wanglab/gogpt-training-data huggingface dataset:
Protein: Type VI secretion protein (D3GUX5)
Organism: Escherichia coli O44:H18 (strain 042 / EAEC)
Interaction partners:
Sequence:
MAIIAGKAGYGLIIALFSLSLSGCGLTQRVADGTVSATKSLFYRQIKTLHLDIRAREAINTSAAGIPLSVVVRIYQLKDNRSFDSADYQALFTGDNEILAGDIIAQKDVWLQPGGSVAVDMPLDDAAKFTGVAAMFLEPDQKKNTWRVVLGRDELEPDTPRLIEVSGNTLTLLPVKDK
Protein: Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase) (P11217)
Organism: Homo sapiens (Human)
Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Glycogen debranching enzyme
- UTP--glucose-1-phosphate uridylyltransferase
- Alpha-amylase 2B
- demerged
- Pancreatic alpha-amylase
- Maltase-glucoamylase
- Phosphopentomutase
- Glycogen phosphorylase, brain form
- Receptor-interacting serine/threonine-protein kinase 3
Sequence:
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDKLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEAI
Protein: Probable proton-coupled zinc antiporter SLC30A4 (Lethal milk protein) (Solute carrier family 30 member 4) (Zinc transporter 4) (ZnT-4) (O35149)
Organism: Mus musculus (Mouse)
Function: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment. Controls zinc deposition in milk.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:O55174}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within the basal region of epithelial cells. {ECO:0000250|UniProtKB:O55174}.
Interaction partners:
- Zinc transporter 6
- Zinc transporter ZIP1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter ZIP4
- Zinc transporter ZIP13
- Zinc transporter SLC39A7
- Zinc transporter ZIP10
- Zinc transporter ZIP6
- Zinc transporter ZIP11
- Metal cation symporter ZIP14
Sequence:
MAGPGAWKRLKSLLRKDDTPLFLNDTSAFDFSDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQDLPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAVQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTFRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKSTAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTIQLQSYRQEVIRTCANCHSSST
Protein: Solute carrier family 12 member 8 (Cation-chloride cotransporter 9) (A0AV02)
Organism: Homo sapiens (Human)
Function: Cation/chloride cotransporter that may play a role in the control of keratinocyte proliferation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cystatin-A
Sequence:
MTQMSQVQELFHEAAQQDALAQPQPWWKTQLFMWEPVLFGTWDGVFTSCMINIFGVVLFLRTGWLVGNTGVLLGMFLVSFVILVALVTVLSGIGVGERSSIGSGGVYSMISSVLGGQTGGTIGLLYVFGQCVAGAMYITGFAESISDLLGLGNIWAVRGISVAVLLALLGINLAGVKWIIRLQLLLLFLLAVSTLDFVVGSFTHLDPEHGFIGYSPELLQNNTLPDYSPGESFFTVFGVFFPAATGVMAGFNMGGDLREPAASIPLGSLAAVGISWFLYIIFVFLLGAICTREALRYDFLIAEKVSLMGFLFLLGLYISSLASCMGGLYGAPRILQCIAQEKVIPALACLGQGKGPNKTPVAAICLTSLVTMAFVFVGQVNVLAPIVTINFMLTYVAVDYSYFSLSMCSCSLTPVPEPVLREGAEGLHCSEHLLLEKAPSYGSEGPAQRVLEGTLLEFTKDMDQLLQLTRKLESSQPRQGEGNRTPESQKRKSKKATKQTLQDSFLLDLKSPPSFPVEISDRLPAASWEGQESCWNKQTSKSEGTQPEGTYGEQLVPELCNQSESSGEDFFLKSRLQEQDVWRRSTSFYTHMCNPWVSLLGAVGSLLIMFVIQWVYTLVNMGVAAIVYFYIGRASPGLHLGSASNFSFFRWMRSLLLPSCRSLRSPQEQIILAPSLAKVDMEMTQLTQENADFATRDRYHHSSLVNREQLMPHY
Protein: Trichohyalin (A0A0B4J1F9)
Organism: Mus musculus (Mouse)
Interaction partners:
- Loricrin
- Repetin
- Protein-arginine deiminase type-3
- Protein-glutamine gamma-glutamyltransferase K
Sequence:
