wanglab/gogpt-training-data huggingface dataset:
Protein: TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TGF-beta-activated kinase 1-binding protein 2) (Q5RFW2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (By similarity). Involved in heart development.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9NYJ8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NYJ8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NYJ8}. Note=Following IL1 stimulation, translocation occurs from the membrane to cytosol. {ECO:0000250|UniProtKB:Q9NYJ8}.
Interaction partners:
- TNF receptor-associated factor 6
- Mitogen-activated protein kinase kinase kinase 7.
- Receptor
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa B kinase regulatory subunit gamma.
- Interleukin-1 receptor-associated kinase 1
- Interleukin-1 receptor-associated kinase 4.
- TGF-beta-activated kinase 1/MAP3K7-binding protein 1.
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Mitogen-activated protein kinase kinase kinase 7 interacting protein 3 like-binding protein 3)
Sequence:
MAQGNQQIDNQVLHHLRQKFPEVPEDVVCECVLQNKSDLAACCEYLTKVSPRFLYSEGSQSLTDLRNHMTQLNLGVSQNTHGAVQRDAVGMNGSRTLAPSVSDGPLNVPSALSEFYQPETPSVPTHTPASLSMESTRKPQPPQHLGLYQVGGKGHAPPQAPRFNPITVTLAPNTGRNTPTSLHIHGGPQSGLNSPNSIYIRPYVTQPGSTRQVQCRAQYSPTSQPAQQIYQITHPAAPQSSWSQHQTSHVYMPISSPTNTQAPSIPSAVASQAVSSSPLPSSGSSFSQYNIQNISTGPRKNQIEIKLESPQRGSGSSSLLRSSSAPRSACSSTSSSCPSSCTSLASSSGSSTPISIGGAGLSRSQPTVYISPSPPTAATAPSEDCALVPNTPRSQPKIYFSANTSADDGGGRNPPTVYISANPALQGPAGLRALGSQMSMGPAYIHHHPPKSRPSVGAGGTATSPRVVVTQPNTKYTFKITVSPNKPPSVSPGVVSPTFEPNNMLSLPADHHYAEPEISQPDPMRDKAVEPRRLSMGADDAAYTQALLVHQRARMERLWHELELKKRKLEKLKEEVNEMESDLTRRRLQRSNAFCQIPSIEEMQQLRCKNRLLQIDIDCLTKEIDLLQTRGPDFNPIAIHNFYDNLGFLGPVPPKPLKGPTKAEVSRTDAGVRVLSEPEEDDGVQWSCTACTFLNHPALNRCEECEFPRNF
Protein: Thioredoxin domain-containing protein 9 (ATP-binding protein associated with cell differentiation) (Protein 1-4) (O14530)
Organism: Homo sapiens (Human)
Function: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9CQ79}. Nucleus {ECO:0000250|UniProtKB:Q9CQ79}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CQ79}. Midbody {ECO:0000250|UniProtKB:Q9CQ79}. Note=Co-localizes with beta-tubulin in the centrosome. {ECO:0000250|UniProtKB:Q9CQ79}.
