wanglab/gogpt-training-data huggingface dataset:
Protein: FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP and FKBP-like) (WAFL) (Q6P9Q6)
Organism: Mus musculus (Mouse)
Function: Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement (By similarity). May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16756961}. Cell projection, axon {ECO:0000269|PubMed:16756961}. Early endosome {ECO:0000269|PubMed:16756961}. Note=Present in axons and neuronal growth cones. {ECO:0000269|PubMed:16756961}.
Interaction partners:
- WASH complex subunit 2
- WASH complex subunit 5
- TBC1 domain family member 5
- Syntaxin-5
- Golgi SNAP receptor complex member 1
- Vacuolar protein sorting-associated protein 29
Sequence:
MFGAGDEDDTDFLSPSGGAKLASLFGLDQATMGHGNEFFQYTAPKQPKKGQGTAAGNQTAPKPAPATTGTSSVLFATAVHAYRYINGQYAKQGKFGAAVLGNHTSREYRILLYISQQQPVTVATIHLNFELMVRPNNYSTFYDDQRQNWSIMFESEKAAVSFNKQVCVAKCNSISSLDAVLCQDLVAAEGPAVETGDSLEVAYTGWLLQNHVLGQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACAAGSEGVIGWTQPTDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAAPSPIPASDSLSADPVVTPLPLPLKPGEPGLRSKSNSLSEQLTVNSNPDTVKAKLISRMAKMGQPMLPILPPQLDSNDSETEDATVLRGAGQSLVTPSIQPSLQPAHPVLPQMASQAPQPSGSGLQTPSAALMQAVSLDSHSAVSGNAQNFQPYAGVQAYAYPQTPSVTSQLQPVRPLYPAPLSQAPHFQGSGDMMSFLMTEARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQPGPATPGMPPAPPSGETQEAPEVLPEQVVGETTPLPLQALPTPENGAQTRKGEPAEAEVPSEIKDSSLPPQPAGIPAHRVLGPPTSIPPKPPGPVTMDSESEEMLAADQRTVQPNGLLGEEHVREVATDGLLQGNSRRLSLTPDPEKGEPPALDPESQGGEAQPPECKQAEDVSSSGPRETLLDTELASAAAGTSLRHNQDSQHCSLSGDEEDELFKGATLKVPRPTAQPEEEDEDEVSMKGRPPPTPLFGDDDDDDDDDIGWLG
Protein: Vacuolar protein sorting-associated protein 29 (Q9UTI5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor pep1/vps10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be involved in cargo selection.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Vacuolar protein sorting-associated protein 17
- Vacuolar protein sorting-associated protein vps5
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26
- Sorting nexin-3
- Vacuolar protein sorting/targeting protein 10
- Inosine triphosphate pyrophosphatase
- Vacuolar protein sorting-associated protein 9b
- Vacuolar protein sorting-associated protein vps901
- Sorting nexin-4
Sequence:
MLVLVIGDFHIPDRAPKLSEKFRQLLIPGKISQIICLGNLTSTSVYEYLKHVCSDLKLVKGAFDISSKAPIAGKITLGSFKIGYTNGHLVVPQDSPEALSILAREMDADILLFGGTHKFAAYELDGCFFVNPGSATGAPNVSAVEDDEKIVPSFVLMDVQGAVLILYVYRIFDGEVRVEKMQYRKPE
Protein: Sulfiredoxin, chloroplastic/mitochondrial (AtSRX) (EC 1.8.98.2) (Q8GY89)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. Required to switch on the antioxidant pathway to regenerate the oxidative damage. In mitochondrion, catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent.
Subcellular location: Plastid, chloroplast. Mitochondrion.
