wanglab/gogpt-training-data huggingface dataset:
Protein: Golgi apparatus protein 1 (E-selectin ligand 1) (ESL-1) (Golgi sialoglycoprotein MG-160) (Q62638)
Organism: Rattus norvegicus (Rat)
Function: Binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:2909545}; Single-pass type I membrane protein {ECO:0000255}. Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Note=Golgi medial cisternae (PubMed:2909545). Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (PubMed:31522887). {ECO:0000269|PubMed:2909545, ECO:0000269|PubMed:31522887}.
Interaction partners:
- E-selectin
- P-selectin
- Protein FAM234B
- Selectin P ligand
Sequence:
MAVCGRVRRMFRLSAALQLLLLVAAGVQNSHGQGQGLGVNFGPFAGQAGGGNPVGQQPPQLPQLSQQQQQQQPPPQQQQPFPAGGLPARRGGAGPGGTGGGWKLAEEESCREDVTRVCPKHTWSNNLAVLECLQDVREPENEISSDCNHLLWNYKLNLTTDPKFESVAREVCKSTISEIKECAEEPVGKGYMVSCLVDHRGNITEYQCHQYITKMTAIIFSDYRLICGFMDDCKNDINLLKCGSIRLGEKDAHSQGEVVSCLEKGLVKEAEEKEPKIQVSELCKKAILRVAELSSDDFHLDRHLYFACRDDRERFCENTQAGEGRVYKCLFNHKFEESMSEKCREALTTRQKLIAQDYKVSYSLAKSCKSDLKKYRCNVENLPRSREARLSYLLMCLESAVHRGRQVSSECQGEMLDYRRMLMEDFSLSPEIILSCRGEIEHHCSGLHRKGRTLHCLMKVVRGEKGSLGMNCQQALQTLIQETDPGADYRIDRALNEACESVIQTACKHIRSGDPMILSCLMEHLYTEKMVEDCEHRLLELQYFISRDWKLDPVLYRKCQGDASRLCHTHGWNETSELMPPGAVFSCLYRHAYRTEEQGRRLSRECRAEVQRILHQRAMDVKLDPALQDKCLIDLGKWCSEKTETGQELECLQDHLDDLAVECRDIVGNLTELESEDIQIEALLMRACEPIIHNFCHDVADNQIDSGDLMECLIQNKHQKDMNEKCAIGVTHFQLVQMKDFRFSYKFKMACKEDVLKLCPNIKKKVDVVICLSTTVRNDTLQEAKEHRVSLKCRKQLRVEELEMTEDIRLEPDLYEACKSDIKNYCSTVQYGNAQIIECLKENKKQLSTRCHQRVFKLQETEMMDPELDYTLMRVCKQMIKRFCPEADSKTMLQCLKQNKNSELMDPKCKQMITKRQITQNTDYRLNPVLRKACKADIPKFCHGILTKAKDDSELEGQVISCLKLRYADQRLSSDCEDQIRIITQESALDYRLDPQLQLHCSDEIANLCAEEAAAQEQTGQVEECLKVNLLKIRTELCKKEVLNMLKESKADIFVDPVLHTACALDIKHHCAAITPGRGRQMSCLMEALEDKRVRLQPECKKRLNDRIEMWSYAAKVAPADGFSDLAMQVMTSPSKNYILSVISGSICILFLIGLMCGRITKRVTRELKDR
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (A2AT91)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALEAVGKSENDLEGRILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASILEDDNEEEIESADQEEEAHPEYKFGNELSADDYSHKEAVANSVKKTSDDLEHENNKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQMRAMGIETSDIADVPSDTSK
Protein: Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O-methylguanine-DNA methyltransferase) (MGMT) (O-6-methylguanine-DNA-alkyltransferase) (P0AFH0)
Organism: Escherichia coli (strain K12)
Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
Interaction partners:
- DNA-3-methyladenine glycosylase 2
- p-aminobenzoyl-glutamate transport protein
- Universal stress protein E
- Alpha-ketoglutarate-dependent dioxygenase AlkB
- p-aminobenzoyl-glutamate hydrolase subunit A
- p-aminobenzoyl-glutamate hydrolase subunit B
