wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair protein rhp41 (Q10445)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in the nucleotide excision repair (NER) pathway. Acts in both transcription-coupled repair (TCR) which removes damage from the transcribed strand of active genes and in global genome repair (GGR) which removes damage in untranscribed DNA. Involved in the repair of UV-induced damages where it is involved in the removal of cyclobutane pyrimidine dimers (CPDs).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- UV excision repair protein rhp23
- DNA repair protein rhp7
- DNA repair protein rhp26
- DNA repair protein rhp42
- DNA repair protein rad14
- Cell division control protein 31
- General transcription and DNA repair factor IIH subunit tfb1
- DNA repair protein rad16
- Mating-type switching protein swi10
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
Sequence:
MMSDEDNTYSDDEEWLDLDLGLPNNDIKTAPILNSSLLSSAVHGERLIQERPTHDFGDVEATVDRTVEKRSRLKITSVDRKIRLQIHQLHLLCLTYHLCTRNTWCDDNRLNYLVKYIPPGIRVSLHPSSQKSQMIRNKTFLHGLAGLVEVWKRKYKITTNGLRKPNYGLLQNNSLISESLSLEEFCKNSKLLSGSRDYGTQLFASILRNLNVPTRLVFSLQVLSFRFKGAINEASSHEIVPAWSQQMENDSSSDISESAHITSRFRKRRKIIQPSFSNLSHLDASDIVTEDTKLKVIDSPKPVFWVEAFNKAMQKWVCVDPFGDASVIGKYRRFEPASSDHLNQMTYVFAIEANGYVKDVTRKYCLHYYKILKNRVEIFPFGKAWMNRIFSKIGKPRDFYNDMDAIEDAELLRLEQSEGIPRNIQDLKDHPLFVLERHLKKNQAIKTGKSCGRINTKNGVELVYPRKYVSNGFSAEHWYRKGRIIKPGAQPLKHVKNGDKVLPLYDEEATQLYTPKPVVANIVPKNAYGNIDLYVPSMLPYGAYHCRKRCALAAAKFLEIDYAKAVVGFDFQRKYSKPKLEGVVVSKRYEEAIDLIAEEIDQEEKEAEARNVRKTCLLLWKRLITGLRIRQRVFEEYG
Protein: At3g51500 (Q9SCZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein EIN6 ENHANCER
- At4g18400
- SWR1 complex subunit 6
- At5g57910
- At4g30630
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Lysine-specific demethylase REF6
- SWR1 complex subunit 2
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Transcription initiation factor TFIID subunit 14b
Sequence:
MQDSKIPPFSEAKRMKIPTPKQPLTQLPPRIGKKVSNRSKSNQVHAISHQLEMSPNSDSSPGNEYRALRRKYLLLEEDSFALERELKEAEDEVKALEDEKLELLDKLVVMEGLVDP
Protein: GDSL esterase/lipase At3g26430 (EC 3.1.1.-) (Extracellular lipase At3g26430) (Q9LIN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipase that can hydrolyze p-nitrophenyl butyrate and p-nitrophenyl palmitate in vitro. Possesses low activity against p-nitrophenyl acetate. Substrate preference is p-nitrophenyl palmitate > p-nitrophenyl butyrate >> p-nitrophenyl acetate. Lacks cholinesterase activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Putative EG45-like domain containing protein 1
- Glycine-rich RNA-binding protein RZ1A
- Transcription factor TCP21
- Probable xyloglucan galactosyltransferase GT12
- Alpha-L-fucosidase 2
Sequence:
METNLLLVKCVLLASCLIHPRACSPSCNFPAIFNFGDSNSDTGGLSASFGQAPYPNGQTFFHSPSGRFSDGRLIIDFIAEELGLPYLNAFLDSIGSNFSHGANFATAGSTVRPPNATIAQSGVSPISLDVQLVQFSDFITRSQLIRNRGGVFKKLLPKKEYFSQALYTFDIGQNDLTAGLKLNMTSDQIKAYIPDVHDQLSNVIRKVYSKGGRRFWIHNTAPLGCLPYVLDRFPVPASQIDNHGCAIPRNEIARYYNSELKRRVIELRKELSEAAFTYVDIYSIKLTLITQAKKLGFRYPLVACCGHGGKYNFNKLIKCGAKVMIKGKEIVLAKSCNDVSFRVSWDGIHFTETTNSWIFQQINDGAFSDPPLPVKSACTR
Protein: Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain] (P08709)
Organism: Homo sapiens (Human)
Function: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
Subcellular location: Secreted {ECO:0000269|PubMed:36951360}.