Interaction partners:
- 2-Cys peroxiredoxin BAS1, chloroplastic
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- 1-Cys peroxiredoxin PER1
- NADPH-dependent thioredoxin reductase 3
- Peroxiredoxin-2F, mitochondrial
- Peroxiredoxin Q, chloroplastic
- Peroxiredoxin-2E, chloroplastic
- DEAD-box ATP-dependent RNA helicase 55
- Thioredoxin-like protein CDSP32, chloroplastic
Sequence:
MANLMMRLPISLRSFSVSASSSNGSPPVIGGSSGGVGPMIVELPLEKIRRPLMRTRSNDQNKVKELMDSIRQIGLQVPIDVIEVDGTYYGFSGCHRYEAHQKLGLPTIRCKIRKGTKETLRHHLR
Protein: Mechanosensitive ion channel protein 6 (Mechanosensitive channel of small conductance-like 6) (MscS-Like protein 6) (Q9SYM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mechanosensitive ion channel protein 2, chloroplastic
- Mechanosensitive ion channel protein 3, chloroplastic
- Mechanosensitive ion channel protein 1, mitochondrial
- Casparian strip membrane protein 4
- AT4g33900 family protein)
- Protein MID1-COMPLEMENTING ACTIVITY 1
- Protein MID1-COMPLEMENTING ACTIVITY 2
- Extracellular ligand-gated ion channel protein
- At1g13195
- AT5g37540/mpa22_p_70
Sequence:
MAVDAADRREVIVKIDGENGNNNGVSGETVGKIWRDGSYDFWTDGEGNLNKGHNAAAVDSDRSAATTGEQQKDEGFEFRRGEDPPTKLIGQFLHKQQASGEICLDMDLGMDELQSRGLTPVSESPRVSTKRDPVGRRDSRSNTNNNDDGEVVKCSGNNAPIQRSSSTLLKMRTRSRLSDPPTPQLPPQTADMKSGRIPKSGQMKSGFFGKSPKTQGEEEEDDPFAAEDLPEEYRKDKLSLWIVLEWLSLILIIAGFVCTLAIPSLRKKKLWELQLWKWESMVLVLICGRLVSSWIVKIVVFFIERNFLLRKRVLYFVYGVRKAVQNCLWLGLVLLAWHFLFDEKVAKAANTKALRVVTKIFVCLLVGFLLWLVKTLLVKVLASSFHMSTYFDRIQESLFTQYVIETLSGPPLIEIQKNEEEEERISVEVKKFQNPGGVEIQSGAQKSPMKTGKSPFLSHVLSNGGGGGGENKGITIDSLHKLNPKNVSAWKMKRLMNIIRNGSLTTLDEQLQDPSLDDDKGNQIRSEFEAKLAARKIFHNVAKPGSKFIYANDIMRFLPDDEALKTLSLFEGASETNRISKSSLKNWVVNAFRERRALALTLNDTKTAVNRLHKMVNIVVGIIILVIWLIILGITSTKFLVVMSSQVVVVAFIFGNMCKIVFESIIYLFVIHPFDVGDRCEIDGVQMVVEEMNILTTVFLRFDNQKVVYPNSLLWTKSIGNYYRSPDMGDGIEFSIHITTPAEKIILIKQRITSYIEGKKDHWYPAPMIVFKDMESLNSVRIAVWPTHRMNHQDMGEKWARRSQLVEEIAKICRELDIEYRLYPLDINVRNLPTSTALPVSDRLPPNWSAPASGSN
Protein: Reticulon-like protein (Q54CA6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}.