- Fumarate and nitrate reduction regulatory protein
- Lipid-A-disaccharide synthase
- Putative acyl-CoA dehydrogenase AidB
- HTH-type transcriptional regulator AbgR
Sequence:
MLRLLEEKIATPLGPLWVICDEQFRLRAVEWEEYSERMVQLLDIHYRKEGYERISATNPGGLSDKLREYFAGNLSIIDTLPTATGGTPFQREVWKTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEGYLLL
Protein: RNA helicase (EC 3.6.4.13) (B7WN81)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGRGRGQQNPAFVPRPRDTPPQYGGHQAAQQFVKPDSKYKFTKPATEEAHEQVPVPADIALLNKFIQKEVKMMKDVVVDVQRQDPKSPLYSISSFRELRLKPEVLKALDTMNFQFPTRIQETALPLLLMEPPSNLIAQAQSGTGKTAAFVLTMLCRIDVNLMCPQCICLAPTLELAKQIGEVVEKMGKFIDNLKIHYAIKGGNMAAMRGRKLTEQIVIGTPGITRDYLQKYKCIDPSKIRCLVLDEADVMIYHQGFTDISTTIYNMVEDASDSVQSMLFSATYDEPVINFATKIIKNAIVVMLKREEQALPNIKQFYVQCACRDSKYAAIVNLYSGLAVASSVIFCHTKASVMWLYENMRARGHQVDVLHGDMTVVERADTIIHFKRGDFKVLITTNVFARGIDVAQVSVVINYDLPIKYTDEGTPMVVDGFTQPDCETYLHRIGRTGRFGKTGIAINLIDSEDSMNMINVLENHFQMKIARMDPSNLVELEAIEMA
Protein: Globin domain-containing protein (Q20638)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLLTTRPRFLFRQRSHSASSVSEKGASFSTPQANRKNKVNGNRRMSDSNNVAYSNGSKKVFEGDIEKWEPNVYEKELLRRTWSDEFDNLYELGSAIYCYIFDHNPNCKQLFPFISKYQGDEWKESKEFRSQALKFVQTLAQVVKNIYHMERTESFLYMVGQKHVKFADRGFKHEYWDIFQDAMEFALEHRLSIMTDLDDNQKRDAVTVWRTLALYTTVHMRNGFIDGLKGVNRFPPLV
Protein: Preprotein translocase subunit SECE1 (O23342)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the import/insertion pathway in the thylakoids. The signal recognition particle is not involved in the insertion of SECE1 in the thylakoid membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:10207046, ECO:0000269|PubMed:12054533}; Single-pass membrane protein {ECO:0000269|PubMed:10207046, ECO:0000269|PubMed:12054533}.
Interaction partners:
- Transmembrane protein
- Protein translocase subunit SECA2, chloroplastic
- Preprotein translocase subunit SCY2, chloroplastic
- Preprotein translocase subunit SCY1, chloroplastic
- Protein translocase subunit SECA1, chloroplastic
- Riboflavin synthase
- CAAX amino terminal protease family protein
- Splicing factor Cactin
- Probable phospholipid-transporting ATPase 12
- Heat shock protein 90-5, chloroplastic
Sequence:
MSLTAQFSPPVTGITRSLRDTKPSLSNLRVFPVYTEIRTMTTSNLRKSACFVAKAIEQRRDTAGSESESEATPSPAEESGSGEDKEVEISAIGAEIKAAMEQRKTAEEEKGKNEFLSGVAEEVKEIEWPAFQKVLGTTGVVLGVIAGSSVVLLTVNFLLAELSDRVFIGRGVQDFFS
Protein: Pro-neuregulin-2, membrane-bound isoform (Pro-NRG2) [Cleaved into: Neuregulin-2 (NRG-2) (Divergent of neuregulin-1) (DON-1) (Neural- and thymus-derived activator for ERBB kinases) (NTAK)] (O14511)
Organism: Homo sapiens (Human)
Function: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor.