Interaction partners:
- Insulin receptor
- Keratin, type I cytoskeletal 17
- 14-3-3 protein gamma
- Huntingtin
- Tubulin alpha chain-like 3
- 14-3-3 protein epsilon
- 14-3-3 protein sigma
- 14-3-3 protein eta
- 14-3-3 protein beta/alpha
- Tubulin alpha-1B chain
Sequence:
MEADASVDMFSKVLEHQLLQTTKLVEEHLDSEIQKLDQMDEDELERLKEKRLQALRKAQQQKQEWLSKGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQDYVVGFTDLGNTDDFTTETLEWRLGSSDILNYSGNLMEPPFQNQKKFGTNFTKLEKKTIRGKKYDSDSDDD
Protein: Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase (Type 1 PtdIns-4,5-P2 4-Ptase) (EC 3.1.3.78) (PtdIns-4,5-P2 4-Ptase I) (Transmembrane protein 55B) (Q3TWL2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity). Regulates lysosomal positioning by recruiting JIP4 to lysosomal membranes, thus inducing retrograde transport of lysosomes along microtubules (By similarity). Contributes to assembly of the V-ATPase complex in lipid rafts of the lysosomal membrane and to subsequent amino acid-dependent activation of mTORC1. May play a role in the regulation of cellular cholesterol metabolism (By similarity).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:29644770}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:29378918}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- C-Jun-amino-terminal kinase-interacting protein 4
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Myotubularin
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR4
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Synaptojanin-1
- Inositol polyphosphate 5-phosphatase OCRL
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
Sequence:
MAADGERSPLLSEAGDGGAGGNGLAGPGGSATGPGGGLTPSAPPYGAGKHAPPQAFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQSPINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNCLLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGVRVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKRCICCFLLGLLLAVTATGLAFGTWKHAQQYGGIYAAWAFVILLAVLCLGRALYWACMKVSHPVQNFS
Protein: LD23683p (Q8SZS6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIRSVLGTFQTLLKQLQPVASEEMPDISMKMYHIVCVPSCYSYFQTLLEQAGLYGLVQLHHFNWDFIYFDQGVLSLELPNLYECLYLQKNTSPLPAVAQSLRLLQMICGQPSLILSFGHHSSQLMQMAKTLGKLPAPTNPPDYGGWLVIDRDKDYPASLLTPAIYAGLLLEVFEHSSGEILVDNSKNKIRSQRVELLQGKKSKIGVNSASKPCSIRLNSTSDEIYGDNRYKRFAQVSSLIHAQVKALGLELQKLNDMQLDEMHDYVARKLPKLTELKSKVLRHLNASEIVIQMMGNFRKLQTLEEDILNNDSRKRLLSEIDELLTTDGQRFNTLRLLCLLHHCVGVAPEELQIFARNYCNLFGHQELGVFQQLSQAGLLPPLVVEKKAPTKLLSNLPLPKFQQTEFQANANRLKLLTSSGDGQDGGSSSKSQSSGLQTCPSFVFNGTYIPLVAQLCSILLKINSAEELSSKLGMIEGLHLHLDSGKITPKAYASQVKLNGVADQDMFPLRLRNLFVFIVGGASYAEIAACDFVAKLTGAQITVASDSLMAGSDLIATAFNR
Protein: Hsp70-Hsp90 organizing protein 1 (AtHop1) (Stress-induced-phosphoprotein 1) (STI1) (Q9LNB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Meiosis-specific protein ASY1
- Meiosis-specific protein ASY3
- Heat shock protein 90-1
- Meiotic recombination protein DMC1 homolog
- Mitotic spindle checkpoint protein MAD2
- Heat shock protein 90-5, chloroplastic
- Co-chaperone protein p23-1
- Peptidyl-prolyl cis-trans isomerase CYP40
- Cytochrome P450 83B1
Sequence:
MAEEAKAKGNAAFSSGDFTTAINHFTEAIALAPTNHVLFSNRSAAHASLHQYAEALSDAKETIKLKPYWPKGYSRLGAAHLGLNQFELAVTAYKKGLDVDPTNEALKSGLADAEASVARSRAAPNPFGDAFQGPEMWTKLTSDPSTRGFLQQPDFVNMMQEIQKNPSSLNLYLKDQRVMQSLGVLLNVKFRPPPPQGDEAEVPESDMGQSSSNEPEVEKKREPEPEPEPEVTEEKEKKERKEKAKKEKELGNAAYKKKDFETAIQHYSTAIEIDDEDISYLTNRAAVYLEMGKYNECIEDCNKAVERGRELRSDYKMVARALTRKGTALTKMAKCSKDYEPAIEAFQKALTEHRNPDTLKRLNDAERAKKEWEQKQYFDPKLGDEEREKGNDFFKEQKYPEAIKHYTEAIKRNPNDHKAYSNRAASYTKLGAMPEGLKDAEKCIELDPTFSKGYSRKAAVQFFLKEYDNAMETYQAGLEHDPSNQELLDGVKRCVQQINKANRGDLTPEELKERQAKGMQDPEIQNILTDPVMRQVLSDLQENPSAAQKHMQNPMVMNKIQKLISAGIVQMK
Protein: Double C2-like domain-containing protein gamma (Doc2-gamma) (Q9ESN1)
Organism: Mus musculus (Mouse)
Function: May be involved in regulation of vesicular trafficking. In vitro, does not bind calcium and phospholipids.