Interaction partners:
- Tissue factor
- Tissue factor pathway inhibitor
- Coagulation factor X
- Coagulation factor IX
- Coagulation factor VIII
- Vitamin K-dependent gamma-carboxylase
- Thrombomodulin
- Prothrombin
- Protein O-glucosyltransferase 1
- Endothelial protein C receptor
Sequence:
MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP
Protein: Small COPII coat GTPase SAR1B (Sar1) (EC 3.6.5.2) (Q9QVY3)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex. Synergizes with the cargo receptor SURF4 to mediate the export of lipoproteins from the endoplasmic reticulum, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8138575}; Peripheral membrane protein {ECO:0000269|PubMed:8138575}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:8138575}; Peripheral membrane protein {ECO:0000269|PubMed:8138575}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y6B6}. Lysosome membrane {ECO:0000250|UniProtKB:Q9Y6B6}. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII (PubMed:11739406, PubMed:8138575). Upon leucine deprivation, associates with lysosomal membranes to repress TORC1 signaling (By similarity). {ECO:0000250|UniProtKB:Q9Y6B6, ECO:0000269|PubMed:11739406, ECO:0000269|PubMed:8138575}.
Interaction partners:
Sequence:
MSFIFDWIYSGFSSVLQFLGLYKKTGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHIQARRVWKNYLPAINGIVFLVDCADHERLLESKEELDSLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQTTGKGSVSLKELNARPLEVFMCSVLKRQGYGEGFRWMAQYID
Protein: Serine/threonine/tyrosine-interacting-like protein 1 (Dual specificity phosphatase inhibitor MK-STYX) (Dual specificity protein phosphatase 24) (Inactive dual specificity protein phosphatase MK-STYX) (Map kinase phosphatase-like protein MK-STYX) (Q9Y6J8)
Organism: Homo sapiens (Human)
Function: Catalytically inactive phosphatase. By binding to G3BP1, inhibits the formation of G3BP1-induced stress granules. Does not act by protecting the dephosphorylation of G3BP1 at 'Ser-149'. Inhibits PTPMT1 phosphatase activity. By inhibiting PTPMT1, positively regulates intrinsic apoptosis. May play a role in the formation of neurites during neuronal development.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:21262771}.
Interaction partners:
Sequence:
MPGLLLCEPTELYNILNQATKLSRLTDPNYLCLLDVRSKWEYDESHVITALRVKKKNNEYLLPESVDLECVKYCVVYDNNSSTLEILLKDDDDDSDSDGDGKDLVPQAAIEYGRILTRLTHHPVYILKGGYERFSGTYHFLRTQKIIWMPQELDAFQPYPIEIVPGKVFVGNFSQACDPKIQKDLKIKAHVNVSMDTGPFFAGDADKLLHIRIEDSPEAQILPFLRHMCHFIEIHHHLGSVILIFSTQGISRSCAAIIAYLMHSNEQTLQRSWAYVKKCKNNMCPNRGLVSQLLEWEKTILGDSITNIMDPLY
Protein: Hepcidin (Liver-expressed antimicrobial peptide 1) (LEAP-1) (Putative liver tumor regressor) (PLTR) [Cleaved into: Hepcidin-25 (Hepc25); Hepcidin-20 (Hepc20)] (P81172)
Organism: Homo sapiens (Human)
Function: Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin/SLC40A1, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:11034317}.
Interaction partners:
- Ferroportin
- Neutrophil gelatinase-associated lipocalin
- Hemojuvelin
- Immunoglobulin lambda-like polypeptide 5
- Hereditary hemochromatosis protein
- Transmembrane protease serine 6
- Natural resistance-associated macrophage protein 2
- Transferrin receptor protein 2
- Transferrin receptor protein 1
- Interleukin-6
Sequence:
MALSSQIWAACLLLLLLLASLTSGSVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCHRSKCGMCCKT
Protein: Pleckstrin homology domain-containing family B member 1 (PH domain-containing family B member 1) (Evectin-1) (PH domain-containing protein in retina 1) (PHRET1) (Pleckstrin homology domain retinal protein 1) (Q9QYE9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000269|PubMed:20301200}. Cytoplasm {ECO:0000269|PubMed:20301200}. Note=Membrane-associated. Highly expressed in the outer segments of photoreceptor cells, both in rods and cones (By similarity). Localizes to the apical juxta-nuclear Golgi region of the cytoplasm (PubMed:20301200). {ECO:0000250|UniProtKB:Q9UF11}.