Subcellular location: [Pro-neuregulin-2, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-2]: Secreted {ECO:0000250}.
Interaction partners:
- Receptor tyrosine-protein kinase erbB-3
- Receptor tyrosine-protein kinase erbB-4
- Pro-neuregulin-4, membrane-bound isoform
- Epidermal growth factor receptor
- Receptor tyrosine-protein kinase erbB-2
- Pro-neuregulin-3, membrane-bound isoform
- Pro-neuregulin-1, membrane-bound isoform
- Pro-epidermal growth factor
- Probetacellulin
- Proepiregulin
Sequence:
MRQVCCSALPPPPLEKGRCSSYSDSSSSSSERSSSSSSSSSESGSSSRSSSNNSSISRPAAPPEPRPQQQPQPRSPAARRAAARSRAAAAGGMRRDPAPGFSMLLFGVSLACYSPSLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLDKWPLRSGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLDTNGKNLKKEVGKILCTDCATRPKLKKMKSQTGQVGEKQSLKCEAAAGNPQPSYRWFKDGKELNRSRDIRIKYGNGRKNSRLQFNKVKVEDAGEYVCEAENILGKDTVRGRLYVNSVSTTLSSWSGHARKCNETAKSYCVNGGVCYYIEGINQLSCKCPNGFFGQRCLEKLPLRLYMPDPKQKAEELYQKRVLTITGICVALLVVGIVCVVAYCKTKKQRKQMHNHLRQNMCPAHQNRSLANGPSHPRLDPEEIQMADYISKNVPATDHVIRRETETTFSGSHSCSPSHHCSTATPTSSHRHESHTWSLERSESLTSDSQSGIMLSSVGTSKCNSPACVEARARRAAAYNLEERRRATAPPYHDSVDSLRDSPHSERYVSALTTPARLSPVDFHYSLATQVPTFEITSPNSAHAVSLPPAAPISYRLAEQQPLLRHPAPPGPGPGPGPGPGPGADMQRSYDSYYYPAAGPGPRRGTCALGGSLGSLPASPFRIPEDDEYETTQECAPPPPPRPRARGASRRTSAGPRRWRRSRLNGLAAQRARAARDSLSLSSGSGGGSASASDDDADDADGALAAESTPFLGLRGAHDALRSDSPPLCPAADSRTYYSLDSHSTRASSRHSRGPPPRAKQDSAPL
Protein: DNA damage-binding protein 1 (Q5BFT4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin ligase subunit CulD, putative
- WD repeat protein
- WD repeat protein
- RING-box protein 1
- DNA damage-binding protein cmr1
- WD repeat-containing protein
- WD repeat protein
- Uncharacterized protein
- non-specific serine/threonine protein kinase
- COP9 signalosome complex subunit 1
Sequence:
MSYIAPIHRASSIRHALKLHFLNAEDECLVVAKANQLEFYSVTPDGLALVTSCSIFARVTMLACLPAPANSPTDHLFVGTDRYSYFTLSWDSARNQVRTERDYVDIADPSSRDARTGSRCMIDPSGRFMTLEIYDGMIVVIPIIQLPSKRRGRQVALPTGPDAPRIGELGEPIITRIDELFVRSSAFLHVQAGSPRLALLYEDNQKKVKLKVRELKYSTAAGAESEFTSIADYAQELDLGASHLIPVPAPLAAAGGLLILGETSIKYVDADNNEIVSQPLEEATIFVAWEQVDSQRWLLADDYGRLFFLMLVLRNSEVERWELHSLGNTSRASVLVYLGGGVVFVGSHQGDSQVIRIGDQSFQVIQTLSNIAPVLDFTIMDLGNRTSENQMHEFSSGQARIVTGSGAFDDGTLRSVRSGVGLEELGVLGDMEHITDLWGLQVGSRGDFLDTLLVTFVNETRVFRFSPDGEAEELESFLGLSLSENTLLAANLPGSRILQVTEQRVLIADIECGMTIFEWTPKNQLIITAASANDDTIVLVAGGKHVTVLDIQSEARVVSEKDFGADNQISGVTLPTTPTDVCIVGFPQLAKVSVLKLQDLSHISSTSLGPAGEAFPRSVLVASVLAENAPTLFISMADGSVITYDYNDQDHSLSGMNKLVLGSEQPTFKKLPRGNGLSNVFATCENPSLIYGSEGRIIYSAVNSEGASRICHFNSEAYPESIAVATAQELKIGLVDKERTTQIQTLPIKATVRRVAYSPSEKAFGMGTIERKLVSGEEIVKSQFVLADEILFRRLDAFDLEGEEIVECVIRAEAPESKDGEAKDRFVVGSAYLGEDDGDSTLGYIRVFEVDNGRKLAKVAQERVKGACRALAVMGDKIVAALVKTVVVFQVVPRSGGLQLQRLASYRTSTAPVDITVTRNVIAIADLMKSVCVVEYHEGENGAPDKLVEVARHFQTVWATGVTSVAPDTYLESDAEGNLIVLRRNRSGVEEDDRRRLEVTGEICLNEMVNRIRPVNIQQLPSATVVPRAFLATVEGSIYLYAIINPDYQDFLMRLQATMASRADSLGGIPFTDYRAFRTMTRQATEPYRFVDGELIERFLTCEPAVQKEIVDIVGSSLEEVRAIVEALRRLH
