wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein Rv2306c (P9WLC9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MTRVALLTTGRELSQAAPPARARTPLPVPTPRGERPDDGGHAPHRDRRVNQRRRQVGDRRAQRGVDEHPWRRPDERPNDHLPQRNSERPEGVRGQRIRDAGDEALTDHRPQSAPFDLCIEAMGAIDTQQRLGVIPACAPAEKAGRVTKVSSSGPNSTPLPAARIGPGTNNAPSAADTTTYARGAIGPVATTIALRTPSTWMTRATATR
Protein: Phospholipase D1 (PLD 1) (hPLD1) (EC 3.1.4.4) (Choline phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D1) (Q13393)
Organism: Homo sapiens (Human)
Function: Function as phospholipase selective for phosphatidylcholine. Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Z280}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}.
Interaction partners:
- Ras-related protein Ral-A
- Transforming protein RhoA
- ADP-ribosylation factor 1
- ADP-ribosylation factor 6
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Ras-related protein Ral-B
- Protein kinase C alpha type
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 2
- Cholinephosphotransferase 1
Sequence:
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Protein: Putative Bardet-Biedl syndrome 1 protein (BBS1-like protein 1) (E9AFP5)
Organism: Leishmania major
Interaction partners:
- Intergrin alpha chain protein
- Hypothetical tetratricopeptide repeat protein
- Uncharacterized protein
- PTHB1 N-terminal domain-containing protein
- BBSome complex member BBS5 PH domain-containing protein
- Putative Bardet-Biedl syndrome 4 protein homolog
- Putative kinesin
Sequence:
MSAPKEGNRGESKEKFWLYAFRDHLANLRAFSNCIETADVNGVGDYQLLVADGSKRIKVYAGTSLQRELPLFGVPSAITSFFMDDADAFGKPVVAVATGPYIFMYRSNKPLYRFMVPPVPLNPQESAIWQDLATEALTVEEAVKQLESLLDSGVETSSRTLELLLETPEERGEFVSRLRSVPLIQMDVVCCLTSIPLNSLDEGGRSVLVIGTEAGFLYVLKHNAAEVALKVVLPRTPVFLIAAGCFEVDYRMVVACRDGRVYSIKQGNLQNAVIQPDAQPCAIARYNNLIAVATTANTLAYYNLKGKKQQSVFLPCSISGLSTINDTVTGEARGLVVALSNGEIRVYVGTQLHHVSLAYGTVTAMKFGRYGRSDGALVLVLQNGSLVVELLHRGVNLSCSKTVETGPPPQQDIPIPIPHLSSVFATQSSRERKHGVEMYQLFQYDLSQLRLTTAKAYLDMIANGSVPSELGNVTQENEGVAEPSLRLNAVVQGLGPVFKVKVQLQNVGEAPLHAVRVVFCLSEDNVYCMPQQIFLIPTLLPSVPLSCAAFVTTSEGEAKGNAILVVATGPKSRTPLARTLVDLPEVEAMAEV
Protein: Fasciclin-like arabinogalactan protein 18 (Q93W32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Putative defensin-like protein 263
- Fasciclin-like arabinogalactan protein 9
- Fasciclin-like arabinogalactan protein 13
- Fasciclin-like arabinogalactan protein 21
- Fasciclin-like arabinogalactan protein 4
- Fasciclin-like arabinogalactan protein 1
- Fasciclin-like arabinogalactan protein 2
- Putative fasciclin-like arabinogalactan protein 20
- Fasciclin-like arabinogalactan protein 19
- Fasciclin-like arabinogalactan protein 3
Sequence:
MDRCIYGCSVITIFFSFFFLLNASALESGHHNITGSGQINSNSVLVALLDSRYTELAELVEKALLLQTLEDAVGRHNITIFAPRNEALERDLDPDFKRFLLQPGNLKSLQTLLLSHIIPKRVGSNQWPEENSGRVKHVTLGHDQVLHLSKLKGTNGKRLVNSAVITRPDDLTRPDGLIHGIERLLIPRSVQEDFNRRRNLRSISAVLPEGAPEIDPRTNRLKKSATAVSVPAGSPPVLPIESAMAPGPSLAPAPAPGPGGAHKHFNGDAQVKDFIHTLLHYGGYNEMADILVNLTSLATEMGRLVSEGYVLTVLAPNDEAMGKLTTDQLSEPGAPEQIMYYHIIPEYQTEESMYNSVRRFGKVKYETLRFPHKVGAKEADGSVKFGSGDRSAYLFDPDIYTDGRISVQGIDGVLFPEEKEEETVKKPTGPVKKVVQPRRGKLLEVACSMLGAIGKDSYLSRC
Protein: Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG) (Q28640)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Binds T-cells and alters the cell morphology Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity). Tethers plasminogen to the cell surface.