Interaction partners:
- Synaptogyrin-4
Sequence:
MSPATPVPPDSILESPFEEMALVRGGWLWRQSSILRRWKRNWFALWLDGTLGYYHDETAQDEEDRVVIHFNVRDIKVGQECQDVQPPEGRSRDGLLTVNLREGSRLHLCAETRDDAIAWKTALMEANSTPAPAGATVPPRSRRVCPKVRCTTLSWNPCKVERRIWVRVYSPYQDYYEVVPPNAHEATYVRSYYGPPYAGPGVTHVIVREDPCYSSGAPLAMGMLAGAATGAALGSLMWSPCWF
Protein: BTB domain-containing protein (Q38FX9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein kinase, putative
- Serine/threonine-protein kinase, putative
- Uncharacterized protein
- Uncharacterized protein
- Ankyrin repeat protein
- ACB domain-containing protein
- ODAD1 central coiled coil region domain-containing protein
- Outer dynein arm docking complex
- Uncharacterized protein
- 3-hydroxyacyl-CoA dehydrogenase C-terminal domain-containing protein
Sequence:
MELLETVEVLANNSVRFRYSCPVQILQTIARTDTVHCSPKFGIGDHLWRLHLQQRCAPPSNEPYLSVHLQLCTQQHVVAQFKLTLVCYMDTRLSKSSTFRCTFQKTGSAWGVNHFVPLRQLTGAQSEFLYRDEASNAYFIDIEVLLMVCDTNESQRRRSLSISSNPCPANVDRHRDADSSARRGHAGDRVNGSVHRSPSNNQRFTQAPGNSFIPSPLTIPLRAPLLYPFEHLEGLADMTFEVEGGCFKAHRCIVAARMRPILPAAILPLQPGCSVAISVSSAVFSAFLRYIYTEELPEQGVMSAEALLDLYLLAAACEFYDLCSLCVRFVEPLLTSENILNIALTRFNAADEVLNALYLSALLENYDTLIQDPKFEEIPGHLFRRLSLILRSQETVPPICIPAVKNTLSKQLTWLAESGEYSDINLTVGPQKFVLKAHRFVLASRCILFSQAMGSKLPSSQLSFTSEEFDFSQRAWHKLLAAIYSHHIDSQHDFSAEDVAIVLKMHAVFGMDGQLKKEADEAFNYQNALRMLMYSTKHQVPELHERAIKYVGGNFFTLLQEEPQVWELVGELPQHTVVSLFRTVIENQGFSKCQSIGQTQL
Protein: Actin filament-associated protein 1 (110 kDa actin filament-associated protein) (AFAP-110) (Neural actin filament protein) (pp110) (Q90738)
Organism: Gallus gallus (Chicken)
Function: Functions as an adapter molecule that links other proteins to the actin cytoskeleton. May function in facilitating interactions between SRC and actin filaments. May modulate changes in actin filament integrity and induce lamellipodia formation. Can cross-link actin filaments into both network and bundle structures.
Subcellular location: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:2476666, ECO:0000269|PubMed:8247004, ECO:0000269|PubMed:9619827}.
Interaction partners:
- SH3 domain and tetratricopeptide repeats 1
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MEELIVELRLFLELLDHEYLTSTVREKKAVITNILLRIQSSKGFEIKEHVQKPEVANSLPAPPQMPLPEIPQQWLPPDNGPPPLPTSSLPEGYYEEAVPVSPGKAPEYITSNYDSDAMSSSYESYDEEEEDGKGKKMRHQWPSEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKENKLLCYKSSKDQQPQMELLLNDCSITYIPKDSKKKKHELKISHQGADALVLAVQSKEQAEQWLKVIKDVCSNCTGTVDSDGPLSSSPVHKTELEKKLSSERPSSDGEGAVENGITTVCNGKEQVKRKKSSKTEAKGTVTKVTGKKITKIIGLGKKKPSTDEQTSSAEEDVPTCGYLNVLSNNRWRERWCRVKDNKLIFHKDRTDLKTHIVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVAVLEASSSEDMGRWIGMLLAETGSSTDPGALHYDYIDVEMTASVIQAAKQTFCFMNRRVISTNPYRGSTANGYACPSGMALHYDDVPCINGSFKGKKPPATANGITGKVRTLNSQPKKPESVSCVKRTASNAEQYKYGKNRVEAVAKRLQSKEEELLKRKEALRNRLAQLRKERKDLRAAIEVNAGRKTQVILEDKLKKLEEECKTKEAERVNLELELTEVKESLKKALAGGITLGLAIEPKSGTSSPQSPIFKHRTLENSPISSCDTSDTECSIPVNSAAALKRPPSSNNSPCRGHVLRKAKEWEMKNGT
Protein: D-xylonate dehydratase YjhG (EC 4.2.1.82) (P39358)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dehydration of D-xylonic acid to form 2-dehydro-3-deoxy-D-pentonate.