Protein: Antifungal protein ginkbilobin-like protein 2 (Embryo-abundant protein 35) (Q40858)
Organism: Picea glauca (White spruce) (Pinus glauca)
Function: Exerts antifungal activity through its carbohydrate-binding specificity.
Interaction partners:
Sequence:
MSMGSFGFALAVMVLAVLVASAAGAPNTNLVSSACNGNKIPSGNPFFNNLGALLVDLEKNTAFSGFDYKASRAGSGGAPTAYGRGVCKQSISQSDCTACLTNLGGRIWGISKNAIGARVQLTDCFIRYEQYSI
Protein: Integrin beta-7 (Gut homing receptor beta subunit) (P26010)
Organism: Homo sapiens (Human)
Function: Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT). Integrin alpha-4/beta-7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract. Interacts also with VCAM1 and fibronectin, an extracellular matrix component. It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin. Binds to HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease. Interaction would involve a tripeptide L-D-I in HIV-1 gp120. Integrin alpha-E/beta-7 (HML-1) is a receptor for E-cadherin.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Integrin alpha-4
- Integrin alpha-E
- Mucosal addressin cell adhesion molecule 1
- Integrin alpha-5
- Fibronectin
- Integrin alpha-L
- Filamin-A
- Vascular cell adhesion protein 1
- Integrin alpha-10
- Integrin alpha-11
Sequence:
MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSAANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVVQLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKREGKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRALGFSEELIVELHTLCDCNCSDTQPQAPHCSDGQGHLQCGVCSCAPGRLGRLCECSVAELSSPDLESGCRAPNGTGPLCSGKGHCQCGRCSCSGQSSGHLCECDDASCERHEGILCGGFGRCQCGVCHCHANRTGRACECSGDMDSCISPEGGLCSGHGRCKCNRCQCLDGYYGALCDQCPGCKTPCERHRDCAECGAFRTGPLATNCSTACAHTNVTLALAPILDDGWCKERTLDNQLFFFLVEDDARGTVVLRVRPQEKGADHTQAIVLGCVGGIVAVGLGLVLAYRLSVEIYDRREYSRFEKEQQQLNWKQDSNPLYKSAITTTINPRFQEADSPTL
Protein: Calcium-dependent protein kinase 5 (EC 2.7.11.1) (Calmodulin-domain protein kinase CDPK isoform 5) (Q38871)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Respiratory burst oxidase homolog protein D
- Respiratory burst oxidase homolog protein F
- Respiratory burst oxidase homolog protein B
- Serine/threonine-protein kinase BIK1
- Exocyst complex component EXO70B1
- Calcium-binding protein CP1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Guard cell S-type anion channel SLAC1
- Mitogen-activated protein kinase 6