Interaction partners:
- Rab effector Noc2
Sequence:
MACAGPASGRHGVSMQEHMAIDVSPGPIRPIRLISNYFPHFYPFLEPVLRAPDRQAMLAPAIPSAPQLQPNPEPEGDSDDSTALGTLEFTLLFDEDNSALHCTAHRAKGLKPPAAGSVDTYVKANLLPGASKASQLRTRTVRGTREPVWEETLTYHGFTCQDAGRKTLRLCVCEDSRLRRRRRGPPLGELRVPLRKLVPNRARSFDICLEKRKLTKRPKSLDTARGMSLYEEEEVEAEVFGEERGRILLSLCYSSERGGLLVGVLRCVHLAPMDANGYSDPFVRLFLHPSSGKKSKYKTSVRRKTLNPEFNEEFFYAGHREELAQKALLVSVWDYDLGTADDFIGGVQLSGRASGERLRHWRECLGHCDHRLELWHLLDSVPPQLGD
Protein: RNA-editing ligase 2, mitochondrial (RNA ligase 2) (EC 6.5.1.3) (TbMP48) (P86924)
Organism: Trypanosoma brucei brucei
Function: RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11134327}.
Interaction partners:
Sequence:
MLRRLGVRHFRRTPLLFVGGDGSIFERYTEIDNSNERRINALKGCGMFEDEWIATEKVHGANFGIYSIEGEKMIRYAKRSGIMPPNEHFFGYHILIPELQRYVTSIREMLCEKQKKKLHVVLINGELFGGKYDHPSVPKTRKTVMVAGKPRTISAVQTDSFPQYSPDLHFYAFDIKYKETEGGDYTTLVYDEAIELFQRVPGLLYARAVIRGPMSKVAAFDVERFVTTIPPLVGMGNYPLTGNWAEGLVVKHSRLGMAGFDPKGPTVLKFKCTAFQEISTDRAQGPRVDEMRNVRRDSINRAGVQLPDLESIVQDPIQLEASKLLLNHVCENRLKNVLSKIGTEPFEKEEMTPDQLATLLAKDALKDFLKDTEPSIVNIPVLIRKDLTRYVIFESRRLVCSQWKDILKRQSPDFSE
Protein: Serine/threonine-protein kinase RIO3 (EC 2.7.11.1) (RIO kinase 3) (sudD homolog) (O14730)
Organism: Homo sapiens (Human)
Function: Involved in regulation of type I interferon (IFN)-dependent immune response which plays a critical role in the innate immune response against DNA and RNA viruses. May act as an adapter protein essential for the recruitment of TBK1 to IRF3. Phosphorylates IFIH1 on 'Ser-828' interfering with IFIH1 filament assembly on long dsRNA and resulting in attenuated IFIH1-signaling. Can inhibit CASP10 isoform 7-mediated activation of the NF-kappaB signaling pathway. May play a role in the biogenesis of the 40S ribosomal subunit. Involved in the processing of 21S pre-rRNA to the mature 18S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22418843}.
Interaction partners:
- Serine/threonine-protein kinase RIO2
- Serine/threonine-protein kinase RIO1
- RNA-binding protein NOB1
- Protein LTV1 homolog
- Bystin
- Pre-rRNA-processing protein TSR1 homolog
- Nucleolar protein 14
- Small subunit processome component 20 homolog
- RNA-binding protein PNO1
- Eukaryotic translation initiation factor 1A, Y-chromosomal
Sequence:
MDLVGVASPEPGTAAAWGPSKCPWAIPQNTISCSLADVMSEQLAKELQLEEEAAVFPEVAVAEGPFITGENIDTSSDLMLAQMLQMEYDREYDAQLRREEKKFNGDSKVSISFENYRKVHPYEDSDSSEDEVDWQDTRDDPYRPAKPVPTPKKGFIGKGKDITTKHDEVVCGRKNTARMENFAPEFQVGDGIGMDLKLSNHVFNALKQHAYSEERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYGGSMEDEKEDSKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEALSERELFNAVSGLNITADNEADFLAEIEALEKMNEDHVQKNGRKAASFLKDDGDPPLLYDE
Protein: Biotin carboxylase (EC 6.3.4.14) (Acetyl-coenzyme A carboxylase biotin carboxylase subunit A) (P24182)
Organism: Escherichia coli (strain K12)
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Interaction partners:
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Malonyl CoA-acyl carrier protein transacylase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Bifunctional ligase/repressor BirA