MSPLIRSIVDITEVFNQYASQSCDGASLSKKDLKNLLERELGDVLQRPHDPETIDLTLELLDRDCNGRVDFNEFLLFLFKIAQACYYALDQAAELGEKRALPNEKRNLSQDRRQEDQRRFEPRSRQLDEEPGRRSWQKRREQEERAEEQRLEQRYRQHRDEEQRLQRRELQELEERLAEKEPLGWSKGRDAEEFSEVEEQQRQERQELKGKGQTEERRLQKRRQEELREPLLRRDLELRREQELRREQELRQEQRREQELRREQELRQELRREQELNRRQELRREQELRREQELRQELRREQELRREQELRQELRREQELRREQELRQELRREQELRREQELRQELRREQELRREQELRQELAEEDELTRIREPDESITQRWQWQLENEADARQNKVYSRPSRQEQRLRQELGERQLREQEEQRRDLQQERPAEEARQRNQWERPQRAEERLEQEQRFRDREEQRFREEKLQRAELQDSLLDEEQRRLQEERREPNRSRQLREESQRRRTLYAKPSQRQRREEELREERLLQEEQRQQRERKHRREEDLQQEEKRLQQDEEQLQRERRRLQRERQYQEEDLQQEEERLQQEEERLQRERRRLQQERQYQEEDLQRLRDEDQRRDLKWQWQPRKENEVRSNRLFTKRRGDEEPIQQLEDSQERERRQDRRPLQDEEEEKRELEQERRRRQQRDRQILEEEQFQREHQREARRRDETFQEEEQLQGESRRRQQEREGKFLEEERQLRTEREEQRRRQEQEREFQEEEEHLQEREKELRQECDRKSREQERRQQREEEQLRRQERDQRFRREQERHLEREEEQLRDRPSRREQERHQEREEEQLRDRPSRREQERHQEREEEQLRDRPSRREQERHQEREEEQLRDRPFRREQERRLEREEEQLRDRPSRREQERHQEREEEQLRDRPSRREQERRLEREEEQLRDRSFRREQELRRDRKFHEEEERREELEEEQRGQERDRLRVEEQLRGQREEEQRRRQECDRKLHRELEVRQELEEERLRDRKLRREQELRRDRKFHEEEERRHEEFEEKQLRLQEPDRRFRREQELRQECVEEERLRDSKIRREQELRREREEERLRDRKIRRDQELRQGLEEEQLRRQELDRKFREEQELDQELEEERLRDRKIRREQELRREQELRREQEFRREQELRREQEFRREQELRQEREEERLRDRKIRRDQELRQGLEEEQLRRQERDRKVREEQELDQELEEERLRDRKIRREQELRREQELRREQEFRREQGLRREREEERLRDRKIRRDQELRQGLEEEQLRRQERDRKFREEQELGQELEEERLRDRKIRREQELRREREQEQRRRLEREEEQQRLHEREEEQRRRQEREQEQQRCLEREEEQFRFEEQQRRRQEREQQLRQERDRRVLEEEELRQEREELLHRQVGGRKFREEERLRLEREEQQRRLQERDNRRFREEVELRQEREGQQLRQERDRKFREVEELRQEEQRRRQERDRKFREEKHPREEREEQQLRREKRDGQYLAEEQFARDTIRRQEQELRQEEEQRRRQERERKFQEEQIRRRQEEQRRRQILEPGTRQFANVPVRSSPLYEYIQEQRSQYRP
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (EC 7.1.1.2) (Complex I-30kD) (CI-30kD) (NADH-ubiquinone oxidoreductase 30 kDa subunit) (O75489)
Organism: Homo sapiens (Human)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18826940, ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:17209039}; Peripheral membrane protein {ECO:0000305|PubMed:18826940}; Matrix side {ECO:0000269|PubMed:18826940}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MAAAAVARLWWRGILGASALTRGTGRPSVLLLPVRRESAGADTRPTVRPRNDVAHKQLSAFGEYVAEILPKYVQQVQVSCFNELEVCIHPDGVIPVLTFLRDHTNAQFKSLVDLTAVDVPTRQNRFEIVYNLLSLRFNSRIRVKTYTDELTPIESAVSVFKAANWYEREIWDMFGVFFANHPDLRRILTDYGFEGHPFRKDFPLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPVYRQPPESLKLEAGDKKPDAK
Protein: Very long-chain-fatty-acid--CoA ligase bubblegum (EC 6.2.1.3) (Q9V3S9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Probably by regulating lipid storage and catabolism, plays a role in neuronal function.
Interaction partners:
- long-chain-fatty-acid--CoA ligase
- Lysosomal thioesterase PPT2 homolog
- Long-chain-fatty-acid--CoA ligase heimdall
- Palmitoyl-protein thioesterase 1
- Fatty acid synthase
- carnitine O-palmitoyltransferase
- Fatty acid synthase
- Fatty acid synthase
- Long-chain-fatty-acid--CoA ligase
- Peroxisomal multifunctional enzyme type 2
Sequence:
MSTIDALYNRPGPNRLRQADAYRTTNRQDAVKIRMAKDGIGAEEPISVPGLLKRTVNNYGDYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEDGYYRWSEIESMNVSDVEDQYMTRLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADKDALKGTLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGITLKHYMVSQGKSSGGFRYKIAKSLIMSKVKQALGFDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKELDAISNAFLVGEQRKYLTVLITLKTEVDKDSGEPLDELSHESSVWVKSLGVEHKTVSDILAAGPCPKVWKSIEDAIKRANKQSISNAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLYA
Protein: Transcription factor (A0A8I6A268)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009404, ECO:0000256|RuleBase:RU003796}.