Interaction partners:
- Probable 2-dehydro-3-deoxy-D-pentonate aldolase YjhH
- Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagE
- D-xylonate dehydratase YagF
- Uncharacterized HTH-type transcriptional regulator YjhI
- 3-isopropylmalate dehydratase large subunit
- Acetolactate synthase isozyme 1 large subunit
- Glutamate synthase large chain
- Xylose isomerase
- 3-isopropylmalate dehydratase small subunit
- Xylulose kinase
Sequence:
MSVRNIFADESHDIYTVRTHADGPDGELPLTAEMLINRPSGDLFGMTMNAGMGWSPDELDRDGILLLSTLGGLRGADGKPVALALHQGHYELDIQMKAAAEVIKANHALPYAVYVSDPCDGRTQGTTGMFDSLPYRNDASMVMRRLIRSLPDAKAVIGVASCDKGLPATMMALAAQHNIATVLVPGGATLPAKDGEDNGKVQTIGARFANGELSLQDARRAGCKACASSGGGCQFLGTAGTSQVVAEGLGLAIPHSALAPSGEPVWREIARASARAALNLSQKGITTREILTDKAIENAMTVHAAFGGSTNLLLHIPAIAHQAGCHIPTVDDWIRINKRVPRLVSVLPNGPVYHPTVNAFMAGGVPEVMLHLRSLGLLHEDVMTVTGSTLKENLDWWEHSERRQRFKQLLLDQEQINADEVIMSPQQAKARGLTSTITFPVGNIAPEGSVIKSTAIDPSMIDEQGIYYHKGVAKVYLSEKSAIYDIKHDKIKAGDILVIIGVGPSGTGMEETYQVTSALKHLSYGKHVSLITDARFSGVSTGACIGHVGPEALAGGPIGKLRTGDLIEIKIDCRELHGEVNFLGTRSDEQLPSQEEATAILNARPSHQDLLPDPELPDDTRLWAMLQAVSGGTWTGCIYDVNKIGAALRDFMNKN
Protein: Histone H2B type 1-A (Histone H2B, testis) (Testis-specific histone H2B) (P70696)
Organism: Mus musculus (Mouse)
Function: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. In condensing spermatids, the heterodimer between H2AB1 and H2BC1/TH2B is loaded onto the nucleosomes and promotes loading of transition proteins (TNP1 and TNP2) onto the nucleosomes. Inclusion of the H2AB1-H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition proteins (TNP1 and TNP2). Then, transition proteins drive the recruitment and processing of protamines, which are responsible for histone eviction. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:23884607}. Chromosome {ECO:0000269|PubMed:23884607}.