Interaction partners:
- GTP cyclohydrolase 1
- Vacuolar protein sorting-associated protein VTA1 homolog
- J domain-containing protein
- Protein SEY1 homolog
- SMP-LTD domain-containing protein
- SMP-LTD domain-containing protein
- Bacterial surface antigen
Sequence:
MEDTQEQIEQVEQQVEETVEKVKEEATEKVEAAIEEVKEDINKLKNDVKGVAENVSNVVSSKIEATTSSAKATINDIKDGVKQVVSGNSGCPYSMNGEFSMCSQVCKVSKVVQKNPSFECVKKIVLWEDIVQTGILFAIINLVFILISFCNYSLISLFGYTAFTVTITSILFHLISLILSKYVQGVSLNNQFTDQLKTLSFHIHDAVIEKQVNNVAELINTVLSIAKDVFGCKSVYLSAQFAIVFYLIGCLSKCLSNTAILYFGFLVSFVVPRLYVEKKEVIDQQFSKVCALAKEPLSKLHSLIPQSQTTSTKKSN
Protein: Mitochondrial SSU ribosomal protein (Q387C7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Mitochondrial SSU ribosomal protein
- Ubiquitin-like domain-containing protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MRRWHRSLNPALFGERGSGHYFSTTRARLQLQAQDRIICGTHGAGIVAHQTAVNSSDNPMLSSVTTAAPAADLSRTKPHEGTGTSERDPYIRTLHNQRSAAPESSVLQSHTVNAPTVDECEMLAERWGTMNYWHNDTFPRLVVLLKKLLVPDVSPLSPTAESLLSMFEKVVIPKLTSDEEDRRKLVSLWSETTLQAEAAVTKFLFQRGSFESMLHRIITDALEKMSTLALGGQEGNLALEALKRQTLFKRNDFIQKRLIDVVSNSAYLGYGDSVWQVFFAAVEANEENLLSDRATTDAIRAAWEGVMREDVVRLPDVTGVVALYLTLVCIRESGRLVPVELKELSSGLEDGVRPGVRKLQQYPLIFLHPTVKRRFVVKAVAEILHNSSSNAFSNMLRENGLHDTAREVALCEAMNRNKELAEGDVGDAVGRFVSKGEVKTLLSSLVSGTDAVVRDAVAGIFGIGTTITIDWDAVMQNVDWSNNWQRLATALLSNSAVLSAIVKLVKNAIGAKGMSKHLFTDEYADQLQLILDAREERAASRKQRIENIAQELSSFERVDLSCDLLRKLGVDMTELDTAAAATRNMNVVQRPCIEDGLLSLVLEAVTKRHPNWVKAGVIQTTLKDPFDALRWMMHIFIRLSYVPHAGAATIARLSRRRIGPIGLEPHQFNVPAELGFVEQYDNLQYKRYDWQGWYQRMLDVHNRNVSLRCRICDLQRLDGNGVQFVDMQTERRLRILAQHRVGMGVLKLDADKYEDQADNVTFGTTKLSELLADARKAQLGEEYWPSVELKVRKPSGQSKAHYSLIDNERIEKRSRELYEKYRDAKKRSLFVTPMETWLEVKGMQVRKSVDNADEDGYTLDALQDMMDGDDEDKV
Protein: PTEN upstream open reading frame MP31 (Micropeptide 31) (Mitochondrial lactate dehydrogenase regulator) (C0HLV8)
Organism: Homo sapiens (Human)
Function: Inhibits lactate dehydrogenase (LDH)-mediated conversion of lactate to pyruvate in mitochondria by competing with mitochondrial LDH for binding to NAD(+). Also inhibits cellular lactate utilization.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:33406399}.
Interaction partners:
Sequence:
MWRDSLCAAAGYALGAGTRLRSVLSSRKLQP
Protein: Sphingosine-1-phosphate lyase 1 (S1PL) (SP-lyase 1) (SPL 1) (hSPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase) (O95470)
Organism: Homo sapiens (Human)
Function: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP (By similarity). Seems to play a role in establishing neuronal contact sites and axonal maintenance (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14570870}; Single-pass type III membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8R0X7}.
