Q8IXB1 (DJC10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DnaJ homolog subfamily C member 10

Alternative name(s):
ER-resident protein ERdj5
Macrothioredoxin
Short name=MTHr

Gene names

Name:	DNAJC10
Synonyms:	ERDJ5
ORF Names:	UNQ495/PRO1012

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	793 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	This endoplasmic reticulum co-chaperone may play a role in protein folding and translocation across the endoplasmic reticulum membrane. May act as a co-chaperone for HSPA5. Ref.1
Subunit structure	Interacts with HSPA5 via its J domain. Ref.1
Subcellular location	Secreted Potential. Endoplasmic reticulum lumen By similarity Ref.1.
Induction	By endoplasmic reticulum stress.
Sequence similarities	Contains 1 J domain. Contains 4 thioredoxin domains.
Sequence caution	The sequence BAB55121.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC11281.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Molecular function	Chaperone
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Inferred from mutant phenotype. Source: UniProtKB apoptosis in response to endoplasmic reticulum stress Inferred from direct assay. Source: UniProtKB cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro negative regulation of protein phosphorylation Inferred from direct assay. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro response to endoplasmic reticulum stress Inferred from direct assay. Source: UniProtKB
Cellular component	endoplasmic reticulum chaperone complex Inferred from direct assay. Source: UniProtKB endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATPase activator activity Inferred from sequence or structural similarity. Source: UniProtKB ATPase binding Inferred from physical interaction Ref.1. Source: UniProtKB chaperone binding Inferred from direct assay Ref.1. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heat shock protein binding Inferred from electronic annotation. Source: InterPro misfolded protein binding Inferred from direct assay. Source: UniProtKB protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8IXB1-1)