- Phosphate acetyltransferase
- Probable pyruvate-flavodoxin oxidoreductase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
Sequence:
MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQEK
Protein: Pyoverdine export outer membrane protein OpmQ (Q9I189)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:19906986}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Pyoverdine export membrane fusion protein PvdR
- Pyoverdine export ATP-binding/permease protein PvdT
- PvdO
- PvdN
- Acyl-homoserine lactone acylase PvdQ
- Probable Resistance-Nodulation-Cell Division
- Probable Resistance-Nodulation-Cell Division
- FpvR
- Ferripyoverdine receptor
- PvdP
Sequence:
MSMKNLSLISACLLLGACGSTPAPLDSGLAAPSQWRYLAAGRSDASDIRQWWKAFGAPELDSLLQRALLNSQDLGAAVARVRQAQASAVIAGAPLLPELNATLGASRQKLLRDSGYSGTDATSDNDAVDSFSAGLSASYEVDFWGGRQAAYRSALESLKASEYDRATVELTLLSGVANSYLQVLALREQQRIARLNLDNAEHVLRLVETRHAAGSATALEVAQQSSLVASQRKQLPLLEQQAHEALITLATLIGEPVQALQVAERPFDSLRWPETGAGLPSELLSRRPDIANAEAQLAAAQADVQVARAALFPKLTLSASLSSGANRAADTFRNPYYNLGANLLAPIFNHGRLRAERDRSLARQEELLETYRKAILTAFADTERSLNSIDGLDRQLHWQQQELEQAQRAFDLSDSRYQAGAETLLTVLETQRTLYAAQDAAVQLRLARLQASVGLYKALGGGWQSDRQGLARKD
Protein: Cellulose synthase-like protein D5 (AtCslD5) (EC 2.4.1.-) (Q9SRW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in stem and root growth. Possesses xylan and homogalacturonan synthase activity.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:17892446}; Multi-pass membrane protein {ECO:0000305|PubMed:17892446}.
Interaction partners:
- UDP-glucuronic acid decarboxylase 5
- UDP-glucuronic acid decarboxylase 2
- Beta-D-xylosidase 4
- Glucomannan 4-beta-mannosyltransferase 7
- UDP-glucuronic acid decarboxylase 1
- Putative UDP-arabinose 4-epimerase 2
- UDP-glucuronic acid decarboxylase 3
- UDP-glucuronic acid decarboxylase 6
- Putative UDP-arabinose 4-epimerase 4
- UDP-glucuronic acid decarboxylase 4
Sequence:
MVKSAASQSPSPVTITVTPCKGSGDRSLGLTSPIPRASVITNQNSPLSSRATRRTSISSGNRRSNGDEGRYCSMSVEDLTAETTNSECVLSYTVHIPPTPDHQTVFASQESEEDEMLKGNSNQKSFLSGTIFTGGFKSVTRGHVIDCSMDRADPEKKSGQICWLKGCDEKVVHGRCECGFRICRDCYFDCITSGGGNCPGCKEPYRDINDDPETEEEDEEDEAKPLPQMGESKLDKRLSVVKSFKAQNQAGDFDHTRWLFETKGTYGYGNAVWPKDGYGIGSGGGGNGYETPPEFGERSKRPLTRKVSVSAAIISPYRLLIALRLVALGLFLTWRVRHPNREAMWLWGMSTTCELWFALSWLLDQLPKLCPVNRLTDLGVLKERFESPNLRNPKGRSDLPGIDVFVSTADPEKEPPLVTANTILSILAVDYPVEKLACYLSDDGGALLTFEALAQTASFASTWVPFCRKHNIEPRNPEAYFGQKRNFLKNKVRLDFVRERRRVKREYDEFKVRINSLPEAIRRRSDAYNVHEELRAKKKQMEMMMGNNPQETVIVPKATWMSDGSHWPGTWSSGETDNSRGDHAGIIQAMLAPPNAEPVYGAEADAENLIDTTDVDIRLPMLVYVSREKRPGYDHNKKAGAMNALVRTSAIMSNGPFILNLDCDHYIYNSMALREGMCFMLDRGGDRICYVQFPQRFEGIDPNDRYANHNTVFFDVSMRALDGLQGPMYVGTGCIFRRTALYGFSPPRATEHHGWLGRRKVKISLRRPKAMMKKDDEVSLPINGEYNEEENDDGDIESLLLPKRFGNSNSFVASIPVAEYQGRLIQDLQGKGKNSRPAGSLAVPREPLDAATVAEAISVISCFYEDKTEWGKRVGWIYGSVTEDVVTGYRMHNRGWRSIYCVTKRDAFRGTAPINLTDRLHQVLRWATGSVEIFFSRNNAIFATRRMKFLQRVAYFNVGMYPFTSLFLIVYCILPAISLFSGQFIVQSLDITFLIYLLSITLTLCMLSLLEIKWSGITLHEWWRNEQFWVIGGTSAHPAAVLQGLLKVIAGVDISFTLTSKSSAPEDGDDEFADLYVVKWSFLMVPPLTIMMVNMIAIAVGLARTLYSPFPQWSKLVGGVFFSFWVLCHLYPFAKGLMGRRGRVPTIVFVWSGLLSIIVSLLWVYINPPSGKQDYMQFQFP