Interaction partners:
- Sphingosine kinase 2
- Sphingosine kinase 1
- Sphingosine-1-phosphate phosphatase 1
- Sphingosine-1-phosphate phosphatase 2
- Phospholipid phosphatase 3
- Phospholipid phosphatase 2
- A disintegrin and metalloproteinase with thrombospondin motifs 14
- Sphingosine 1-phosphate receptor 2
- Ceramide synthase 6
- Serine palmitoyltransferase 1
Sequence:
MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH
Protein: [histone H3]-trimethyl-L-lysine(9) demethylase (EC 1.14.11.66) (C8VTU6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Histone H2A.Z
- Serine/threonine-protein kinase tel1
- SUMO-conjugating enzyme UBC9
- B-zip transcription factor
- Ubiquitin-like domain-containing protein
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- Double-strand break repair protein
- DNA repair protein RAD50
- Histone H4.2
- Histone H4.1
Sequence:
MAATIDRPLFEPIAGGPATDAASITPPHSINGKKDGPDGAPSELSDLELDSKPTDAQEDISVEEGDQEIEPDHYYGGGKIPVFKPFRDFQSFIKRIDKYGMRSGVVKVIPPKEWRDALPPLDEAVKKIRVKNPIMQEFHGSHGTYTQANIEKQRSYNLPQWKALCEDGSHQPPARRGERRRNQERVTRAPSAPKAQTTRADTPKRGPGRPAKRSNQAKVKEEPVKIKEEPAADEVMEKIKPEGPPTPVSPESIPAETKSEALSDGESLSAPKSRGRQPKSVTARRKQNKGDTVEHVDEEAYKNFDYRIHDNEDYTPERCEELETAYWKSLMFNNPMYGADMPGSLFDDRITSWNVAKLPNLLDVIGQKVPGVNTAYLYLGMWKATFAWHLEDVDLYSINYIHFGAPKQWYSISQEDAPRFEQAMKSIWPSDAKTCDQFLRHKTYLVSPSLLKSQYGITVNKMVHYEGEFVITYPYGYHSGYNLGYNCAESVNFATEKWLDYGRVAKKCNCEADSVWIDVEEIERKLRGELTPEYYGEYDSDLDGYEAASDLLTPPRSVPEKTSNRGRKRKHDGDMNKAKRMRADMGIPRRLPCLLCPNDLDYEDLLPTEDGKSHAHRRCALYTEETSILRDGSGKEVVCDIDKIPKARMGLKCLYCREVRGACFQCNFGKCTRSYHATCALLAGVQVEEGLVTVVADDGSQYSVPSVDLKCKYHRQKKPTWMTSSESPENDRKLMDTARRLVTGDILQFQADKEIYGAVVIENRVAERTLQVKVLPRGDVIELPYRWMLVVRRSNFAPLAAGIKPLPAHLSRKPEGRRELESALPVAGNPFGDGRSPYQWAEFETVDSTNRPAAPPAVQVDLGKMEQIWYYLGQSSTECRAQYTHNPSVPIHNPRSNFLDSVKSLGAVMARLPSYPHHRLPSYVLTTPPPHLLSSAAATTTASAVAAAAASRPLLPPRPPFAPPRSSPAAPTSAAVAASAMPSAYRSLPNQIARHAPYPQVTKAHLQSQQQHSHQQQQQNTNGSHSTANSHLPANNFANVRELIARRRLAQITDHANVFAGYTIVGPELVVETLLGPMGSVPPSNGLEKLELAMAQQRVQPRAPDGTLLPMQPLNMRSEEVTRLLQMLRFSLISHRDRLDVLQKKETETAKQEAANKVKGATPKLPRKYAYLELQREQAPTVYQSPYDMPSGFTEYARTTFGLTRHEPELPKPSLANDYFASLSPENQEKILKTCGSFVQRAIERSAPHSRQSSSSNFRLASALAQQTENPTIDITTVENMPLSGLDFPLRADSPCSNFSRSHLRFHSPNDFSHHGTEVHHDHHDLFGDQQANTRFWQHGPWAAGDGNTPNEENRPFFGPHERLKHDYASSDISLGRGGPGSLHSVDMAGFGLDNPDDLCAALSP
Protein: L-rhamnose 1-dehydrogenase (NADP(+)) (RHAD) (EC 1.1.1.377) (Q9HK58)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Involved in the non-phosphorylated metabolic pathway of L-rhamnose catabolism. Catalyzes the oxidation of L-rhamnose to yield L-rhamnono-1,4-lactone. It can also oxidize L-lyxose and L-mannose, and uses only NADP.