Subcellular location: Secreted.
Interaction partners:
- Plasminogen
- Fibrinogen alpha chain
- Kininogen 1
- Apolipoprotein A-V
- Coagulation factor XIII B chain
- Afamin
- Alanine--glyoxylate aminotransferase
- Alpha-2-HS-glycoprotein
- Fibrinogen gamma chain
- Fetuin B
Sequence:
ATLQCSWALTPTDCKTTKPLAEKALDLINKWRRDGYLFQLLRVADAHLDGAESATVYYLVLDVKETDCSVLSRKHWEDCDPDLTKRPSLDVIGQCKVIATRYSDEYQTLRLNDFNCTTSSVSSALANTKDSPVLFDFIEDTEPFRKSADKALEVYKSESEAYASFRVDRVERVTRVKGGERTNYYVDFSVRNCSRSHFHRHPAFGFCRADLSFDVEASNLENPEDVIISCEVFNFEEHGNISGFRPHLGKTPLGTDGSRDHHHPHKPHKFGCPPPQEGEDFSEGPPLQGGTPPLSPPFRPRCRHRPFGTNETHRFPHHRISVNIIHRPPPHGHHPHGPPPHGHHPHGPPPHGHPPHGPPPRHPPHGPPPHGHPPHGPPPHGHPPHGPPPHGHPPHGPPPHGHPPHGHGFHDHGPCDPPSHKEGPQDLHQHAMGPPPKHPGKRGPGKGHFPFHWRRIGSVYQLPPLQKGEVLPLPEANFPQLLLRNHTHPLKPEIQPFPQVASERCPEEFNGEFAQLSKFFPSTFPK
Protein: 1,3-beta-glucan synthase component GSC2 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (FK506 sensitivity protein 2) (Glucan synthase of cerevisiae protein 2) (P40989)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Required for spore wall assembly. Negative regulation of activity by SMK1 is important for spore wall deposition. Activity is positively regulated by RHO1.
Subcellular location: Membrane {ECO:0000269|PubMed:7565718}; Multi-pass membrane protein {ECO:0000269|PubMed:7565718}.