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: Q8IXB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     284-329: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 793	761	DnaJ homolog subfamily C member 10		PRO_0000281483
Regions
	Domain	35 – 100	66	J
	Domain	130 – 232	103	Thioredoxin 1
	Domain	454 – 553	100	Thioredoxin 2
	Domain	557 – 662	106	Thioredoxin 3
	Domain	671 – 778	108	Thioredoxin 4
	Motif	790 – 793	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	530	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	284 – 329	46	Missing in isoform 2.		VSP_024011
	Natural variant	76	1	D → N. Ref.2 Ref.7 Corresponds to variant rs6729801 [ dbSNP | Ensembl ].		VAR_031247
	Natural variant	347	1	L → I. Corresponds to variant rs13414223 [ dbSNP | Ensembl ].		VAR_048912
	Natural variant	414	1	Y → C. Corresponds to variant rs11681366 [ dbSNP | Ensembl ].		VAR_031248
	Natural variant	646	1	H → Q. Ref.3 Ref.6 Ref.7 Corresponds to variant rs288334 [ dbSNP | Ensembl ].		VAR_031249
Experimental info
	Sequence conflict	5	1	L → S in AAM09527. Ref.2
	Sequence conflict	5	1	L → S in BAB55304. Ref.4
	Sequence conflict	213	1	P → A in AAN73271. Ref.1
	Sequence conflict	356 – 359	4	NTLE → KRVK in AAN73271. Ref.1
	Sequence conflict	446	1	F → S in BAB55121. Ref.4
	Sequence conflict	565	1	T → A in CAD89982. Ref.7
	Sequence conflict	633	1	E → K in CAB70858. Ref.7
	Sequence conflict	755	1	K → N in BAB55304. Ref.4
	Sequence conflict	771	1	I → T in CAD89982. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: BD39B64325432D5D	FASTA	793	91,080
	10 20 30 40 50 60 MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE IRQAFKKLAL 70 80 90 100 110 120 KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY 130 140 150 160 170 180 DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR 190 200 210 220 230 240 IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL 250 260 270 280 290 300 WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 310 320 330 340 350 360 CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF ELLSANTLED 370 380 390 400 410 420 RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR FDCSSAPDIC SNLYVFQPSL 430 440 450 460 470 480 AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPANDKEP WLVDFFAPWC 490 500 510 520 530 540 PPCRALLPEL RRASNLLYGQ LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH 550 560 570 580 590 600 HSAEQILEFI EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 610 620 630 640 650 660 MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY NGWNRDAYSL 670 680 690 700 710 720 RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK 730 740 750 760 770 780 VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YERAKRNFQE EQINTRDAKA IAALISEKLE 790 TLRNQGKRNK DEL
	Isoform 2 [UniParc]. Checksum: D9F26A53E1B35455	FASTA	747	86,136
	10 20 30 40 50 60 MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE IRQAFKKLAL 70 80 90 100 110 120 KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY 130 140 150 160 170 180 DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR 190 200 210 220 230 240 IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL 250 260 270 280 290 300 WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLFLNSLDA KEIYLEVIHN 310 320 330 340 350 360 LPDFELLSAN TLEDRLAHHR WLLFFHFGKN ENSNDPELKK LKTLLKNDHI QVGRFDCSSA 370 380 390 400 410 420 PDICSNLYVF QPSLAVFKGQ GTKEYEIHHG KKILYDILAF AKESVNSHVT TLGPQNFPAN 430 440 450 460 470 480 DKEPWLVDFF APWCPPCRAL LPELRRASNL LYGQLKFGTL DCTVHEGLCN MYNIQAYPTT 490 500 510 520 530 540 VVFNQSNIHE YEGHHSAEQI LEFIEDLMNP SVVSLTPTTF NELVTQRKHN EVWMVDFYSP 550 560 570 580 590 600 WCHPCQVLMP EWKRMARTLT GLINVGSIDC QQYHSFCAQE NVQRYPEIRF FPPKSNKAYH 610 620 630 640 650 660 YHSYNGWNRD AYSLRIWGLG FLPQVSTDLT PQTFSEKVLQ GKNHWVIDFY APWCGPCQNF 670 680 690 700 710 720 APEFELLARM IKGKVKAGKV DCQAYAQTCQ KAGIRAYPTV KFYFYERAKR NFQEEQINTR 730 740 DAKAIAALIS EKLETLRNQG KRNKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress." Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R., Spyrou G. J. Biol. Chem. 278:1059-1066(2003) [PubMed: 12411443] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5.
[2]	"Cloning and identification of a novel cDNA which encodes a putative protein with a DnaJ domain and a thioredoxin active motif, human macrothioredoxin." Gu S.-H., Chen J.-Z., Ying K., Wang S., Jin W., Qian J., Zhao E.-P., Xie Y., Mao Y.-M. Biochem. Genet. 41:245-253(2003) [PubMed: 14587667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASN-76. Tissue: Fetal brain.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-646.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-646. Tissue: Colon.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-793 (ISOFORM 1), VARIANTS ASN-76 AND GLN-646. Tissue: Spinal cord and Testis.
[8]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-793. Tissue: Teratocarcinoma.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF038503 mRNA. Translation: AAN73271.1. AF490904 mRNA. Translation: AAM09527.1. AY358577 mRNA. Translation: AAQ88940.1. AK027450 mRNA. Translation: BAB55121.1. Different initiation. AK027647 mRNA. Translation: BAB55263.1. AK027696 mRNA. Translation: BAB55304.1. AC073951 Genomic DNA. Translation: AAX88931.1. AC105396 Genomic DNA. Translation: AAY24240.1. BC117299 mRNA. Translation: AAI17300.1. BC126168 mRNA. Translation: AAI26169.1. AL137648 mRNA. Translation: CAB70858.1. AL832646 mRNA. Translation: CAD89982.1. AK074905 mRNA. Translation: BAC11281.1. Different initiation.
IPI	IPI00293260. IPI00844115.
PIR	T46333.
RefSeq	NP_061854.1. NM_018981.1.
UniGene	Hs.516632.
3D structure databases
HSSP	HSSP built from PDB template 1BQZ based on UniProtKB P08622.
ProteinModelPortal	Q8IXB1.
SMR	Q8IXB1. Positions 34-782.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48947N.
IntAct	Q8IXB1. 5 interactions.
MINT	MINT-1451539.
STRING	Q8IXB1.
Polymorphism databases
DMDM	142981524.
Proteomic databases
PRIDE	Q8IXB1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264065; ENSP00000264065; ENSG00000077232.
GeneID	54431.
KEGG	hsa:54431.
NMPDR	fig|9606.3.peg.19011.
UCSC	uc002uow.1. human. uc002uoz.1. human.
Organism-specific databases
CTD	54431.
GeneCards	GC02P183580.
H-InvDB	HIX0002649.
HGNC	HGNC:24637. DNAJC10.
HPA	HPA031111.
MIM	607987. gene.
neXtProt	NX_Q8IXB1.
PharmGKB	PA134917195.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15167.
HOVERGEN	HBG057048.
OMA	HHGKKIL.
OrthoDB	EOG480HW1.
PhylomeDB	Q8IXB1.
Gene expression databases
ArrayExpress	Q8IXB1.
Bgee	Q8IXB1.
Genevestigator	Q8IXB1.
Family and domain databases
InterPro	IPR021170. DnaJ_homolog_subfam-C. IPR001623. DnaJ_N. IPR003095. Hsp_DnaJ. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 5 hits.
KO	K09530.
Pfam	PF00226. DnaJ. 1 hit. PF00085. Thioredoxin. 4 hits. [Graphical view]
PIRSF	PIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTS	PR00625. JDOMAIN. PR00421. THIOREDOXIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit. SSF52833. Thiordxn-like_fd. 6 hits.
PROSITE	PS00636. DNAJ_1. False negative. PS50076. DNAJ_2. 1 hit. PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	56629.
SOURCE	Search...

Entry information

Entry name

DJC10_HUMAN

Accession

Primary (citable) accession number: Q8IXB1
Secondary accession number(s): Q17RJ6 , Q4ZG06, Q53QT7, Q6UWZ6, Q86T61, Q8NC82, Q8TD87, Q96K38, Q96K44, Q96K54, Q9NSY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	January 25, 2012
This is version 83 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.