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Protein

Thrombospondin-4

Gene

THBS4

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

Functioni

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions and is involved in various processes including cellular proliferation, migration, adhesion and attachment, inflammatory response to CNS injury, regulation of vascular inflammation and adaptive responses of the heart to pressure overload and in myocardial function and remodeling. Binds to structural extracellular matrix (ECM) proteins and modulates the ECM in response to tissue damage, contributing to cardioprotective and adaptive ECM remodeling. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors and protects myocardium from pressure overload. May contribute to spinal presynaptic hypersensitivity and neuropathic pain states after peripheral nerve injury. May play a role in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury in a NOTCH1-dependent manner (By similarity).By similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. heparin binding Source: UniProtKB
  3. integrin binding Source: UniProtKB

GO - Biological processi

  1. behavioral response to pain Source: UniProtKB
  2. endothelial cell-cell adhesion Source: UniProtKB
  3. myoblast migration Source: UniProtKB
  4. negative regulation of angiogenesis Source: UniProtKB
  5. positive regulation of cell division Source: UniProtKB-KW
  6. positive regulation of endothelial cell proliferation Source: UniProtKB
  7. positive regulation of neutrophil chemotaxis Source: UniProtKB
  8. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  9. regulation of tissue remodeling Source: UniProtKB
  10. response to endoplasmic reticulum stress Source: UniProtKB
  11. response to unfolded protein Source: UniProtKB-KW
  12. tissue remodeling Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Keywords - Biological processi

Cell adhesion, Tissue remodeling, Unfolded protein response

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_16888. Signaling by PDGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombospondin-4
Gene namesi
Name:THBS4
Synonyms:TSP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:11788. THBS4.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. sarcoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Extracellular matrix, Sarcoplasmic reticulum, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 961935Thrombospondin-4PRO_0000035852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi258 – 258InterchainCurated
Disulfide bondi261 – 261InterchainCurated
Disulfide bondi290 ↔ 301PROSITE-ProRule annotation
Disulfide bondi295 ↔ 310PROSITE-ProRule annotation
Disulfide bondi313 ↔ 324PROSITE-ProRule annotation
Disulfide bondi330 ↔ 341PROSITE-ProRule annotation
Disulfide bondi335 ↔ 350PROSITE-ProRule annotation
Disulfide bondi353 ↔ 377PROSITE-ProRule annotation
Disulfide bondi383 ↔ 394PROSITE-ProRule annotation
Disulfide bondi388 ↔ 403PROSITE-ProRule annotation
Disulfide bondi406 ↔ 418PROSITE-ProRule annotation
Disulfide bondi424 ↔ 438PROSITE-ProRule annotation
Disulfide bondi432 ↔ 448PROSITE-ProRule annotation
Disulfide bondi450 ↔ 461PROSITE-ProRule annotation
Disulfide bondi477 ↔ 482PROSITE-ProRule annotation
Disulfide bondi487 ↔ 507PROSITE-ProRule annotation
Disulfide bondi523 ↔ 543PROSITE-ProRule annotation
Disulfide bondi546 ↔ 566PROSITE-ProRule annotation
Disulfide bondi582 ↔ 602PROSITE-ProRule annotation
Disulfide bondi605 ↔ 625PROSITE-ProRule annotation
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi643 ↔ 663PROSITE-ProRule annotation
Disulfide bondi683 ↔ 703PROSITE-ProRule annotation
Disulfide bondi719 ↔ 940PROSITE-ProRule annotation
Glycosylationi941 – 9411N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP35443.
PaxDbiP35443.
PeptideAtlasiP35443.
PRIDEiP35443.

PTM databases

PhosphoSiteiP35443.

Expressioni

Gene expression databases

BgeeiP35443.
CleanExiHS_THBS4.
ExpressionAtlasiP35443. baseline and differential.
GenevestigatoriP35443.

Organism-specific databases

HPAiCAB004597.

Interactioni

Subunit structurei

Homopentamer; disulfide-linked. Interacts with PTBP3. Interacts with NOTCH1 (By similarity). Interacts (via EGF-like 3; calcium-binding domain) with ATF6 and facilitates its processing, activation and nuclear translocation.By similarity3 Publications

Protein-protein interaction databases

BioGridi112918. 1 interaction.
IntActiP35443. 1 interaction.
STRINGi9606.ENSP00000339730.