Interaction partners:
- 1,3-beta-glucan synthase component FKS1
- 1,3-beta-glucan synthase component FKS3
- GTP-binding protein RHO1
- Protein kinase C-like 1
- Glucan 1,3-beta-glucosidase
- RHO1 GDP-GTP exchange protein 2
- UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Glucan 1,3-beta-glucosidase I/II
- Glycogen [starch] synthase isoform 1
Sequence:
MSYNDPNLNGQYYSNGDGTGDGNYPTYQVTQDQSAYDEYGQPIYTQNQLDDGYYDPNEQYVDGTQFPQGQDPSQDQGPYNNDASYYNQPPNMMNPSSQDGENFSDFSSYGPPSGTYPNDQYTPSQMSYPDQDGSSGASTPYGNGVVNGNGQYYDPNAIEMALPNDPYPAWTADPQSPLPIEQIEDIFIDLTNKFGFQRDSMRNMFDHFMTLLDSRSSRMSPEQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMKLGKLSRKARKAKKKNKKAMQEASPEDTEETLNQIEGDNSLEAADFRWKSKMNQLSPFEMVRQIALFLLCWGEANQVRFTPECLCFIYKCASDYLDSAQCQQRPDPLPEGDFLNRVITPLYRFIRSQVYEIVDGRYVKSEKDHNKVIGYDDVNQLFWYPEGIAKIVMEDGTRLIDLPAEERYLKLGEIPWDDVFFKTYKETRSWLHLVTNFNRIWIMHISVYWMYCAYNAPTFYTHNYQQLVDNQPLAAYKWATAALGGTVASLIQVAATLCEWSFVPRKWAGAQHLSRRFWFLCVIMGINLGPVIFVFAYDKDTVYSTAAHVVGAVMFFVAVATLVFFSVMPLGGLFTSYMKKSTRSYVASQTFTASFAPLHGLDRWMSYLVWVTVFAAKYAESYFFLILSLRDPIRILSTTSMRCTGEYWWGNKICKVQPKIVLGLMIATDFILFFLDTYLWYIVVNTVFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQIWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWDCFVKDTKILAEETAAYENNEDEPEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNADGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLNEGEEPRIYSALIDGHCEILENGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELGIEQIHPYTPGLKYEDQSTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAVLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPIDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLHALAHESILCVYDRDKPITDVLYPIGCYNFHPAIDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFRHILSLSPMFEVFAGQIYSSALLSDIAVGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGSRSMLMLLFGTVAHWQAPLLWFWASLSALIFAPFIFNPHQFAWEDFFLDYRDYIRWLSRGNNKYHRNSWIGYVRMSRSRVTGFKRKLVGDESEKSAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDEDRVNSTLRIIICTLAPIVIDIGVLFFCMGLSCCSGPLLGMCCKKTGSVMAGIAHGIAVVVHIVFFIVMWVLEGFSFVRMLIGVVTCIQCQRLIFHCMTVLLLTREFKNDHANTAFWTGKWYSTGLGYMAWTQPTRELTAKVIELSEFAADFVLGHVILIFQLPVICIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQARLRKRMVRRYCSLYFLVLIIFAGCIVGPAVASAHVPKDLGSGLTGTFHNLVQPRNVSNNDTGSQMSTYKSHYYTHTPSLKTWSTIK
Protein: UDP-glycosyltransferase 708A6 (EC 2.4.1.-) (A0A096SRM5)
Organism: Zea mays (Maize)
Function: Bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids. Converts 2-hydroxynaringenin to isovitexin. Converts eriodictyol to orientin and isoorientin. Converts naringenin and eriodictyol to naringenin 7-O-glucoside and eriodictyol 7-O-glucoside, respectively.
Interaction partners:
- Putative cytochrome P450 superfamily protein
- Cytochrome P450 family 93 subfamily D polypeptide 1
Sequence:
MAANGGDHTSARPHVVLLPSAGMGHLVPFARLAVALSEGHGCNVSVAAVQPTVSSAESRLLDALFVAAAPAVRRLDFRLAPFDESEFPGADPFFLRFEATRRSAPLLGPLLDAAEASALVTDIVLASVALPVARERGVPCYVLFTSSAAMLSLCAYFPAYLDAHAAAGSVGVGVGNVDIPGVFRIPKSSVPQALHDPDHLFTQQFVANGRCLVACDGILVNTFDAFEPDAVTALRQGSITVSGGFPPVFTVGPMLPVRFQAEETADYMRWLSAQPPRSVVYVSFGSRKAIPRDQLRELAAGLEASGKRFLWVVKSTIVDRDDTADLGGLLGDGFLERVQGRAFVTMGWVEQEEILQHGSVGLFISHCGWNSLTEAAAFGVPVLAWPRFGDQRVNAALVARSGLGAWEEGWTWDGEEGLTTRKEVAKKIKGMMGYDAVAEKAAKVGDAAAAAIAKCGTSYQSLEEFVQRCRDAERK
Protein: Protein JTB (O88824)
Organism: Mus musculus (Mouse)
Function: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity (By similarity). Inhibits apoptosis induced by TGFB1. Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17369841}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected at the centrosome and along spindle fibers during prophase and metaphase. Detected at the midbody during telophase (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MLAGAGRRGLPRAGHLCWLLCAFTLKLCEAEAPVREEKLSVSTSTSPCWLAEEFVVTEECTPCSNFQIKTTPECGSTGYVEKITCSSSKRNEFKSCRSALLEQHLFWKFEGVVVAVALVFACLVIVRQRQLDRKALEKVRKQIESI
Protein: Gastric inhibitory polypeptide (GIP) (Glucose-dependent insulinotropic polypeptide) (P48756)
Organism: Mus musculus (Mouse)
Function: Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.