- Mitogen-activated protein kinase 3
Sequence:
MGNSCRGSFKDKLDEGDNNKPEDYSKTSTTNLSSNSDHSPNAADIIAQEFSKDNNSNNNSKDPALVIPLREPIMRRNPDNQAYYVLGHKTPNIRDIYTLSRKLGQGQFGTTYLCTEIASGVDYACKSISKRKLISKEDVEDVRREIQIMHHLAGHGSIVTIKGAYEDSLYVHIVMELCAGGELFDRIIQRGHYSERKAAELTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDDDFSLKAIDFGLSVFFKPGQIFTDVVGSPYYVAPEVLLKRYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGYIDFESDPWPVISDSAKDLIRRMLSSKPAERLTAHEVLRHPWICENGVAPDRALDPAVLSRLKQFSAMNKLKKMALKVIAESLSEEEIAGLREMFQAMDTDNSGAITFDELKAGLRKYGSTLKDTEIHDLMDAADVDNSGTIDYSEFIAATIHLNKLEREEHLVAAFQYFDKDGSGFITIDELQQACVEHGMADVFLEDIIKEVDQNNDGKIDYGEFVEMMQKGNAGVGRRTMRNSLNISMRDA
Protein: enoyl-CoA hydratase (EC 4.2.1.17) (Q7JR58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Isovaleryl-CoA dehydrogenase, mitochondrial
Sequence:
MANIAKIFASRAQCVLQAAARQPQVATRFSSSSTNNNWEYIKTEVAGEGKNVGVITLNRPKALNALCNGLMKELSTALQQFSKDKTISAIVLTGSEKAFAAGADIKEMVGNTYSQCIQGNFLNDWTEVARTQKPIIAAVNGYALGGGCELAMMCDIIYAGDKAKFGQPEIALGTIPGAGGTQRLTRVVGKSKAMEMCLTGNMIGAQEAEKLGLASKVVPADQLLGEAVKLGEKIGTHSNLIVQLCKEAVNTAYETTLQEGLKFERRTFHATFSTADRKEGMTAFAEKRPAKFTNE
Protein: Kinase (EC 2.7.-.-) (Q6PBN6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Inositol-pentakisphosphate 2-kinase
- Kinase
- Kinase
Sequence:
MSPAIEGMQTEPQGFLGKGVLLEPFVHQVGGHSCVLRFGEQTICKPLIPREHQFYKSLPAAMRKFTPQYRGVVSVSFEEDEEGNLCLIAYPLHNELGDLENVDPSADLEPNNKITWVSKMLLDNDSYSKERSRHARKDKDKSVKREEELEWLKQAEVFYYSLERSNAAGPQLKHNPWSLKCHQQHLQRMKENAKHRNQYKFILLENLTWSYAVPCVLDLKMGTRQHGDDASEEKKAMQIRKCQQSTSASIGVRLCGMQVYHPATGQLMFMNKYHGRKLTLSGFKEAIFQFFHDGRRLRRELLSPVLRRLRDMQAALEACESYRFYSSSLLIIYDGDPPRTRHSAEDGLSEEEEEEDDDDDEEEEEEEEEEGAAFGFPHGAGAASSSSGACGGGSSTSSSSVVRRMARSDSGPAVDVRMIDFAHTTCRHYGEDSVVHEGQDSGYIFGLENLITIISQLEDHSTD
Protein: Protein kinase gsk3 (EC 2.7.11.1) (Protein kinase skp1) (Q10452)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Interacts with cdc14 which is thought to play a role in the initiation and completion of mitosis. Involved in the positive regulation of mis12.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Regulator of G-protein signaling 1
- Tuberous sclerosis 1 protein homolog
Sequence:
MNHGTKIPVDPFRIIKETARDGSTGEVKQLSYTSSKVVGSGSFGVVMQVHLIESDSKAAIKRVLQDKRFKNRELQIMRIMKHPNIVDLIAYYYTTGDNSDEVYLNLVLEFMPETIYRASRLYTRQKLSMPMLEVKLYIYQLLRSLAYIHASGICHRDIKPQNLLLDPENGILKLCDFGSAKILVAGEPNVSYICSRYYRAPELIFGATDYTHAIDIWSTGCVMAELMLGHPLFPGESGIDQLVEIIKILGTPSREQIKTMNPNYMEHRFPQIRPQPLSRVFSRSVPLDALDLLSKMLQYTPTDRLTAAEAMCHPFFDELRDPNTKLHNSRNPDASPRHLPELFNFSPFELSIRPDLNQKLIPSHARDALPVKLDDFVPIPIHRARID
Protein: PHD finger protein 6 (Q5JRC6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEAADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYK
Protein: Glycine receptor alphaZ2 subunit (Glycine receptor, alpha 4a) (Q9DES9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MTHFSLIITDCINCSFCHVYFSGFFSISLPLCFLYLWQKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINSFGSITETTMDYRLNVFLRQQWNDPRLAYSEYPDASLDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFQNGNVLYSIRLTLILSCPMDLKNFPMDIQTCTMQLESFGYTMNDLIFEWLSDNPVQVADDLTLPQFVLKEEKDLGYCTKHYNTGKFTCIEVKFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLIVFAALLEYAAVNFVSRQHKEFIRLRKKQRRQRIEEDLVRESRGFYFRGYGLGHCLQTKDGTAVEGSSVFAPPPPVQVLYDGEAVRKRFVDRAKRIDTISRAVFPLSFLIFNVFYWITYKVLRHEDIHANP
Protein: Cadherin-1 (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3] (Q9R0T4)
Organism: Rattus norvegicus (Rat)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:P12830}. Cell membrane {ECO:0000250|UniProtKB:P12830}; Single-pass type I membrane protein. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000250|UniProtKB:P09803}. Cell junction, desmosome {ECO:0000250|UniProtKB:P12830}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane (By similarity). Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (By similarity). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P09803, ECO:0000250|UniProtKB:P12830}.
Interaction partners:
- Catenin beta-1
- Killer cell lectin-like receptor subfamily G member 1
- Junction plakoglobin
- Catenin delta 1
- Cadherin-2
- Catenin alpha-1
- Ras GTPase-activating-like protein IQGAP1
- Receptor protein-tyrosine kinase
- Occludin
- Tight junction protein ZO-1
Sequence:
MGARCRSFSALLLLLQVSSWLCQQPESESDSCRPGFSSEVYTFLVPERHLERGHILGRVKFEGCTGRPRTAFFSEDSRFKVSTDGVITVKRHLKLHKLETSFLVHAWDSSYRKLSTKVTLKSLGHHHHRHHHRDPVSESNPELLTFPSFHQGLRRQKRDWVIPPINCPENQKGEFPQRLVQIKSNRDKETTVFYSITGPGADKPPVGVFIIERETGWLKVTQPLDREAIDKYLLYSHAVSSNGEAVEDPMEIVVTVTDQNDNRPEFIQEVFEGSVAEGALPGTSVMQVSATDADDDINTYNAAIAYTILSQDPELPHKNMFTVNRDTGVISVVTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPIFNPSTYQGQVLENEVGARIATLKVTDDDAPNTPAWNAVYTVVNDPDHQFTVITDPKTNEGILKTAKGLDFEAKQQYILHVTVENEEPFEGSLVPSTATVTVDVVDVNEAPIFVPAEKRVEVPEDFGVGLEIASYTAREPDTFMEQKITYRIWRDTANWLEINPETGVISTRAEMDREDSEHVKNSTYTALIIATDDGSPIATGTGTLLLVLSDVNDNAPIPEPRNMQFCQRNPKPHVITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAEQESLILQPRKDLEIGEYKINLKLSDNQNKDQVTTLEVHVCDCEGTVNNCMKAISLEAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVIRNDVAPTLMSMPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEED
Protein: WW domain-containing oxidoreductase (EC 1.1.1.-) (Q91WL8)
Organism: Mus musculus (Mouse)
