain	The EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B By similarity.
Post-translational modification	Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated carbohydrate structure By similarity. O-glycosylated on Thr-36 or Thr-37 with a core 1 or possibly core 8 glycan.
Sequence similarities	Belongs to the tenascin family. Contains 5 EGF-like domains. Contains 1 fibrinogen C-terminal domain. Contains 9 fibronectin type-III domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil EGF-like domain Repeat Signal
Ligand	Sialic acid
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	associative learning Inferred from electronic annotation. Source: Compara axon guidance Non-traceable author statement PubMed 8940128. Source: ProtInc cell adhesion Non-traceable author statement PubMed 8940128. Source: ProtInc extracellular matrix organization Inferred from electronic annotation. Source: Compara locomotory exploration behavior Inferred from electronic annotation. Source: Compara long-term synaptic potentiation Inferred from electronic annotation. Source: Compara negative regulation of axon extension involved in regeneration Inferred from electronic annotation. Source: Compara negative regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of synaptic transmission Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara neuron cell-cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara synapse organization Inferred from electronic annotation. Source: Compara telencephalon cell migration Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay. Source: HPA membrane raft Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA perineuronal net Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92752-1)

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.

Isoform 2 (identifier: Q92752-2)

The sequence of this isoform differs from the canonical sequence as follows:
     773-862: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 1358	1327	Tenascin-R		PRO_0000007747
Regions
	Domain	188 – 199	12	EGF-like 1
	Domain	219 – 230	12	EGF-like 2
	Domain	250 – 261	12	EGF-like 3
	Domain	281 – 292	12	EGF-like 4
	Domain	312 – 323	12	EGF-like 5
	Domain	325 – 413	89	Fibronectin type-III 1
	Domain	414 – 502	89	Fibronectin type-III 2
	Domain	503 – 592	90	Fibronectin type-III 3
	Domain	593 – 684	92	Fibronectin type-III 4
	Domain	685 – 772	88	Fibronectin type-III 5
	Domain	773 – 862	90	Fibronectin type-III 6
	Domain	863 – 951	89	Fibronectin type-III 7
	Domain	952 – 1039	88	Fibronectin type-III 8
	Domain	1040 – 1127	88	Fibronectin type-III 9
	Domain	1129 – 1344	216	Fibrinogen C-terminal
	Coiled coil	127 – 157	31	Potential
	Compositional bias	155 – 314	160	Cys-rich
Amino acid modifications
	Modified residue	724	1	Phosphoserine By similarity
	Glycosylation	36	1	O-linked (GalNAc...) Probable
	Glycosylation	37	1	O-linked (GalNAc...) Probable
	Glycosylation	55	1	N-linked (GlcNAc...) Potential
	Glycosylation	180	1	N-linked (GlcNAc...) Potential
	Glycosylation	198	1	N-linked (GlcNAc...) Potential
	Glycosylation	278	1	N-linked (GlcNAc...) Potential
	Glycosylation	392	1	N-linked (GlcNAc...) Potential
	Glycosylation	470	1	N-linked (GlcNAc...) Potential
	Glycosylation	581	1	N-linked (GlcNAc...) Potential
	Glycosylation	791	1	N-linked (GlcNAc...) Potential
	Glycosylation	874	1	N-linked (GlcNAc...) Potential
	Glycosylation	1036	1	N-linked (GlcNAc...) Potential
	Glycosylation	1046	1	N-linked (GlcNAc...) Potential
	Glycosylation	1261	1	N-linked (GlcNAc...) Potential
	Disulfide bond	292 ↔ 301		By similarity
	Disulfide bond	297 ↔ 312		By similarity
	Disulfide bond	314 ↔ 323		By similarity
Natural variations
	Alternative sequence	773 – 862	90	Missing in isoform 2.		VSP_012993
	Natural variant	17	1	I → V. Ref.1 Ref.2 Corresponds to variant rs859398 [ dbSNP | Ensembl ].		VAR_021479
	Natural variant	128	1	A → S. Corresponds to variant rs2239819 [ dbSNP | Ensembl ].		VAR_021906