Subcellular location: Secreted.
Interaction partners:
- Gastric inhibitory polypeptide receptor
- Glucagon-like peptide 1 receptor
- Dipeptidyl peptidase 4
- Glucose-dependent insulinotropic receptor
- Vasoactive intestinal polypeptide receptor 2
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Adrenocorticotropic hormone receptor
- 5-hydroxytryptamine receptor 4
- Beta-1 adrenergic receptor
Sequence:
MVALKTCSLLLVLLFLAVGLGEKEEVEFRSHAKFAGPRPRGPRYAEGTFISDYSIAMDKIRQQDFVNWLLAQRGKKSDWKHNITQREARALVLAGQSQGKEDKEAQESSLPKSLSDDDVLRDLLIQELLAWMVDQTELCRLRSQ
Protein: Female-specific lacrimal gland protein (Female-specific LG protein) (Q99MG7)
Organism: Mesocricetus auratus (Golden hamster)
Subcellular location: Secreted {ECO:0000269|PubMed:15950295, ECO:0000269|PubMed:7887957}. Note=Secreted by the lacrimal gland into tears. {ECO:0000269|PubMed:15950295, ECO:0000269|PubMed:7887957}.
Interaction partners:
Sequence:
MVKFLLLALALGVSCAHYQNLEVSPSEVDGKWYSLYIAADNKEKVSEGGPLRAYIKNVECIDECQTLKITFYTKVEGVCQEHTIVGRKGEDGKYITDFSGQNYFHIVEKSDDTMTFHNVNVDDSGKTNVILVVGRGESSSIEQKQRFEKTAEEYDIPKENIEDLVPTDNCDQ
Protein: 5,6-dimethylbenzimidazole synthase (DMB synthase) (EC 1.13.11.79) (Q92PC8)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Function: Involved in the biosynthesis of cobalamin (vitamin B12). Catalyzes the oxidative fragmentation and contraction of the isoalloxazine heterocycle and the cleavage of the ribityl tail of FMN(2) to form 5,6-dimethylbenzimidazole (DMB) and D-erythrose 4-phosphate (E4P). NAD(P)H is only required initially to reduce FMN and oxygen drives the oxidative fragmentation.