Protein: Cell migration-inducing and hyaluronan-binding protein (EC 3.2.1.35) (Hyaluronan binding protein involved in hyaluronan depolymerization) (Protein 12H19.01.T7) (Q8BI06)
Organism: Mus musculus (Mouse)
Function: Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial-mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-dependent manner. May be involved in hearing.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:18448257, ECO:0000269|PubMed:24251095}. Secreted {ECO:0000250}. Note=Retained in the endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner. Strongly detected in the cytoplasm of breast carcinoma cells, whereas poorly detected in adjacent normal epithelial cells, stromal cells, or benign breast tissues. Localized in the nucleus and cytoplasm of colon adenocarcinomas (By similarity). Colocalized with clathrin heavy chain/CLTC in clathrin-coated vesicles. {ECO:0000250}.
Interaction partners:
Sequence:
MRASGRHDVSLKIVLATGCLLLANFSGASSAVATECPDQSPELQPWSPGHNRDYQVHIGHGRKLLLTSSATVHSITISGGGKLVIKDHHEHIVLRTRYILIDDGGELHAGSALCPFEGNFSIVLYGRADENILPDPYYGLKYIGVDKGGTLELHGQKKLSWTFLNKTLHPGGMQEGGYFFERSWGHRGVIVHVIDAKLGTVVHSDRFDTYRSKKESERLVQYLNAVPDGRILSVAVNDEGSRNLDDTARKAMTKLGSKHFLHLGFRHPWSFITVKGNPSSSVEDHIEYHGHKGSAAARVFKLFQTEHGEHFNVSSSSEWVQDVEWTEWFDHDKVPQSKGGEKISDLRAAYPGKICNRPIDIQATTMDGVALSTEVVYKNGQDYRFACYTRGRACRSYRVRFLCGKPVRPKLTVSIDTNVNSTILSLVDNVRSWRPGDTLVVASTDYSMYQAEEFRVLPCKACTSTQVKVAGKPQYLHIGEEIDGVDMRAEVGLLTRNIVVMGEMEDRCYPYTNHICDFFDFDTFGGHIKFALGFKAAHLEGVELKYMGQQLVGQYPIHFHLAGDLDEQGGYDPPTYIRDLSIHHTFSRCITVHGSNGLLIKDVVGYNSLGHCFFTEDGPEERNTFDHCLGLLVKSGTLLPSDRDSRMCKVITEDSYPGYIPKPRQDCNAVSTFWMANPNNNLINCAAAGSEETGFWFIFHHVPTGPSVGMYSPGYSEHIPLGKFYNNRAHSNYRAGMIIDNGVKTTEASAKDKRPFLSIISARYSPHQDADPLKPREPAIIRHFTAYKNQDHGAWLRGGDVWLDSCRFADNGIGLTLASGGTFPYDDGSKQEIKNSLFVGESGNVGTEMMDNRIWGPGGLDHSGRTLPIGQNFPIRGIQFYDGPINIQNCTFRKFAALEGRHTSALAFRLNNAWQSCPHNNVTNIAFEDVPITSRVFFGEPGPWFNQLDMDGDKTSVFHDLDGSVSEYPGSYLTKDDNWLVRHPDCINVPDWRGAICSGRYAQMYIQAYKSSNLRMKIIKNDFPSHPLYLEGALTRSTHYQQYQPVITLQKGYTIHWDQTAPAELAIWLINFNKGDWIRVGLCYPRGTTFSILSDVHNRLLKQTSKTGTFVRTLQMDKVEQSYPGRSHYYWDEDSGLLFLKLKAQNEREKFAFCSMKGCERIKIKALLPRNAGISDCTATAYPRFTERAIVDVPMPRKLFGAQLKTKDHFLEVKMESSRQHFFHLRNDFAYIEVDGRRYPCSEDGIQIVVIDGSRGHVVSHGSFRNAILQGIPWQLFNYVAAIPDNSIVLMASKGRYITRGPWTRVLEKLGADKGLKLKEKMAFVGFKGSFRPIWVTLETEDHKAKIFQVVPIPVVRKKKL
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 (Complex I-PDSW) (CI-PDSW) (NADH-ubiquinone oxidoreductase PDSW subunit) (O96000)
Organism: Homo sapiens (Human)
Function: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:28040730, ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase flavoprotein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 1
Sequence:
MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS
Protein: Mitochondrial fission factor (Q9GZY8)
Organism: Homo sapiens (Human)
Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23921378}; Single-pass type IV membrane protein {ECO:0000255}. Peroxisome {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23921378}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4KM98}.