	Natural variant	293	1	G → S. Corresponds to variant rs3752516 [ dbSNP | Ensembl ].		VAR_021907
	Natural variant	302	1	S → N. Corresponds to variant rs35736986 [ dbSNP | Ensembl ].		VAR_055780
	Natural variant	643	1	R → K. Corresponds to variant rs859427 [ dbSNP | Ensembl ].		VAR_030737
Experimental info
	Sequence conflict	629	1	S → I in CAA66709. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 2, 2010. Version 3. Checksum: E4DE356B44D117E7	FASTA	1,358	149,562
	10 20 30 40 50 60 MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG IANYNTSSKE 70 80 90 100 110 120 QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE YMGQTSDHES QVTFTHRINF 130 140 150 160 170 180 PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNANCC QESAATGQLD YIPHCSGHGN 190 200 210 220 230 240 FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS 250 260 270 280 290 300 SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA 310 320 330 340 350 360 CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ 370 380 390 400 410 420 PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG 430 440 450 460 470 480 LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY 490 500 510 520 530 540 IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL 550 560 570 580 590 600 VGGEGGRTTF RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL 610 620 630 640 650 660 RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR ATLTDLVPGT 670 680 690 700 710 720 EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF 730 740 750 760 770 780 TPSSGIASEV TVPKDRTSYT LTDLEPGAEY IISVTAERGR QQSLESTVDA FTGFRPISHL 790 800 810 820 830 840 HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDEEEEMMEV SLDATKRHAV LMGLQPATEY 850 860 870 880 890 900 IVNLVAVHGT VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP 910 920 930 940 950 960 TQVGRLDSSV VPNTVTEFTI TRLNPATEYE ISLNSVRGRE ESERICTLVH TAMDNPVDLI 970 980 990 1000 1010 1020 ATNITPTEAL LQWKAPVGEV ENYVIVLTHF AVAGETILVD GVSEEFRLVD LLPSTHYTAT 1030 1040 1050 1060 1070 1080 MYATNGPLTS GTISTNFSTL LDPPANLTAS EVTRQSALIS WQPPRAEIEN YVLTYKSTDG 1090 1100 1110 1120 1130 1140 SRKELIVDAE DTWIRLEGLL ENTDYTVLLQ AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ 1150 1160 1170 1180 1190 1200 HLMNGDTLSG VYPIFLNGEL SQKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG 1210 1220 1230 1240 1250 1260 FGNVEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAS YDRFSVEDSR NLYKLRIGSY 1270 1280 1290 1300 1310 1320 NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG 1330 1340 1350 INWYHWKGHE FSIPFVEMKM RPYNHRLMAG RKRQSLQF
	Isoform 2 [UniParc]. Checksum: E4EB4095284A4E29	FASTA	1,268	139,695
	10 20 30 40 50 60 MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG IANYNTSSKE 70 80 90 100 110 120 QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE YMGQTSDHES QVTFTHRINF 130 140 150 160 170 180 PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNANCC QESAATGQLD YIPHCSGHGN 190 200 210 220 230 240 FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS 250 260 270 280 290 300 SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA 310 320 330 340 350 360 CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ 370 380 390 400 410 420 PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG 430 440 450 460 470 480 LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY 490 500 510 520 530 540 IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL 550 560 570 580 590 600 VGGEGGRTTF RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL 610 620 630 640 650 660 RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR ATLTDLVPGT 670 680 690 700 710 720 EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF 730 740 750 760 770 780 TPSSGIASEV TVPKDRTSYT LTDLEPGAEY IISVTAERGR QQSLESTVDA FTGIDPPKDI 790 800 810 820 830 840 TISNVTKDSV MVSWSPPVAS FDYYRVSYRP TQVGRLDSSV VPNTVTEFTI TRLNPATEYE 850 860 870 880 890 900 