Interaction partners:
Sequence:
MLPDPNGCLTAAGAFSSDERAAVYRAIETRRDVRDEFLPEPLSEELIARLLGAAHQAPSVGFMQPWNFVLVRQDETREKVWQAFQRANDEAAEMFSGERQAKYRSLKLEGIRKAPLSICVTCDRTRGGAVVLGRTHNPQMDLYSTVCAVQNLWLAARAEGVGVGWVSIFHESEIKAILGIPDHVEIVAWLCLGFVDRLYQEPELAAKGWRQRLPLEDLVFEEGWGVR
Protein: Transcription factor IIIA (TFIIIA) (P79797)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Function: Involved in ribosomal large subunit biogenesis. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's (By similarity).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MGERFKDPAKNFVCSFLNCKASFSKAWKLEAHYCKHTGLRPFACDRCDKTFCTRCQLTRHNLSHSGKKPYQCLEDGCSESFISTAGLKNHVERVHQHKEKHYVCDYEGCAKEFRKKKQLRSHKCEHMNQLPFECQYEGCGKKYTTSKKLQKHEKVHDVYPCAEEGCDFQGRMWTEYQAHRKAAHREALQCDSCAKVFHKAWFLKKHKLFVHLGVRRVFKCTKEGCQKTYTTHFNLQNHILSFHEGIRSFICPHDGCGKAFAMEGSLKRHAVVHDPQKKKLQKKTKRGRKKKLEPKTNVSDDSELPAQLHGLSLNTSTSQNNP
Protein: Vomeronasal 2, receptor 120 (A0A3Q4L2Y3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMLHPFLKNIQFNNPSGDKVDLSHTGKLETKYDIFNFWNFPQGLGLKVKVGTFSSFLPRNKQFSLSDGMIEWGTKDKQTPLSVCSTSCAPGLMKSPQEGKASCCFDCHPCLENEISNETDSIQCIKCPDDQYANTEQTHCIPKAVTFLAYEDPLGMALACMALCFSALTALVLGVFVKHHETPIVKANNRTLSYILLISLILCFLCSLPFIGLPNMATCILQQMSFGVVFTIAVSTVLAKTVTVVLAFRSTVPGRRMRWILVSPNLIIPICTLIQMVLCAIWLGASAPFVDINAHNERGHITIMCNKGSATAFYCVLGYLGFLAMGTLTVAFWARNLPDIFNEAKFLTFSMLVFCSVWVTFLPVYHSTKGKVMVAVEVFSILASSAGLLGCIFVPKCYIILIRPKNGSFKGLRGTRVCK
Protein: Intermediate filament protein ifa-4 (Cel IF A4) (Intermediate filament protein A4) (IF-A4) (P90900)
Organism: Caenorhabditis elegans
Function: Cytoplasmic intermediate filaments provide mechanical strength to cells. Non-essential protein.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Intermediate filament protein ifb-1
- Cysteine-rich protein 1
- Intermediate filament protein ifp-1
- Intermediate filament protein ifc-1
- Intermediate filament protein ifc-2
Sequence:
MSESEYRSSISVRPTFNRTMQSTATYGSTISSGTSRTLKITEIGGSNLTSGMSPFGGHAASAIRESRTREKKEMSELNDRLASYIEKVRFLEAQNRKMEKDLNLLRGKWGHDSTSVKVMYETELRSAKDLIADSDKERAQLEDQIKKLVEELNNYRNKLHEAERGADVTRKELDNVLGRLGALEAEIELLKRRISLMEESIGHLKRENHRMIDSLHHARNAVEQETLNRIDYQNQVQTLLEECDFIRRIHDSEIHDLLAMASRDTTVENREYFKNELSSAIREIRSEYDHVSNTTRTDIESWYKLKVQEIHTQNSRNCLEQNYAREEVKRLRTTLGDMRGKMADLEGRNLLLEKQIEDLNYQMEEDMRSYEQSLNDKDTSINKLRDESKILMVELQMLIDTKQTLDAEIVIYRKMLDGEENRAGLRQLVEQVVKTTSIHQTKEIESLRVLKGETTSHSSYSRSAKGNIAIQEAEPSGKYIVLENISRRDENIGDWKLRRKIAGKREIVFTFPREFTLRAQKSVKIFARGQGVHSPPDSLVYDLEDSFGTGNDVVTTLYNKEGEDRASHSQRASHT
Protein: Small G protein signaling modulator 2 (RUN and TBC1 domain-containing protein 1) (O43147)
Organism: Homo sapiens (Human)
Function: Possesses GTPase activator activity towards RAB32, RAB33B and RAB38. Regulates the trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes by inactivating RAB32 and RAB38. Inhibits RAB32 and RAB38 activation both directly by promoting their GTPase activity and indirectly by disrupting the RAB9A-HPS4 interaction which is required for RAB32/38 activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26620560}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Melanosomal localization is mediated by RAB9A. {ECO:0000269|PubMed:26620560}.