Function: Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm (By similarity). May also play a role in tumor necrosis factor (TNF)-mediated cell death. Required for normal bone development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19366691}. Nucleus {ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}. Mitochondrion {ECO:0000269|PubMed:11058590}. Golgi apparatus {ECO:0000250|UniProtKB:Q9NZC7}. Lysosome {ECO:0000250|UniProtKB:Q9NZC7}. Note=Partially localizes to the mitochondria (By similarity). Translocates to the nucleus in response to TGFB1 (PubMed:19366691). Translocates to the nucleus upon genotoxic stress or TNF stimulation (PubMed:11058590). Localized to the lysosome probably upon binding to VOPP1 (By similarity). {ECO:0000250|UniProtKB:Q9NZC7, ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}.
Interaction partners:
- Transcription factor AP-2 gamma
- Receptor tyrosine-protein kinase erbB-4
- Bis
- Transmembrane protein 207
- Cellular tumor antigen p53
Sequence:
MAALRYAGLDDTDSEDELPPGWEERTTKDGWVYYANHTEEKTQWEHPKTGKRKRVAGDLPYGWEQETDENGQVFFVDHINKRTTYLDPRLAFTVDDNPTKPTTRQRYDGSTTAMEILQGRDFTGKVVLVTGANSGIGFETAKSFALHGAHVILACRNLSRASEAVSRILEEWHKAKVEAMTLDLAVLRSVQHFAEAFKAKNVSLHVLVCNAGTFALPWGLTKDGLETTFQVNHLGHFYLVQLLQDVLCRSSPARVIVVSSESHRFTDINDSSGKLDLSRLSPPRSDYWAMLAYNRSKLCNILFSNELHRRLSPRGVTSNAVHPGNMMYSAIHRNSWVYKLLFTLARPFTKSMQQGAATTVYCAVAPELEGLGGMYFNNCCRCLPSEEAQSEETARALWELSERLIQDRLGSPSS
Protein: E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8 (EC 2.3.2.27) (RING finger protein slx8) (RING-dependent E3 ubiquitin-protein ligase slx8) (RING-type E3 ubiquitin transferase slx8) (Synthetic lethal of unknown function protein 8) (P87176)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Acts as a critical suppressor of gross chromosomal rearrangements (GCRs) during normal cell cycle progression. Involved in stabilizing, restarting or resolving transiently stalled replication forks. Prevents accumulation of DNA damage during cell cycle progression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:17762865}.
Interaction partners:
- E3 SUMO-protein ligase pli1
- Peroxisome assembly protein 12
- E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1
- Ubiquitin-like protein pmt3/smt3
- E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp2
- DNA repair protein rad60
- Uncharacterized protein C17C9.14
- SUMO-conjugating enzyme ubc9
- Ubiquitin-conjugating enzyme E2 4
- E3 SUMO-protein ligase nse2
Sequence:
MPPAHKRDTNVRNLSAPYNIPSQSARVAAGNAAINRRRSSPVENSPGNGFPVSEDATDYPSGTTSENESLPLNRAPRSLREVASELAQEETLPVETSDLNIDVESEVFDLEDINFQNDADDINQRFTYNNHPASVENSLTNVNSIHAQPTTISDMIDLTDETSYDPRKQKFEQGKNPSTTNAEIEKEEPSKKQVVPSSQRLADYKCVICLDSPENLSCTPCGHIFCNFCILSALGTTAATQKCPVCRRKVHPNKVICLEMMLGSQKKKS