Interaction partners:
- Dynamin-1-like protein
- Density-regulated protein
- Mitochondrial fission 1 protein
- Mitochondrial dynamics protein MID49
- Mitochondrial dynamics protein MIEF1
- Mitofusin-1
- Mitofusin-2
- Dynamin-like GTPase OPA1, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- Mitochondrial import receptor subunit TOM20 homolog
Sequence:
MSKGTSSDTSLGRVSRAAFPSPTAAEMAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVPNASVIMQVPERIVVAGNNEDVSFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPPTTPQNEEIRAVGRLKRERSMSENAVRQNGQLVRNDSLWHRSDSAPRNKISRFQAPISAPEYTVTPSPQQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDENRRPVLRGGSAAATSNPHHDNVRYGISNIDTTIEGTSDDLTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR
Protein: Lymphocyte antigen 6H (Ly-6H) (Q9WUC3)
Organism: Mus musculus (Mouse)
Function: Believed to act as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. May play a role in the intracellular trafficking of alpha-7-containing nAChRs and may inhibit their expression at the cell surface. Seems to inhibit alpha-7/CHRNA7 signaling in hippocampal neurons (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Ly-6/neurotoxin-like protein 1
- Lymphocyte antigen 6K
- Secreted Ly-6/uPAR-related protein 1
- Ly6/PLAUR domain-containing protein 6
Sequence:
MLPAAMKSLGLALLALLLCPSPAHGLWCQDCTLANSSHCAPKQCQPTDTVCASVRITDPSSSRKDHSVNKMCASSCDFVKRHFFSDYLMGFINSGILKVDVDCCEKDLCNGASVAGRSPWALAGGLLLSLGPALLWAGP
Protein: Hrp65 protein (Ct-Hrp65) (Q9U1N0)
Organism: Chironomus tentans (Midge) (Camptochironomus tentans)
Function: Component of nuclear connecting fibers associated with the transport of ribonucleoprotein particles from either the chromosome to the nuclear pore complex or their transient retention in the nucleoplasm.
Subcellular location: [Isoform 3]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
Interaction partners:
Sequence:
MDVKAEAPNGPAPVKNENQNQPKPQRENMNMNKNQNQNQNNNMGGGGGPNKRNNMNMNKNFQNRGGKGGPGMGPRGPMKNEDFIVNSKLKNLAGPTHDLPELVCEEIKFSGRNRLYIGNLTSDVTEEELKELFSPYGEISEAFINAEKNFAFLKIDYRANAERAKKDLDGRMRKNKPIRIRFAPNATTIRVKNLTPFVSNELLFKSFEVFGQVERAVIIVDDRGKTTGEGIVEFARKSGAMSALKYCSEKCYFLTSSLRPCVVETFDHIDETDGFPEKSLMRKSNDYYKARQNGPRFAEMGSFEHEFGTKWKQMYDMYKQKHDALKREMQLEEEKLEAQMEYAKFEHETESLREQLRKREQDRDRQKKEWEDRERQADESRIRDEQQMRRQQDDMQMRMQRQDEEMRRRQQENSLFMQAQQLSNMLDQQEMNHQGGGGGGGNGGNGNNQGGGGNQGGGRRNYNNDRNNDRNQNFDMMNQGGGNHGGNQYQGNQHYQGNQDQGNRFDGPPQRGNVRPWNNNDRGHRDDFQNKRRRY