Interaction partners:
- Small G protein signaling modulator 3
- Ras-related protein Rab-9A
- Ras-related protein Rap-1b
- Ras-related protein Rab-4A
- Ras-related protein Rab-3A
- Ras-related protein Rap-2a
Sequence:
MGSAEDAVKEKLLWNVKKEVKQIMEEAVTRKFVHEDSSHIIALCGAVEACLLHQLRRRAAGFLRSDKMAALFTKVGKTCPVAGEICHKVQELQQQAEGRKPSGVSQEALRRQGSASGKAPALSPQALKHVWVRTALIEKVLDKVVQYLAENCSKYYEKEALLADPVFGPILASLLVGPCALEYTKLKTADHYWTDPSADELVQRHRIRGPPTRQDSPAKRPALGIRKRHSSGSASEDRLAACARECVESLHQNSRTRLLYGKNHVLVQPKEDMEAVPGYLSLHQSAESLTLKWTPNQLMNGTLGDSELEKSVYWDYALVVPFSQVVCIHCHQQKSGGTLVLVSQDGIQRPPLHFPQGGHLLSFLSCLENGLLPRGQLEPPLWTQQGKGKVFPKLRKRSSIRSVDMEEMGTGRATDYVFRIIYPGHRHEHNAGDMIEMQGFGPSLPAWHLEPLCSQGSSCLSCSSSSSPHATPSHCSCIPDRLPLRLLCESMKRQIVSRAFYGWLAHCRHLSTVRTHLSALVHHSVIPPDRPPGASAGLTKDVWSKYQKDKKNYKELELLRQVYYGGIEHEIRKDVWPFLLGHYKFGMSKKEMEQVDAVVAARYQQVLAEWKACEVVVRQREREAHPATRTKFSSGSSIDSHVQRLIHRDSTISNDVFISVDDLEPPEPQDPEDSRPKPEQEAGPGTPGTAVVEQQHSVEFDSPDSGLPSSRNYSVASGIQSSLDEGQSVGFEEEDGGGEEGSSGPGPAAHTLREPQDPSQEKPQAGELEAGEELAAVCAAAYTIELLDTVALNLHRIDKDVQRCDRNYWYFTPPNLERLRDVMCSYVWEHLDVGYVQGMCDLLAPLLVTLDNDQLAYSCFSHLMKRMSQNFPNGGAMDTHFANMRSLIQILDSELFELMHQNGDYTHFYFCYRWFLLDFKRELLYEDVFAVWEVIWAARHISSEHFVLFIALALVEAYREIIRDNNMDFTDIIKFFNERAEHHDAQEILRIARDLVHKVQMLIENK
Protein: Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A) (P12643)
Organism: Homo sapiens (Human)
Function: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation. Stimulates also the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein receptor type-2
- Activin receptor type-2B
- Chordin
- Bone morphogenetic protein receptor type-1B
- Activin receptor type-2A
- Noggin
- Bone morphogenetic protein receptor type-1A
- Hemojuvelin
- Gremlin-1
- Repulsive guidance molecule B
Sequence:
MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
Protein: Histidine-containing phosphotransfer protein (F4JGC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU369004}. Nucleus {ECO:0000256|RuleBase:RU369004}.