Structurei

3D structure databases

ProteinModelPortaliP35443.
SMRiP35443. Positions 218-262, 290-952.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 192166Laminin G-likeAdd
BLAST
Domaini286 – 32540EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini326 – 36338EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini379 – 41941EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini420 – 46243EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati463 – 49533TSP type-3 1Add
BLAST
Repeati496 – 53136TSP type-3 2Add
BLAST
Repeati532 – 55423TSP type-3 3Add
BLAST
Repeati555 – 59036TSP type-3 4Add
BLAST
Repeati591 – 61323TSP type-3 5Add
BLAST
Repeati614 – 65138TSP type-3 6Add
BLAST
Repeati652 – 69140TSP type-3 7Add
BLAST
Repeati692 – 72736TSP type-3 8Add
BLAST
Domaini731 – 945215TSP C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi562 – 5643Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the thrombospondin family.Curated
Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074507.
HOGENOMiHOG000007542.
HOVERGENiHBG000636.
InParanoidiP35443.
KOiK04659.
OMAiRTFQRKP.
OrthoDBiEOG76QFGD.
PhylomeDBiP35443.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 2 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAPRGAAVL LLHLVLQRWL AAGAQATPQV FDLLPSSSQR LNPGALLPVL
60 70 80 90 100
TDPALNDLYV ISTFKLQTKS SATIFGLYSS TDNSKYFEFT VMGRLNKAIL
110 120 130 140 150
RYLKNDGKVH LVVFNNLQLA DGRRHRILLR LSNLQRGAGS LELYLDCIQV
160 170 180 190 200
DSVHNLPRAF AGPSQKPETI ELRTFQRKPQ DFLEELKLVV RGSLFQVASL
210 220 230 240 250
QDCFLQQSEP LAATGTGDFN RQFLGQMTQL NQLLGEVKDL LRQQVKETSF
260 270 280 290 300
LRNTIAECQA CGPLKFQSPT PSTVVPPAPP APPTRPPRRC DSNPCFRGVQ
310 320 330 340 350
CTDSRDGFQC GPCPEGYTGN GITCIDVDEC KYHPCYPGVH CINLSPGFRC
360 370 380 390 400
DACPVGFTGP MVQGVGISFA KSNKQVCTDI DECRNGACVP NSICVNTLGS
410 420 430 440 450
YRCGPCKPGY TGDQIRGCKA ERNCRNPELN PCSVNAQCIE ERQGDVTCVC
460 470 480 490 500
GVGWAGDGYI CGKDVDIDSY PDEELPCSAR NCKKDNCKYV PNSGQEDADR
510 520 530 540 550
DGIGDACDED ADGDGILNEQ DNCVLIHNVD QRNSDKDIFG DACDNCLSVL
560 570 580 590 600
NNDQKDTDGD GRGDACDDDM DGDGIKNILD NCPKFPNRDQ RDKDGDGVGD
610 620 630 640 650
ACDSCPDVSN PNQSDVDNDL VGDSCDTNQD SDGDGHQDST DNCPTVINSA
660 670 680 690 700
QLDTDKDGIG DECDDDDDND GIPDLVPPGP DNCRLVPNPA QEDSNSDGVG
710 720 730 740 750
DICESDFDQD QVIDRIDVCP ENAEVTLTDF RAYQTVVLDP EGDAQIDPNW
760 770 780 790 800
VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD FEGTFHVNTQ TDDDYAGFIF
810 820 830 840 850
GYQDSSSFYV VMWKQTEQTY WQATPFRAVA EPGIQLKAVK SKTGPGEHLR
860 870 880 890 900
NSLWHTGDTS DQVRLLWKDS RNVGWKDKVS YRWFLQHRPQ VGYIRVRFYE
910 920 930 940 950
GSELVADSGV TIDTTMRGGR LGVFCFSQEN IIWSNLKYRC NDTIPEDFQE
960
FQTQNFDRFD N
Length:961
Mass (Da):105,869
Last modified:November 23, 2004 - v2
Checksum:i18F867AA5FFDA54B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961N → S no nucleotide entry (PubMed:8350346).Curated
Sequence conflicti96 – 961N → S in CAA79635 (PubMed:7852353).Curated
Sequence conflicti276 – 2761P → A no nucleotide entry (PubMed:8350346).Curated
Sequence conflicti276 – 2761P → A in CAA79635 (PubMed:7852353).Curated
Sequence conflicti737 – 7371V → G no nucleotide entry (PubMed:8350346).Curated
Sequence conflicti737 – 7371V → G in CAA79635 (PubMed:7852353).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551L → Q.1 Publication
Corresponds to variant rs17881847 [ dbSNP | Ensembl ].
VAR_019951
Natural varianti387 – 3871A → P Gain of function mutation; resulting in a pro-atherogenic phenotype. 3 Publications
Corresponds to variant rs1866389 [ dbSNP | Ensembl ].
VAR_019952
Natural varianti420 – 4201A → V.3 Publications
Corresponds to variant rs17882372 [ dbSNP | Ensembl ].
VAR_019953
Natural varianti646 – 6461V → I.1 Publication
Corresponds to variant rs2229396 [ dbSNP | Ensembl ].
VAR_019954
Natural varianti737 – 7371V → I.
Corresponds to variant rs2229398 [ dbSNP | Ensembl ].
VAR_052659