ISLNSVRGRE ESERICTLVH TAMDNPVDLI ATNITPTEAL LQWKAPVGEV ENYVIVLTHF 910 920 930 940 950 960 AVAGETILVD GVSEEFRLVD LLPSTHYTAT MYATNGPLTS GTISTNFSTL LDPPANLTAS 970 980 990 1000 1010 1020 EVTRQSALIS WQPPRAEIEN YVLTYKSTDG SRKELIVDAE DTWIRLEGLL ENTDYTVLLQ 1030 1040 1050 1060 1070 1080 AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ HLMNGDTLSG VYPIFLNGEL SQKLQVYCDM 1090 1100 1110 1120 1130 1140 TTDGGGWIVF QRRQNGQTDF FRKWADYRVG FGNVEDEFWL GLDNIHRITS QGRYELRVDM 1150 1160 1170 1180 1190 1200 RDGQEAAFAS YDRFSVEDSR NLYKLRIGSY NGTAGDSLSY HQGRPFSTED RDNDVAVTNC 1210 1220 1230 1240 1250 1260 AMSYKGAWWY KNCHRTNLNG KYGESRHSQG INWYHWKGHE FSIPFVEMKM RPYNHRLMAG RKRQSLQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human tenascin-R: complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24." Carnemolla B., Leprini A., Borsi L., Querze G., Urbini S., Zardi L. J. Biol. Chem. 271:8157-8160(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANT VAL-17. Tissue: Brain.
[2]	"Isolation of the gene for neural cell adhesion molecule tenascin-R and fine mapping relative to loci in 1q25-31." Williams H., Schachner M., Wang B., Goodfellow P., Kenwrick S. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-17. Tissue: Brain.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-37, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z67996 mRNA. Translation: CAA91947.1. X98085 mRNA. Translation: CAA66709.1. AL021919 Genomic DNA. No translation available. AL023285 Genomic DNA. No translation available. AL136530 Genomic DNA. No translation available. Z94057, Z94055 Genomic DNA. Translation: CAI21650.1. Z94055, Z94057 Genomic DNA. Translation: CAI19943.1.
IPI	IPI00160552. IPI00554760.
RefSeq	NP_003276.3. NM_003285.2.
UniGene	Hs.659864.
3D structure databases
ProteinModelPortal	Q92752.
SMR	Q92752. Positions 162-323, 326-1355.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92752. 1 interaction.
STRING	9606.ENSP00000263525.
PTM databases
PhosphoSite	Q92752.
Polymorphism databases
DMDM	311033534.
Proteomic databases
PaxDb	Q92752.
PRIDE	Q92752.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263525; ENSP00000263525; ENSG00000116147. ENST00000367674; ENSP00000356646; ENSG00000116147.
GeneID	7143.
KEGG	hsa:7143.
UCSC	uc001gkp.1. human.
Organism-specific databases
CTD	7143.
GeneCards	GC01M175291.
H-InvDB	HIX0028854.
HGNC	HGNC:11953. TNR.
HPA	CAB022343. HPA027134. HPA027150. HPA029859.
MIM	601995. gene.
neXtProt	NX_Q92752.
PharmGKB	PA36642.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG311251.
HOGENOM	HOG000234355.
HOVERGEN	HBG008949.
InParanoid	Q92752.
KO	K06252.
OMA	KACPCAS.
OrthoDB	EOG42FSGP.
Gene expression databases
ArrayExpress	Q92752.
Bgee	Q92752.
CleanEx	HS_TNR.
Genevestigator	Q92752.
GermOnline	ENSG00000116147. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.10. 9 hits. 3.90.215.10. 1 hit. 4.10.530.10. 1 hit.
InterPro	IPR013032. EGF-like_CS. IPR013111. EGF_extracell. IPR014716. Fibrinogen_a/b/g_C_1. IPR014715. Fibrinogen_a/b/g_C_2. IPR002181. Fibrinogen_a/b/g_C_dom. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. [Graphical view]
Pfam	PF07974. EGF_2. 2 hits. PF00147. Fibrinogen_C. 1 hit. PF00041. fn3. 9 hits. [Graphical view]
SMART	SM00186. FBG. 1 hit. SM00060. FN3. 9 hits. [Graphical view]
SUPFAM	SSF56496. Fibrinogen_a/b/g_C. 1 hit. SSF49265. FN_III-like. 9 hits.
PROSITE	PS00022. EGF_1. 5 hits. PS01186. EGF_2. 4 hits. PS50026. EGF_3. False negative. PS00514. FIBRINOGEN_C_1. False negative. PS51406. FIBRINOGEN_C_2. 1 hit. PS50853. FN3. 9 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	7143.
NextBio	27961.
SOURCE	Search...

Entry information

Entry name

TENR_HUMAN

Accession

Primary (citable) accession number: Q92752
Secondary accession number(s): C9J563, Q15568, Q5R3G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 112 of the entry and version 3 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.