Interaction partners:
- Sorbitol dehydrogenase related protein
Sequence:
MLDFKGKNAVITGGSRGIGRAIALGLAKQGANILISYASHDSEADEVLETASKYGVKAHKVKVDQSDPYESIRFAEKAIETFGKVHILVDNAGICPFEDFFRISVDLFEKVWKVNVESHYFITQRIAKNMIENKINGRILLISSISAHVGGEFQTHYTTTKSALNGFMHSIAIVLGKYGILVNSLEPGTILTDINKEDLSNQEKRAYMERRTVVGRLGLPEDMVAPALFLLSDDNTYVTGTELLADGGMLINLQ
Protein: Subtilase cytotoxin subunit A (EC 3.4.21.-) (Q6EZC2)
Organism: Escherichia coli
Function: Protease subunit of subtilase cytotoxin SubAB5. An endoprotease specific for host endoplasmic reticulum (ER) chaperone BiP/HSPA5, has no activity on human HSP70 or HSPA8. Cleaves between 'Leu-416' and 'Leu-417' of BiP/HSPA5 in the hinge between BiP's ATPase and protein-binding domains. This induces host ER stress response and eventual cell death. Culture supernatant of E.coli expressing both subA and subB are toxic for Vero cells (African green monkey kidney cell line), Chinese hamster ovary cells and Hct-8 cells (human colonic epithelial cell line); the subunits are not toxic individually. Purified SubAB5 is highly toxic, <0.1 pg is able to kill at least 50% of 30'000 Vero cells in a microtiter plate assay after 3 days; no cytotoxicity is seen at 24 hours. Preabsorption with cells expressing a ganglioside GM2 mimic reduced cytotoxicity of SubAB5 by 93% in the Vero cytotoxicity assay. Intraperitoneal injection of 200 ng of purified SubAB5 kills mice; the higher the dose the faster the mice die. Animals injected intraperitoneally with purified SubAB5 have microvascular thrombi in the brain and other organs, including the renal tubules and glomeruli. Injection induces an unfolded response in mice. Mice fed E.coli cells expressing cloned SubAB5 experience drastic weight loss and appear ill and lethargic. Protein synthesis in Vero cells is transiently inhibited by SubAB5; both subunits are required for this effect. Inhibition of protein synthesis is prevented by brefeldin A; cells are arrested in the G1 phase. SubAB5 at 100 ng/ml induced caspase-dependent apoptosis in Vero cells through mitochondrial membrane damage.
Subcellular location: Secreted {ECO:0000269|PubMed:15226357}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:15226357, ECO:0000269|PubMed:17101670}. Host endoplasmic reticulum lumen {ECO:0000305|PubMed:17024087, ECO:0000305|PubMed:18005237, ECO:0000305|PubMed:23921389}. Note=Colocalizes with host BiP/HSPA5 in the endoplasmic reticulum of Vero cells, its activity on BiP/HSPA5 is blocked by pretreatment with brefeldin A, which disrupts the Golgi apparatus and inhibits retrograde transport from the cell surface to the Golgi (PubMed:17024087, PubMed:18005237). Using different inhibitors it has been shown to be actively internalized by membrane-bound vesicles and undergoes clathrin-dependent retrograde transport, via early endosomes and the Golgi network, to the endoplasmic reticulum (PubMed:18042253). Trafficking is similar in Vero cells, human HeLa cells and murine N2A cells (PubMed:18042253). {ECO:0000269|PubMed:15226357, ECO:0000269|PubMed:17024087, ECO:0000269|PubMed:18005237, ECO:0000269|PubMed:18042253}.
Interaction partners:
Sequence:
MLKILWTYILFLLFISASARAEKPWYFDAIGLTETTMSLTDKNTPVVVSVVDSGVAFIGGLSDSEFAKFSFTQDGSPFPVKKSEALYIHGTAMASLIASRYGIYGVYPHALISSRRVIPDGVQDSWIRAIESIMSNVFLAPGEEKIINISGGQKGVASASVWTELLSRMGRNNDRLIVAAVGNDGADIRKLSAQQRIWPAAYHPVSSVNKKQDPVIRVAALAQYRKGETPVLHGGGITGSRFGNNWVDIAAPGQNITFLRPDAKTGTGSGTSEATAIVSGVLAAMTSCNPRATATELKRTLLESADKYPSLVDKVTEGRVLNAEKAISMFCKKNYIPVRQGRMSEEL
Protein: Leucine-rich repeat and fibronectin type-III domain-containing protein 3 (Synaptic adhesion-like molecule 4) (Q8BLY3)
Organism: Mus musculus (Mouse)
Function: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16828986}; Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase F
- Flotillin-1
- Receptor-type tyrosine-protein phosphatase S
- Flotillin-2
Sequence:
MAVLPLLLCLLPLAPASSPPQPAISSPCPRRCRCQTQSMPLSVLCPGAGLLFVPPSLDRRAAELRLADNFIAAVRRRDLANMTGLLHLSLSRNTIRHVAAGAFADLRALRALHLDGNRLTSLGEGQLRGLVNLRHLILSNNQLAALAAGALDDCAETLEDLDLSYNNLEQLPWEALGRLGNVNTLGLDHNLLASVPAGAFSRLHKLARLDMTSNRLTTIPPDPLFSRLPLLARPRGSPASALVLAFGGNPLHCNCELVWLRRLAREDDLEACASPPALGGRYFWAVGEEEFVCEPPVVTHRSPPLAVPAGRPAALRCRAVGDPEPRVRWVSPQGRLLGNSSRARAFPNGTLELLVTEPEDGGTFTCIAANAAGEATAAVELTVGPPPPPQLANSTSCDPPRDGEPDALTPPSAASASAKVADTVAPTDRGVQVTEHGATAALVQWPDQRPVPGIRMYQIQYNSSADDILVYRMIPADSRSFLLTDLASGRTYDLCVLAVYEDSATGLTATRPVGCARFSTEPALRPCAAPHAPFLGGTMIIALGGVIVASVLVFIFVLLLRYKVHGGQPPGKAKATAPVSSVCSQTNGALGPVPSAPAPEPAAPRAHTVVQLDCEPWGPSHEPAGP
Protein: Forkhead box protein F1 (Forkhead-related protein FKHL5) (Forkhead-related transcription factor 1) (FREAC-1) (Hepatocyte nuclear factor 3 forkhead homolog 8) (HFH-8) (Q61080)
Organism: Mus musculus (Mouse)
Function: Probable transcription activator for a number of lung-specific genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Bone morphogenetic protein 4
- Sonic hedgehog protein
- Transcription factor GATA-4
- Indian hedgehog protein
- Homeobox protein BarH-like 1
Sequence:
MSAPDKQQPPHGGGTGGGGGAGGQAMDPAAAGPTKAKKTNAGVRRPEKPPYSYIALIVMAIQSSPSKRLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPVYSMVNGLGFNHLPDTYGFQGSGGLSCAPNSLALEGGLGMMNGHLAGNVDGMALPSHSVPHLPSNGGHSYMGGCGGSAAGEYPHHDSSVPASPLLPAGAGGVMEPHAVYSSSAAAWPPAASAALNSGASYIKQQPLSPCNPAANPLSGSISTHSLEQPYLHQNSHNGPAELQGIPRYHSQSPSMCDRKEFVFSFNAMASSSMHTTGGGSYYHQQVTYQDIKPCVM
Protein: Tropomodulin, isoform N (A0A0B4K6N4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- FI04474p
- Adenylyl cyclase-associated protein
- Myosin light chain alkali
- Profilin
- Supervillin, isoform AE
- Tropomyosin-1, isoforms 9A/A/B
- Tropomyosin-2
- Cofilin/actin-depolymerizing factor homolog
Sequence:
MSDIEDVFGGSAEETKPEPDAQSKTSVVTEHTEEVIPGETEKMVTETIDEDGDVVEETTEVTRKTVKRTMKITETSATTKTTTLTTPAKLYGKDLSEYDDVDVESLLAQLSPEEITILAKEVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQPEFEPFVQGKVRGKKWVPPPRDARDIEAEEQIAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQDQYHASLLNKGQPVGLGWDGITKSTQQKLFPMDPPNNTDVEESIKRVKDDDSKLIDLNLNNIKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFRASNQRSAVLGNKIEMEITDLVEKNSSLLRLGLHLEFNDARHRVAAHLQRNIDRIFRVQKLKPNLPKLILPGNMEIERDLVAYNRSATPSPSPSPQPPVDYEVEEDPDNMVIRGGGDAFDPDVDPDNMVVPGSRSVTPNYDDEGVYQAHTWTSASHGPSDQELHRWRLAVGFIRLGLGSLHILHRKKSIAYQ
Protein: PWWP domain-containing protein2 (O94312)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- PWWP domain-containing protein 3
- PWWP domain-containing protein 1
- Histone acetyltransferase mst2
- Mst2 complex subunit nto1
- Chromatin modification-related protein eaf6
- Histone-lysine N-methyltransferase set9
- Pdp3-interacting factor 1
- Pdp3-interacting factor 2
Sequence:
MTEIKDSSVKDENPGKQEESSIAVESREMSTATNNSKNIETTSSNGAEDIKIQRDVGDDKDLDDKEANDKSSKGLEEESDSKDRKTIETDQPSNNIGDIKSQKSEKSNGNARKETKQSERVNYKPGMRVLTKMSGFPWWPSMVVTESKMTSVARKSKPKRAGTFYPVIFFPNKEYLWTGSDSLTPLTSEAISQFLEKPKPKTASLIKAYKMAQSTPDLDSLSVPSSESEVSEEESDQEMSEPSPIEEDYNDTKARRITRKGTKKKTVTFDPSLESVPQKRLNASSNVSSNPAKKTRVSPRRSTAASKKKSPSSKRASSDEIEKDKEEEEGSVANEEDVAKRTFHSREQSLLFLRHKLQSSLLSPKQDLSQVDYKLVHNYLDKLANFQGIDVPLIQKTKIAVVVRKIFSLAGLPKENEDEVKSICGDILENRWKSLLQEISSQKQLSTDASQTQDASIANENETEIASLDEGSESKPTPSPPAEQLTDQKQNEDNEDKVKADSNGPTQNENETADASKDMISEEKSSKDADNSLEVAGKDFAEDGTEQTPNLAEPEDGVAAVDLSTGQK
Protein: L-arabinose isomerase (EC 5.3.1.4) (P08202)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of L-arabinose to L-ribulose.
Interaction partners:
- Ribulokinase
- L-ribulose-5-phosphate 4-epimerase AraD
- L-ribulose-5-phosphate 4-epimerase SgbE
- L-ribulose-5-phosphate 4-epimerase UlaF
- Arabinose-proton symporter
- Xylose isomerase
- Putative beta-xylosidase
- Xylulose kinase
- Arabinose operon regulatory protein
- L-galactonate-5-dehydrogenase
Sequence:
MTIFDNYEVWFVIGSQHLYGPETLRQVTQHAEHVVNALNTEAKLPCKLVLKPLGTTPDEITAICRDANYDDRCAGLVVWLHTFSPAKMWINGLTMLNKPLLQFHTQFNAALPWDSIDMDFMNLNQTAHGGREFGFIGARMRQQHAVVTGHWQDKQAHERIGSWMRQAVSKQDTRHLKVCRFGDNMREVAVTDGDKVAAQIKFGFSVNTWAVGDLVQVVNSISDGDVNALVDEYESCYTMTPATQIHGKKRQNVLEAARIELGMKRFLEQGGFHAFTTTFEDLHGLKQLPGLAVQRLMQQGYGFAGEGDWKTAALLRIMKVMSTGLQGGTSFMEDYTYHFEKGNDLVLGSHMLEVCPSIAAEEKPILDVQHLGIGGKDDPARLIFNTQTGPAIVASLIDLGDRYRLLVNCIDTVKTPHSLPKLPVANALWKAQPDLPTASEAWILAGGAHHTVFSHALNLNDMRQFAEMHDIEITVIDNDTRLPAFKDALRWNEVYYGFRR
Protein: E3 ubiquitin-protein ligase MARCH8 isoform 1 (EC 2.3.2.27) (Membrane-associated ring finger (C3HC4) 8) (B8A530)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004439}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}.
Interaction partners:
- F-box/LRR-repeat protein 20
Sequence:
MNMPLHQISVIPRDVTSSRVCSSGKAKEKDKQNEKPLGHSASRSSNISKAGSPTSVNAPCSFPRSSVTPSNQDICRICHCEGDDESPLITPCHCTGSLRFVHQACLQQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTASERRKIMCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGILEWPFWTKLVVVAIGFTGGLVFMYVQCKVYIQLWRRLKAYNRVIYVQNRPETCKIKVFDKPSLLEPNLENKEALVPAQSDTNSSQYTETEDYSMEILHV
Protein: Probable phosphatidylinositol phosphate kinase DDB_G0267588 (EC 2.7.1.-) (Q55GN6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May be involved in signaling events that underlie chemotaxis via the chemoattractant-mediated pkgB phosphorylation.
Interaction partners:
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- SAC domain-containing protein
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 3-kinase 2
- phosphoinositide 5-phosphatase
- Phosphatidylinositol 3-kinase 1
- PIPK domain-containing protein
Sequence:
MNTIDTVVPEMNPALSESIVFAPIRTGEEGEKIPIIPINAALSESIVFSPIPPPPSTTDNTTNTTTTTIETTATDNTNDTEEKQENIENNNNNNNSSISSPNSIDGANKKDSIELEEDKEHSIKRKDGSLGDVVDNEKIIPNSLDSDAPEETSNLNKKSEINIKQVLKNPSFDATNDNHNPQEVDNTDNPDKPTTPRQTTTTTTTTTTTTSTNSTSNKLPNNGDNTVSFDEKFDPNVSHSNLNDDYKASGSSDSPNRVRLNTSQRLKMYKQKSEKRLSHRPKSIKLEHKKNVLGEIIYKGHPSWALMLNIQTGIRNAVGKSMGTEGGVNAKTPQQYHTLRKPSEFKRKEDFYVSPKTQRFESAGTAMTNAHSTGAFKFKDYCPNAFRYLRYLFGIDTADFMVSLCNTLKNGENALRELPTPGKSGSLFFFSHDMKFIIKTIPKDEAKLLRDILPSYLEHIQSNPNSLLPRFFGLYRVKPHSGRQVRFVIMGNLFPTKKKIHERYDLKGSVVGREASVDEKKSDSVTFKDIDFRNRKQKIFLGPGKKQSFIDQIKRDCKLLQSLNIMDYSLLIGIHYPHRENEPPSPSLLRSTLEDSSDFESPSMEQSSAGQQQQQRGSGNYDNSGAGRDSTTGGAAPKENDEIYISAFQQDEGGIKSQGGDTEEHYFLGIIDILMLYSLRKKVEHTYKTLKFGAKQEISSVSPDEYSERFQEFLSTIIE