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19585 mRNA. Translation: CAA79635.1.
AK313587 mRNA. Translation: BAG36356.1.
AY566253 Genomic DNA. Translation: AAS66982.1.
BC050456 mRNA. Translation: AAH50456.1.
CCDSiCCDS4049.1.
PIRiA55710. TSHUP4.
RefSeqiNP_003239.2. NM_003248.4.
UniGeneiHs.211426.

Genome annotation databases

EnsembliENST00000350881; ENSP00000339730; ENSG00000113296.
GeneIDi7060.
KEGGihsa:7060.
UCSCiuc021yaw.1. human.

Polymorphism databases

DMDMi55977790.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19585 mRNA. Translation: CAA79635.1.
AK313587 mRNA. Translation: BAG36356.1.
AY566253 Genomic DNA. Translation: AAS66982.1.
BC050456 mRNA. Translation: AAH50456.1.
CCDSiCCDS4049.1.
PIRiA55710. TSHUP4.
RefSeqiNP_003239.2. NM_003248.4.
UniGeneiHs.211426.

3D structure databases

ProteinModelPortaliP35443.
SMRiP35443. Positions 218-262, 290-952.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112918. 1 interaction.
IntActiP35443. 1 interaction.
STRINGi9606.ENSP00000339730.

PTM databases

PhosphoSiteiP35443.

Polymorphism databases

DMDMi55977790.

Proteomic databases

MaxQBiP35443.
PaxDbiP35443.
PeptideAtlasiP35443.
PRIDEiP35443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350881; ENSP00000339730; ENSG00000113296.
GeneIDi7060.
KEGGihsa:7060.
UCSCiuc021yaw.1. human.

Organism-specific databases

CTDi7060.
GeneCardsiGC05P079287.
HGNCiHGNC:11788. THBS4.
HPAiCAB004597.
MIMi600715. gene.
neXtProtiNX_P35443.
PharmGKBiPA36500.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074507.
HOGENOMiHOG000007542.
HOVERGENiHBG000636.
InParanoidiP35443.
KOiK04659.
OMAiRTFQRKP.
OrthoDBiEOG76QFGD.
PhylomeDBiP35443.
TreeFamiTF324917.

Enzyme and pathway databases

ReactomeiREACT_16888. Signaling by PDGF.

Miscellaneous databases

GeneWikiiTHBS4.
GenomeRNAii7060.
NextBioi27609.
PROiP35443.
SOURCEiSearch...

Gene expression databases

BgeeiP35443.
CleanExiHS_THBS4.
ExpressionAtlasiP35443. baseline and differential.
GenevestigatoriP35443.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 2 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
    Tissue: Heart.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420, SUBUNIT.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-387.
    Tissue: Synovium.
  4. SeattleSNPs variation discovery resource
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-55; PRO-387; VAL-420 AND ILE-646.
  5. "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].
    Tissue: PNS.
  6. "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal peptide of thrombospondin-4 and is involved in its mitogenic activity."
    Sadvakassova G., Dobocan M.C., Difalco M.R., Congote L.F.
    J. Cell. Physiol. 220:672-679(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTBP3.
  7. Cited for: INTERACTION WITH ATF6.
  8. "ATF6 [corrected] and thrombospondin 4: the dynamic duo of the adaptive endoplasmic reticulum stress response."
    Doroudgar S., Glembotski C.C.
    Circ. Res. 112:9-12(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. Cited for: REVIEW.
  10. "Thrombospondin-4 polymorphism (A387P) predicts cardiovascular risk in postinfarction patients with high HDL cholesterol and C-reactive protein levels."
    Corsetti J.P., Ryan D., Moss A.J., McCarthy J., Goldenberg I., Zareba W., Sparks C.E.
    Thromb. Haemost. 106:1170-1178(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT PRO-387.

Entry informationi

Entry nameiTSP4_HUMAN
AccessioniPrimary (citable) accession number: P35443
Secondary accession number(s): B2R909, Q86TG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 23, 2004
Last modified: February 4, 2015
This is version 150 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.