Interaction partners:
- Putative two-component response regulator-like APRR6
- Putative two-component response regulator-like APRR4
- Putative two-component response regulator ARR19
- Putative two-component response regulator ARR21
- Two-component response regulator ARR18
- Putative two-component response regulator ARR13
- Two-component response regulator ARR14
- Two-component response regulator ARR11
- Putative two-component response regulator ARR20
- Two-component response regulator ARR2
Sequence:
MGFGSLGMDLNWIGYFVGSSGFLGFLDDQFTELKKLQDDGSPDFVAEVLSLFFEDCVKLISNMARALDKSTGTVDFGQMKLFSCTLVFDTVLVRRGSKLCVLASRNIAKLRITKGKLVQHRLRTHRLRCLQQVDIEYKTLTTKLQDMFNLEKQIIQAGGRVPQVDIN
Protein: Histone deacetylase HDT3 (HD-tuins protein 3) (Histone deacetylase 2c) (Q9LZR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Involved in the modulation of abscisic acid and stress-responsive genes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15144374}.
Interaction partners:
- Histone deacetylase 6
- Histone deacetylase 19
- WD40 repeat-containing protein HOS15
- Histone deacetylase 9
- Zinc finger CCCH domain protein
- SWI/SNF complex subunit SWI3B
- Histone deacetylase 15
- Histone deacetylase 5
- Histone deacetylase 2
- Histone deacetylase 17
Sequence:
MEFWGVEVKNGKPLHLDPGLDRLVHISQVALGESKNNVTEPIQLYVTVGSDKLLIGTLSHEKFPQLSTEIVLERNFALSHTWKNGSVFFSGYKVDASDPEPEDLIDDQLEAAGFKAAPKSAAKQVNFQLPNEDVKAKQDDDADGSEEDSSDDDDSENSGDEEEEKVTAESDSEEDDSSDDEEDDSSEEETPKKPEEPKKRSAEPNSSKNPASNKKAKFVTPQKTDSKKPHVHVATPHPSKQAGKNSGGGSTGETSKQQQTPKSAGAFGCKSCTRTFTSEMGLQSHTKAKHSAAA
Protein: Type IV secretion system protein virB4 (O50330)
Organism: Escherichia coli
Interaction partners:
Sequence:
MGAIESRKLLASETPVGQFIPYSHHVTDTIISTKNAEYLSVWKIDGRSHQSASEADVFQWIRELNNTLRGISSANLSLWTHIVRRRVYEYPDAEFDNVFCRQLDEKYRESFTGYNLMVNDLYLTVVYRPVSDKVLSFFAKRERETPDQKKHRQESCIKALEDINRTLGQSFKRYGAELLSVYEKGGHAFSAPLEFLARLVNGEHIPMPICRDRFSDYMAVNRPMFSKWGEVGELRSLTGLRRFGMLEIREYDDATEPGQLNVLLESDYEFVLTHSFSVLSRPAAKEYLQRHQKNLIDARDVATDQIEEIDEALNQLISGHFVMGEHHCTLTVYGETVQQVRDNLAHASAAMLDVAVLPKPVDLALEAGYWAQLPANWQWRPRPAPITSLNFLSFSPFHNFMSGKPTGNPWGPAVTILKTVSGTPLYFNFHASKEEEDATDKRLLGNTMLIGQSSSGKTVLLGFLLAQAQKFKPTIVAFDKDRGMEISIRAMGGRYLPLKTGEPSGFNPFQLPPTHANLIFLKQFVKKLAAAGGEVTHRDEEEIDQAITAMMSDSIDKSLRRLSLLLQFLPNPRSDDMDARPTVHARLVKWCEGGDYGWLFDNPTDALDLSTHQIYGFDITEFLDNPEARTPVMMYLLYRTESMIDGRRFMYVFDEFWKPLQDEYFEDLAKNKQKTIRKQNGIFVFATQEPSDALESNIAKTLIQQCATYIFLANPKADYEDYTQGFKLTDSEFELVRGLGEFSRRFLIKQGDQSALAEMNLGKFRTIVDGETVERDFDDELLVLSGTPDNAEIAESIIAEVGDDPAVWLPIFLDRVKAERSDV