Interaction partners:
- Histone H3.1
- Histone H3.2
- Histone H3.3
- Histone H2A
- Histone H4
- Plasminogen
- E3 ubiquitin-protein ligase BRE1A
- Histone H2AX
- E3 ubiquitin-protein ligase BRE1B
- Histone H2A
Sequence:
MPEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FV03)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome C complete sequence
- Alkaline phosphatase
- Thiamine thiazole synthase
- Candida glabrata strain CBS138 chromosome D complete sequence
- Adenosine kinase
- Ribokinase
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MKFSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGLQNGVTLVQIREKDADTKFFIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIRKLVGPDMVIGWSVGFPEEVDELSKMGPDMVDYIGVGTLFPTLTKKNPKKAPMGTAGAIRVLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGICVVSDIIASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSIISNTLKARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHATLLLNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNKLLTFGQFSCIKGNSSEILGLAELNKERMKGVDASSGISNELLIQATKIVAFKYKTVAVCTGEFDFIADGTIEGKYSLSKGTNGTSVEDIPCVAVEAGPIEIMGDITASGCSLGSTIACMIGGQPSEGNLFHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRENTPVTWAPKLTHT
Protein: Gamma-aminobutyric acid receptor subunit rho-3 (GABA(A) receptor subunit rho-3) (GABAAR subunit rho-3) (GABA(C) receptor) (P50573)
Organism: Rattus norvegicus (Rat)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit rho-1
- Gamma-aminobutyric acid receptor subunit rho-2
Sequence:
MVLAFWLAFFTYTWITLMLDASAVKEPHQQCLSSPKQTRIRETRMRKDDLTKVWPLKREQLLHIEDHDFSTRPGFGGSPVPVGIDVQVESIDSISEVNMDFTMTFYLRHYWKDERLSFPSTTNKSMTFDRRLIQKIWVPDIFFVHSKRSFIHDTTVENIMLRVHPDGNVLFSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEEDLMLYWKHGNKSLNTEEHISLSQFFIEEFSASSGLAFYSSTGWYYRLFINFVLRRHIFFFVLQTYFPAMLMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIVTGVSASMPQVSYVKAVDVYMWVSSLFVFLSVIEYAAVNYLTTVEEWKQLNRRGKISGMYNIDAVQAMAFDGCYHDGETDVDQTSFFLHSEEDSMRTKFTGSPCADSSQIKRKSLGGNVGRIILENNHVIDTYSRIVFPVVYIIFNLFYWGIYV
Protein: Fibroblast growth factor 5 (FGF-5) (Heparin-binding growth factor 5) (HBGF-5) (P48807)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Platelet-derived growth factor receptor alpha
- Vascular endothelial growth factor receptor 1
Sequence:
MSLSLLFLIFCSHLILSAPAQGEKRLTPEGQPAPPRNPGDSSGSRGRSSATFASSSASSPVAASPGSQGSGSEHSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEASVLSILEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASAIHRTEKTGREWYVALNKRGKAKRGCSPRVKPQHVSTHFLPRFKQSEQPELSFTVTVPEKKKPPRPWKPKVPLSPSRRSPSPVKYRLKFRFG
Protein: Probable xyloglucan glycosyltransferase 8 (EC 2.4.1.-) (Cellulose synthase-like protein C8) (AtCslC8) (Q9SJA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable beta-1,4-glucan synthase rather involved in the synthesis of the xyloglucan backbone than cellulose. Seems to work simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic polysaccharides of plant cell wall and consists of a glucan backbone substituted by xylose, galactose and fucose.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9LJP4}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Hyperosmolality-gated Ca2+ permeable channel 1.5
- Hyperosmolality-gated Ca2+ permeable channel 1.6
- Mechanosensitive ion channel protein 7
- Uncharacterized protein At1g62240
- Transmembrane protein, putative
- Cinnamoyl CoA reductase-like protein
- Cinnamoyl-CoA reductase-like protein
- Cinnamoyl-CoA reductase-like protein
- Cellulose synthase-like protein D5
- Cellulose synthase-like protein D1
Sequence:
MAPRFDFSDLWAKETRRGTPVVVKMENPNYSIVEVEEPDSAFQPMEKSRGKNAKQVTWVLLLKAHKAVGCLTWVATVFWSLLGSVKRRLSFTHPLGSERLGRDGWLFSAIKLFLVASLAILAFELVAYYRGWHYFKNPNLHIPTSKLEIQSLLHLFYVGWLSLRADYIAPPIKALSKFCIVLFLVQSVDRLILCLGCLWIKFKKIKPRIDEEHFRNDDFEGSGSEYPMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRDEVTKWSQKGVNIIYRHRLVRTGYKAGNLKSAMSCDYVEAYEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLNFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGPMQLFRLCLRSILTSKIAMWKKANLILLFFLLRKLILPFYSFTLFCVILPITMFVPEAELPIWVICYVPIFMSLLNILPAPKSFPFIVPYLLFENTMSVTKFNAMVSGLFQLGSSYEWIVTKKAGRSSESDLLALTDKESEKMPNQILRGVSDSELLEISQVEEQKKQPVSVKKTNKIFHKELALAFLLLTAAVRSLLASQGVHFYFLLFQGLTFLLVGLDLIGEQMS
Protein: Phenylalanine-4-hydroxylase (PAH) (EC 1.14.16.1) (Phe-4-monooxygenase) (P04176)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine.
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Sepiapterin reductase
- Dihydropteridine reductase
- 4a-hydroxytetrahydrobiopterin dehydratase
- Tyrosine aminotransferase
- Aromatic-L-amino-acid decarboxylase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Dihydrofolate reductase
- Aldo-keto reductase family 1 member B1
Sequence:
MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKTACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSINSEVGILCNALQKIKS