wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxin 11 (RE39562p) (Q7JZE1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
- Peroxin-19
- Peroxisomal membrane protein PEX13
- Peroxin 11c, isoform B
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- FI14123p
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX16
- RING-type E3 ubiquitin transferase
- Peroxisomal targeting signal 1 receptor
Sequence:
MDQLVQLNNQAGGRDKIARLIQYASRAMWDSLESANSNPALVDNFKTVEYILSTFRKLLRFGKCVDVFYGALKTIHHPDLNIRVTLTLSKLSQSLFLFADHFLWLARTGLTAVNAKRWSNIANKYWLFSIIMNLCRDFYEILRVLDLHRSGSKSGISRCRIPASINSPEDFKRLALQSYVLMQGHKDIVVDTVKNACDFFIPLTALGYTSLTPRTIGLLGAISSLAGLWALLEPRAKLTPA
Protein: Beta-klotho (BKL) (BetaKlotho) (Klotho beta-like protein) (Q86Z14)
Organism: Homo sapiens (Human)
Function: Contributes to the transcriptional repression of cholesterol 7-alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis. Probably inactive as a glycosidase. Increases the ability of FGFR1 and FGFR4 to bind FGF21 (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor receptor 4
- Fibroblast growth factor 21
- Fibroblast growth factor 19
- Fibroblast growth factor receptor 1
- Fibroblast growth factor 23
- Fibroblast growth factor 4
- Fibroblast growth factor receptor 2
- Fibroblast growth factor 18
- Fibroblast growth factor 20
- Fibroblast growth factor receptor 3
Sequence:
MKPGCAAGSPGNEWIFFSTDEITTRYRNTMSNGGLQRSVILSALILLRAVTGFSGDGRAIWSKNPNFTPVNESQLFLYDTFPKNFFWGIGTGALQVEGSWKKDGKGPSIWDHFIHTHLKNVSSTNGSSDSYIFLEKDLSALDFIGVSFYQFSISWPRLFPDGIVTVANAKGLQYYSTLLDALVLRNIEPIVTLYHWDLPLALQEKYGGWKNDTIIDIFNDYATYCFQMFGDRVKYWITIHNPYLVAWHGYGTGMHAPGEKGNLAAVYTVGHNLIKAHSKVWHNYNTHFRPHQKGWLSITLGSHWIEPNRSENTMDIFKCQQSMVSVLGWFANPIHGDGDYPEGMRKKLFSVLPIFSEAEKHEMRGTADFFAFSFGPNNFKPLNTMAKMGQNVSLNLREALNWIKLEYNNPRILIAENGWFTDSRVKTEDTTAIYMMKNFLSQVLQAIRLDEIRVFGYTAWSLLDGFEWQDAYTIRRGLFYVDFNSKQKERKPKSSAHYYKQIIRENGFSLKESTPDVQGQFPCDFSWGVTESVLKPESVASSPQFSDPHLYVWNATGNRLLHRVEGVRLKTRPAQCTDFVNIKKQLEMLARMKVTHYRFALDWASVLPTGNLSAVNRQALRYYRCVVSEGLKLGISAMVTLYYPTHAHLGLPEPLLHADGWLNPSTAEAFQAYAGLCFQELGDLVKLWITINEPNRLSDIYNRSGNDTYGAAHNLLVAHALAWRLYDRQFRPSQRGAVSLSLHADWAEPANPYADSHWRAAERFLQFEIAWFAEPLFKTGDYPAAMREYIASKHRRGLSSSALPRLTEAERRLLKGTVDFCALNHFTTRFVMHEQLAGSRYDSDRDIQFLQDITRLSSPTRLAVIPWGVRKLLRWVRRNYGDMDIYITASGIDDQALEDDRLRKYYLGKYLQEVLKAYLIDKVRIKGYYAFKLAEEKSKPRFGFFTSDFKAKSSIQFYNKVISSRGFPFENSSSRCSQTQENTECTVCLFLVQKKPLIFLGCCFFSTLVLLLSIAIFQRQKRRKFWKAKNLQHIPLKKGKRVVS
Protein: GDP-mannose 4,6-dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (P71790)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- GDP-L-fucose synthase
- Possible GDP-mannose 4,6-dehydratase Gca
- Conserved protein
- Mannose-1-phosphate guanylyltransferase
- Uncharacterized protein Rv1509
- Putative fatty-acid--CoA ligase fadD25
Sequence:
MKRALITGITGQDGSYLAELLLAKGYEVHGLIRRASTFNTSRIDHLYVDPHQPGARLFLHYGDLIDGTRLVTLLSTIEPDEVYNLAAQSHVRVSFDEPVHTGDTTGMGSMRLLEAVRLSRVHCRFYQASSSEMFGASPPPQNELTPFYPRSPYGAAKVYSYWATRNYREAYGLFAVNGILFNHESPRRGETFVTRKITRAVARIKAGIQSEVYMGNLDAVRDWGYAPEYVEGMWRMLQTDEPDDFVLATGRGFTVREFARAAFEHAGLDWQQYVKFDQRYLRPTEVDSLIGDATKAAELLGWRASVHTDELARIMVDADMAALECEGKPWIDKPMIAGRT
Protein: Kielin/chordin-like protein (Cysteine-rich BMP regulator 2) (Cysteine-rich motor neuron 2 protein) (CRIM-2) (Kielin/chordin-like protein 1) (KCP-1) (Q3U492)
Organism: Mus musculus (Mouse)
Function: Enhances bone morphogenetic protein (BMP) signaling in a paracrine manner. In contrast, it inhibits both the activin-A and TGFB1-mediated signaling pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:15793581}.
Interaction partners:
Sequence:
MAGARAALLPLLLHLGSLALAARGGEVSREQPRLADAISQQQAPSHSLVPGETHQQQWCPLEERLERLEAEVTDLRKQNRELQARVVQLESCECWGPGHTCPEGARWEPDACTACVCRDGTAHCGPQPNLPHCRGCSHNGQSYGHGETFSPDACTTCRCLAGTVQCQGPSCSELNCLESFIPPGECCPICRPGCEYEGQLHQEGSSFLSSSNPCLQCSCLRSLVRCVPVKCQPSPCLNPVPRLGHCCPVCQASGCTEGNSHRDHGQEWTTPGDPCRICQCLEGHIQCRQRECASLCPYPARPLPGTCCPVCDGCFLNGREHSSGEPVGSQDPCSSCRCTNGSVQCEPLPCPPAPCRYPGRIPGQCCPVCDGCKYQGHEYRSQETFTLQENGRCLRCVCQAGEVSCEEQDCPVTPCVRSASGPQLCSACVLNGEEFAEGIQWEPDDQPCTSCSCQDGVPVCRAVLCSPVPCQHPTQPPGACCPSCDSCTYHSLVYANGQNFTDVDSPCQTCYCEDGTVRCSLINCPFTTCAKPQNGPGQCCPKCPDCILEAQVFVDGERFPHPRDPCQECWCQEGQAHCQLRACPSAPCVHPLPGTCCKNDCTGCAFGGKEYPNGADFPHPTDPCRLCRCLSGNVQCLARRCPPLSCPQPVLTPGDCCPQCPDAPADCPQSGNMVPVRHQEHFFQPGDPCSRCLCLDGSVSCQRLTCPPAPCAHPRRDACCPSCDGCLYQGKEFASGERFPSPNVACHVCLCWEGSVKCEPRTCAPAQCPFPTREDCCPACDSCDYLGVSYLSSQEFPDPREACNLCTCLGGFVTCTRRPCEPPACSHPLIVPEHCCPTCQGCLYHGITAALGETLPDPLDPTCSLCTCEEGSMRCQKKPCPPAPCAHPSPGPCFCPVCRSCLSQGREHQDGEEFEGPEGSCERCRCLAGQVSCTRLQCPSLPCLHQVTEPGTCCPRCTGCLARGEEHPEGSSWVPADSPCSSCMCHKGIITCAQVQCVSACIWPQEGPSDCCPQCSGCEHGGRKYEPGESFQPGADPCEVCICKQKREGPPSLHCSRRQCPSLVGCPPSQLLPPGPQHCCPTCAQALSNCTEDLVGSELVPPDPCYTCQCQDLTWLCTHRACPELSCPLWERHTTPGSCCPVCKDPTQSCMHQGRWVASGEQWAVDACTSCSCVAGTVHCQTQRCRKLACSRDEVPALSPGSCCLRCLPRPASCMAFGDPHYRTFDGRLLHFQGSCSYVLAKDCHGEDFSVHVTNDDRGRRGVAWTQEVAVLLGTVAVRLLQGRTVMVDQHTVTLPFLREPLLYIELRGHTVILHAQPGLQVLWDGQSQVEVRVPSSYRGQTCGLCGNFNGFAQDDLQGPDGRLLPTEASFGNSWKVPKGLGPGRPCSAGREVDPCRAAGYRARREANARCGILKTSPFSHCHAVVPPEPFFAACVYDLCACGPGSSSDTCLCDALEAYASHCRQAGVTPVWRGPTLCVVGCPVDRGFVFDECGPPCPRTCFNRHIPLGELAAHCVRPCVPGCQCPAGLVEHEGHCISPEVCPPVLLTGD
Protein: 40S ribosomal protein S14 (Q4FKG9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein translation factor SUI1 homolog, putative
- 60S ribosomal protein L19, putative
- 40S ribosomal protein S18, putative
- Polyubiquitin, putative
- 60S ribosomal protein L39, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S26
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S16, putative
Sequence:
MSKKQEVKYYGSSAGKDQLVYGVVHIYASFNDTFVHVTDMSGRETFCKVTGGMKVKADRDESSPYAAMMAAQDVVARCKECGINALHVKMRATGGVGTKSPGPGAQAALRALARAGMKIGRIEDVTPVPTDSTRRKGSRRGRRL
Protein: Olfactory receptor 5AN1 (Olfactory receptor OR11-244) (Q8NGI8)
Organism: Homo sapiens (Human)
Function: Odorant receptor involved in the detection of muscone, cyclopentadecanone, cyclopentadecanol, and omega-pentadecalactone. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Probable).
Subcellular location: Cell membrane {ECO:0000305|PubMed:24361078, ECO:0000305|PubMed:25901328}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MTGGGNITEITYFILLGFSDFPRIIKVLFTIFLVIYITSLAWNLSLIVLIRMDSHLHTPMYFFLSNLSFIDVCYISSTVPKMLSNLLQEQQTITFVGCIIQYFIFSTMGLSESCLMTAMAYDRYAAICNPLLYSSIMSPTLCVWMVLGAYMTGLTASLFQIGALLQLHFCGSNVIRHFFCDMPQLLILSCTDTFFVQVMTAILTMFFGIASALVIMISYGYIGISIMKITSAKGRSKAFNTCASHLTAVSLFYTSGIFVYLSSSSGGSSSFDRFASVFYTVVIPMLNPLIYSLRNKEIKDALKRLQKRKCC
Protein: UV radiation resistance-associated gene (E7EY87)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNSIAGRDLSVSAGSVSGNPGATSSRVLHVELTSQQRRLRHLRSIAARNIVNKNGSPLLDTYFTLHLCQDDQISRDFYKSEVIRDSLNPTWRSLDFAMLPDLLDTSVSCFVVRIWGGREEHYQLLIEWKVNLDGLRFTGQQIRSRNPNEIIFGLNDGYYAAEFDQKESSDRRKNSLLQVDQSSVRNSYSVFSLLRLRMAQRAIKQTQVTVQKIGKEIEEKLRTTASCTEKKKERECMQLRIGILRCELERQKKALTREMDVMQKERAQLIKKEEASSTKQQDLESERTTLTDLQKECTAKRELFLKSKAQLTFRCRQLISELSYIYPIDVNNQNDYVICGVKLPNSEDFQAKDDGSIAVALGYTAHLVLMISCFLQIPLRYPVIHKGSRSTIKDTITDKLTEKEREFPLYPRGERFQFEYGVYLLNKNIAQLRYQHGLSTPDLRQTLPNLKNFLEHGLLVRCDRHHASMSIPVPLKSHLSVSTASEVGFPALSSSPEQDVRRRAASDADKQKCRTPPPSYNTAMAQPDPMTTPELQSEPSVEVLEVGKAVETLEDGETVSEEHPEKPLDVPTDIVSTLPSDSIPQHPGAMNGSAVPTSGGVGLGVASGGEVCCSVEQAEEIMGTEATGLGLGLGGGARLDDYPCIPVEHAVAVECDEQVLGEFDAAGIEEVSRRIYALENMSSFRRPRKNSEK
Protein: ATP synthase subunit 9, mitochondrial (Q2F8W6)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion membrane {ECO:0000256|RuleBase:RU004221}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU004221}.
Interaction partners:
Sequence:
MLEGAKSIGAGAATIALAGAAVGIGNVLSSSIHSVARNPSLAKQLFGYAILGFALTEAIALFAPMMAFLISFVF
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (A0A0G2K2A5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- 26S proteasome regulatory subunit 10B
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 6B
- Proteasomal ubiquitin receptor ADRM1
- Nuclear factor-related to kappa B-binding protein.
- Proteasome
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 8
- Ubiquitin carboxyl-terminal hydrolase
Sequence:
VSGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAVSRVLILKRPICDCSCYNRLLFKFVLMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK
Protein: Phospholipid scramblase 3 (PL scramblase 3) (Ca(2+)-dependent phospholipid scramblase 3) (Q6QBQ4)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of the phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer membrane of the mitochondria. Plays an important role in mitochondrial respiratory function, morphology, and apoptotic response (By similarity). Mediates the translocation of cardiolipin from the mitochondrial inner membrane to outer membrane enhancing t-Bid induced cytochrome c release and apoptosis (By similarity). Enhances TNFSF10-induced apoptosis by regulating the distribution of cardiolipin in the mitochondrial membrane resulting in increased release of apoptogenic factors and consequent amplification of the activity of caspases (By similarity). Regulates cardiolipin de novo biosynthesis and its resynthesis (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:29171872}; Single-pass type II membrane protein {ECO:0000305|PubMed:29171872}. Nucleus {ECO:0000250|UniProtKB:Q9JIZ9}. Note=Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000250|UniProtKB:Q9JIZ9}.
Interaction partners:
- Calcium homeostasis endoplasmic reticulum protein
Sequence:
MAGYLPPKGYAPSPPPPYPVPAGYPEAAALHPGPGQAPVPTQGPAPAPGFSLFPSPGPVVPGPPGPFVPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGTGQQLGQAAEESNCCARLCCGARRPLRIRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTIGHVLQTWHPFIPKFSILDADRQPVLRVVGPCCTCGCGTDTNFEVKTKDESRSVGRISKQWGGLLREALTDADDFGLQFPVDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAITS
Protein: F10A5.16 (Leucine-rich receptor-like protein kinase family protein) (Putative receptor-like protein kinase) (Q9LR04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAATVIFFLHFAAIFFSRFHHTSAISSETQALTSFKLSLHDPLGALESWNQSSPSAPCDWHGVSCFSGRVRELRLPRLHLTGHLSPRLGELTQLRKLSLHTNDINGAVPSSLSRCVFLRALYLHYNSFSGDFPPEILNLRNLQVLNAAHNSLTGNLSDVTVSKSLRYVDLSSNAISGKIPANFSADSSLQLINLSFNHFSGEIPATLGQLQDLEYLWLDSNQLQGTIPSALANCSSLIHFSVTGNHLTGLIPVTLGTIRSLQVISLSENSFTGTVPVSLLCGYSGYNSSMRIIQLGVNNFTGIAKPSNAACVNPNLEILDIHENRINGDFPAWLTDLTSLVVLDISGNGFSGGVTAKVGNLMALQELRVANNSLVGEIPTSIRNCKSLRVVDFEGNKFSGQIPGFLSQLRSLTTISLGRNGFSGRIPSDLLSLYGLETLNLNENHLTGAIPSEITKLANLTILNLSFNRFSGEVPSNVGDLKSLSVLNISGCGLTGRIPVSISGLMKLQVLDISKQRISGQLPVELFGLPDLQVVALGNNLLGGVVPEGFSSLVSLKYLNLSSNLFSGHIPKNYGFLKSLQVLSLSHNRISGTIPPEIGNCSSLEVLELGSNSLKGHIPVYVSKLSLLKKLDLSHNSLTGSIPDQISKDSSLESLLLNSNSLSGRIPESLSRLTNLTALDLSSNRLNSTIPSSLSRLRFLNYFNLSRNSLEGEIPEALAARFTNPTVFVKNPGLCGKPLGIECPNVRRRRRRKLILLVTLAVAGALLLLLCCCGYVFSLWKWRNKLRLGLSRDKKGTPSRTSRASSGGTRGEDNNGGPKLVMFNNKITLAETLEATRQFDEENVLSRGRYGLVFKATFRDGMVLSVRRLMDGASITDATFRNQAEALGRVKHKNITVLRGYYCGPPDLRLLVYDYMPNGNLATLLQEASHQDGHVLNWPMRHLIALGIARGLSFLHSLSIIHGDLKPQNVLFDADFEAHLSEFGLDRLTALTPAEEPSTSSTPVGSLGYIAPEAGLTGETSKESDVYSFGIVLLEILTGKKAVMFTEDEDIVKWVKRQLQKGQIVELLEPGLLELDPESSEWEEFLLGIKVGLLCTGGDVVDRPSMADVVFMLEGCRVGPAISLSADPTSPTSPAATAVS
Protein: E3 ubiquitin-protein ligase RNF149 (EC 2.3.2.27) (Goliath-related E3 ubiquitin-protein ligase 4) (RING finger protein 149) (RING-type E3 ubiquitin transferase RNF149) (Q3U2C5)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAARRRPAAGVGARDALAVLALALCTPGVGGGALEWYSAMVSIEYVDPQSNLTVWSVSESGRFGESSLREERQGLVGVPRAPAPAEGCAPDTRFVAPGALGNAPWVALVARGGCTFKDKVLAAARRNASAVVVYNLESNGNATEPMSHAGTGNIVVIMISYPKGREIFDLVQKGIPVKMRIEIGTRHMQEFISGQSVVFVAIAFITMMIISLAWLIFYYIQRFLYTGSQFGSQNHRKETKKVIGQLPLHTVKHGEKGIDVDAENCAVCIENFKVKDVIRILPCKHIFHRICIDPWLLDHRTCPMCKLDVIKALGYWGDPEDTQELPTPEAAPGRVSVGNLSVTSQDEERSESNLPSSSSSESGPHRPCLKEDAGEDTALLGAGRSEPQHGGSIC
Protein: POTE ankyrin domain family member F (ANKRD26-like family C member 1B) (Chimeric POTE-actin protein) (A5A3E0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:17101985}. Note=Colocalizes with actin filaments.
Interaction partners:
- Actin-like protein 6A
- Glyceraldehyde-3-phosphate dehydrogenase
- Large ribosomal subunit protein uL10
- TATA-box-binding protein
- Dynein light chain 1, cytoplasmic
- Beta-2-microglobulin
- Tubulin beta chain
- Myosin-1
- Tubulin beta-2A chain
- Ezrin
Sequence:
MVVEVDSMPAASSVKKPFGLRSKMGKWCCRCFPCCRESGKSNVGTSGDHDDSAMKTLRSKMGKWCRHCFPCCRGSGKSNVGASGDHDDSAMKTLRNKMGKWCCHCFPCCRGSSKSKVGAWGDYDDSAFMEPRYHVRGEDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLTNGVTAGNGDNGLIPQRKSRTPENQQFPDNESEEYHRICELLSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSENGQPEKRSQEPEINKDGDRELENFMAIEEMKKHRSTHVGFPENLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCEEQNTGILHDEILIHEEKQIEVVEKMNSELSLSCKKEKDILHENSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKRNDNLLKALQLNELTMDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL
Protein: Cytoplasmic dynein 1 intermediate chain (DH IC) (Dynein intermediate chain, cytosolic) (Protein short wing) (Q24246)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the help dynein bind to dynactin 150 kDa component (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9774695}.; SUBCELLULAR LOCATION: [Isoform 2c]: Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around lysosomes.; SUBCELLULAR LOCATION: [Isoform 2a]: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around the nucleus.; SUBCELLULAR LOCATION: [Isoform 2b]: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around the nucleus.
Interaction partners:
- Dynein light chain 1, cytoplasmic
- Dynein light chain Tctex-type
- Dynein light chain roadblock
- Sperm-specific dynein intermediate chain 2, isoform A
- FI21737p1
- GH16657p
- Sperm-specific dynein intermediate chain 1, isoform A
- Dynein light chain 2, cytoplasmic
- Dynein light intermediate chain
- Dynein heavy chain, cytoplasmic
Sequence:
MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMTSDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVNELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMDWSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQKRTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINSLVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDYVMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQPSRDEWSRFNTHLSEIKMNQSDEV
Protein: Uncharacterized transporter YdhK (P76186)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YdhJ
- Uncharacterized protein YdhI
- Uncharacterized protein YfeS
- Uncharacterized protein YfeK
Sequence:
MNASSWSLRNLPWFRATLAQWRYALRNTIAMCLALTVAYYLNLDEPYWAMTSAAVVSFPTVGGVISKSLGRIAGSLLGAIAALLLAGHTLNEPWFFLLSMSAWLGFCTWACAHFTNNVAYAFQLAGYTAAIIAFPMVNITEASQLWDIAQARVCEVIVGILCGGMMMMILPSSSDATALLTALKNMHARLLEHASLLWQPETTDAIRAAHEGVIGQILTMNLLRIQAFWSHYRFRQQNARLNALLHQQLRMTSVISSLRRMLLNWPSPPGATREILEQLLTALASSQTDVYTVARIIAPLRPTNVADYRHVAFWQRLRYFCRLYLQSSQELHRLQSGVDDHTRLPRTSGLARHTDNAEAMWSGLRTFCTLMMIGAWSIASQWDAGANALTLAAISCVLYSAVAAPFKSLSLLMRTLVLLSLFSFVVKFGLMVQISDLWQFLLFLFPLLATMQLLKLQMPKFAALWGQLIVFMGSFIAVTNPPVYDFADFLNDNLAKIVGVALAWLAFAILRPGSDARKSRRHIRALRRDFVDQLSRHPTLSESEFESLTYHHVSQLSNSQDALARRWLLRWGVVLLNCSHVVWQLRDWESRSDPLSRVRDNCISLLRGVMSERGVQQKSLAATLEELQRICDSLARHHQPAARELAAIVWRLYCSLSQLEQAPPQGTLAS
Protein: Myosin light chain 2 (Q9I9H9)
Organism: Oncorhynchus kisutch (Coho salmon) (Salmo kisutch)
Interaction partners:
Sequence:
MAPKKAKRRGAAAEGGSSNVFSMFEQSQIQEYNSGFPITDQNRDGIISKDDLRDVLASMGQLNVKNEELEAMVKEASGPINFTVFLTMFGEKLKGADPEDVIVSAFKVLDPDATGFIKKDFLQELLTTQCDRFSAEEMKNLWAAFPPDVAGNVNYKQICYVITHGEEKEE
Protein: Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial (EC 1.2.4.1) (PDHE1-A type II) (Q06437)
Organism: Rattus norvegicus (Rat)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Ac1164
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- [Pyruvate dehydrogenase
- [Pyruvate dehydrogenase
- Pyruvate kinase PKM
- L-lactate dehydrogenase C chain
- Pyruvate carboxylase, mitochondrial
Sequence:
MRKMLATVLSQVFSGMVQKPALRGLLSSLKFSNDATCDIKKCDLYLLEQGPPTSTVLTREEALKYYRNMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACNVGLEAGINPTDHIITSYRAHGLCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGVALACKYLKNGQICLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNRYGMGTAIERSAASTDYHKKGFVIPGLRVNGMDILSVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGISYRTREEVQNVRSKSDPIMLLRERMISNNLSSVEELKEIDADVKKEVEEAAQFATTDPEPPLEDLANYLYHQNPPFEVRGAHKWLKFKSVS
Protein: Protein Wnt-9a (Protein Wnt-14) (O14904)
Organism: Homo sapiens (Human)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal timing of IHH expression during embryonic bone development, normal chondrocyte maturation and for normal bone mineralization during embryonic bone development. Plays a redundant role in maintaining joint integrity.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
Interaction partners:
- Protein-serine O-palmitoleoyltransferase porcupine
- Wnt inhibitory factor 1
- Palmitoleoyl-protein carboxylesterase NOTUM
- Glypican-3
- Cerberus
- Low-density lipoprotein receptor-related protein 5
- Frizzled-1
- Frizzled-4
- Frizzled-9
- Frizzled-8
Sequence:
MLDGSPLARWLAAAFGLTLLLAALRPSAAYFGLTGSEPLTILPLTLEPEAAAQAHYKACDRLKLERKQRRMCRRDPGVAETLVEAVSMSALECQFQFRFERWNCTLEGRYRASLLKRGFKETAFLYAISSAGLTHALAKACSAGRMERCTCDEAPDLENREAWQWGGCGDNLKYSSKFVKEFLGRRSSKDLRARVDFHNNLVGVKVIKAGVETTCKCHGVSGSCTVRTCWRQLAPFHEVGKHLKHKYETALKVGSTTNEAAGEAGAISPPRGRASGAGGSDPLPRTPELVHLDDSPSFCLAGRFSPGTAGRRCHREKNCESICCGRGHNTQSRVVTRPCQCQVRWCCYVECRQCTQREEVYTCKG
Protein: Lysine-specific demethylase 3B (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) (Nuclear protein 5qNCA) ([histone H3]-dimethyl-L-lysine(9) demethylase 3B) (Q7LBC6)
Organism: Homo sapiens (Human)
Function: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- YTH domain-containing protein 1
- Lysine-specific demethylase 3A demethylase 3A)
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
- Peroxisome proliferator-activated receptor gamma
- AT-rich interactive domain-containing protein 1A
- SWI/SNF complex subunit SMARCC1
- Histone lysine demethylase PHF8
- Lysine-specific demethylase 7A
Sequence:
MADAAASPVGKRLLLLFADTAASASASAPAAAAASGDPGPALRTRAWRAGTVRAMSGAVPQDLAIFVEFDGCNWKQHSWVKVHAEEVIVLLLEGSLVWAPREDPVLLQGIRVSIAQWPALTFTPLVDKLGLGSVVPVEYLLDRELRFLSDANGLHLFQMGTDSQNQILLEHAALRETVNALISDQKLQEIFSRGPYSVQGHRVKIYQPEGEEGWLYGVVSHQDSITRLMEVSVTESGEIKSVDPRLIHVMLMDNSAPQSEGGTLKAVKSSKGKKKRESIEGKDGRRRKSASDSGCDPASKKLKGDRGEVDSNGSDGGEASRGPWKGGNASGEPGLDQRAKQPPSTFVPQINRNIRFATYTKENGRTLVVQDEPVGGDTPASFTPYSTATGQTPLAPEVGGAENKEAGKTLEQVGQGIVASAAVVTTASSTPNTVRISDTGLAAGTVPEKQKGSRSQASGENSRNSILASSGFGAPLPSSSQPLTFGSGRSQSNGVLATENKPLGFSFGCSSAQEAQKDTDLSKNLFFQCMSQTLPTSNYFTTVSESLADDSSSRDSFKQSLESLSSGLCKGRSVLGTDTKPGSKAGSSVDRKVPAESMPTLTPAFPRSLLNARTPENHENLFLQPPKLSREEPSNPFLAFVEKVEHSPFSSFASQASGSSSSATTVTSKVAPSWPESHSSADSASLAKKKPLFITTDSSKLVSGVLGSALTSGGPSLSAMGNGRSSSPTSSLTQPIEMPTLSSSPTEERPTVGPGQQDNPLLKTFSNVFGRHSGGFLSSPADFSQENKAPFEAVKRFSLDERSLACRQDSDSSTNSDLSDLSDSEEQLQAKTGLKGIPEHLMGKLGPNGERSAELLLGKSKGKQAPKGRPRTAPLKVGQSVLKDVSKVKKLKQSGEPFLQDGSCINVAPHLHKCRECRLERYRKFKEQEQDDSTVACRFFHFRRLIFTRKGVLRVEGFLSPQQSDPDAMNLWIPSSSLAEGIDLETSKYILANVGDQFCQLVMSEKEAMMMVEPHQKVAWKRAVRGVREMCDVCETTLFNIHWVCRKCGFGVCLDCYRLRKSRPRSETEEMGDEEVFSWLKCAKGQSHEPENLMPTQIIPGTALYNIGDMVHAARGKWGIKANCPCISRQNKSVLRPAVTNGMSQLPSINPSASSGNETTFSGGGGPAPVTTPEPDHVPKADSTDIRSEEPLKTDSSASNSNSELKAIRPPCPDTAPPSSALHWLADLATQKAKEETKEAGSLRSVLNKESHSPFGLDSFNSTAKVSPLTPKLFNSLLLGPTASNNKTEGSSLRDLLHSGPGKLPQTPLDTGIPFPPVFSTSSAGVKSKASLPNFLDHIIASVVENKKTSDASKRACNLTDTQKEVKEMVMGLNVLDPHTSHSWLCDGRLLCLHDPSNKNNWKIFRECWKQGQPVLVSGVHKKLKSELWKPEAFSQEFGDQDVDLVNCRNCAIISDVKVRDFWDGFEIICKRLRSEDGQPMVLKLKDWPPGEDFRDMMPTRFEDLMENLPLPEYTKRDGRLNLASRLPSYFVRPDLGPKMYNAYGLITAEDRRVGTTNLHLDVSDAVNVMVYVGIPIGEGAHDEEVLKTIDEGDADEVTKQRIHDGKEKPGALWHIYAAKDAEKIRELLRKVGEEQGQENPPDHDPIHDQSWYLDQTLRKRLYEEYGVQGWAIVQFLGDAVFIPAGAPHQVHNLYSCIKVAEDFVSPEHVKHCFRLTQEFRHLSNTHTNHEDKLQVKNIIYHAVKDAVGTLKAHESKLARS