Interaction partners:
Sequence:
MKIISTPQRITNSGSVLIGSPYTPAPAMVTQTHIAEAAGWVPSDRKRAREFIDSDFSESKRSKKGDKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNASNHLAADSQAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAVNSTIQLPFIVINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKIAKSLVPKALEGYITDVSTGPSWLNQGLLLNSTQSVSNLDPTTGATVPQSSVNQGLCLDAEVALATGQFLAPNSHQSSTAASQFSESRGETPCSFNDEEEEDEEEDPSSPE
Protein: Ankyrin repeat-containing protein At5g02620 (Q6AWW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probably inactive leucine-rich repeat receptor-like protein kinase IMK2
- Glucan endo-1,3-beta-glucosidase 10
- UDP-arabinopyranose mutase 2
- LysM domain-containing GPI-anchored protein 2
- Patellin-3
- Proline-rich protein 1
- Plasmodesmata-located protein 1
- Probable calcium-binding protein CML41
- Urease accessory protein D
- Plasmodesmata-located protein 5
Sequence:
MKEIKKTMTKQMTARRDDTPLHTAVREGKTDLLLEMIGEHDGVELKELLAEQNQSGETALYVAAEYGYTDMVKILMKHSDSVLAGTKAKNGFDAFHIAAKNGNLQVLDVLIEANPELSFTFDSSKTTALHTAASQGHGEIVCFLLDKGVDLAAIARSNGKTALHSAARNGHTVIVKKLIEKKAGMVTRVDKKGQTALHMAVKGQNTEIVDVLMEADGSLINSADNKGNTPLHIAVRKNRAEIVQTVLKYCEVSRVAVNKSGETALDIAEKTGLHEIVPLLQKIGMQNARSIKPAEKVEPSGSSRKLKETVSEIGHEVHTQLEQTGRTRREIQGIAKRVNKMHTEGLNNAINSTTLVAILIATVAFAAIFNVPGQYTDDPKDVPPGYSLGEARAAPRPEFLIFVVFDSFALFISLAVVVVQTSVVVIERRAKKQMMAIINKLMWMACIMISVAFVSLSFVVVGEKEKPLAVGVTAIGALIMVSTLGTMCYWVIANRIEGSKSSPASMMSDPELADSKHNRKLYAV
Protein: Transmembrane protein 102 (Common beta-chain associated protein) (CBAP) (Q8N9M5)
Organism: Homo sapiens (Human)
Function: Selectively involved in CSF2 deprivation-induced apoptosis via a mitochondria-dependent pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17828305}; Single-pass membrane protein {ECO:0000269|PubMed:17828305}. Note=Although it is found at the cell surface, the majority of the molecules seems to be located in intracellular compartments.
Interaction partners:
- Guanine nucleotide exchange factor for Rab-3A
Sequence:
MASAVWGSAPWWGPPPPAPARPLTDIDFCSGAQLQELTQLIQELGVQESWSDGPKPGADLLRAKDFVFSLLGLVHRRDPRFPPQAELLLLRGGIREGSLDLGHAPLGPYARGPHYDAGFTLLVPMFSLDGTELQLDLESCYAQVCLPEMVCGTPIREMWQDCLGPPVPGARDSIHRTESEESSKDWQSSVDQPHSYVTEHEAPVSLEKSPSDVSASESPQHDVVDLGSTAPLKTMSSDVTKAAVESPVPKPSEAREAWPTLCSAQVAAWFFATLAAVAESLIPVPGAPRLVHAARHAGFTTVLLATPEPPRRLLLFDLIPVVSVAGWPEGARSHSWAGPLASESASFYLVPGGGTERPCASAWQLCFARQELALKARIPAPLLQAHAAAQALLRPLVAGTRAAAPYLLRTLLYWACERLPALYLARPENAGACCLGLLDELGRVLEAGTLPHYFLNGRQLRTGDDSAALLGELARLRGDPARALRAAVEEAKVARKGGGLAGVGGGAH
Protein: LP06813p (Q95TJ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTFVEREEYQYVVRPDQVKPLDNLKPEGEFYSPEKPKYKPGERPSQVRPEDNLRPEGEFYTPEKPGFRPAERPEQKKPEDNLKPEGEFYSPEKPKYKPGERPSQVRPEDNLRPEGEFYTPEKPGFRPAERPEQKKPEDNLKPEGEFYSPEKPKYKPGERPSQVRPEDNLRPEGEFYTPEKPGFRPAERPEQKKPEDNLKPEGEFYSPEKPKYKPGERPSQVRPEDNLRPEGEFYTPEKPGFRPAERPVQKKPQDNLKPEGEFVKPEKQVYRPADKTERIIRKDNLRTEGEMTFIEREEYQYVVRPDQVKPLDNLKPEGEFYSPEKPKYKPGERPSQVRPEDNLRPEGEFYTPEKPGFRTAERPEQKKPEDNLRPEGDFYSPEKQPYRPGERPTQVRPEDNLRPEGKFFAPEKPGYKAGDRPVPKKPVDNLKTEGEFFTPDRPKYQPADRVTVVRQKDNLKVEGEFYVQEKEVFKPAERPKQKKPHDNLKPEGEMVIPEKGKYKPADKVTRVIHKDNLRSEGEMTFTEKTEYHNVVRPTPVKPEDNLRTSGKLYVPEKPVHTNGERPEPVKPKDNLKPEGVMYTPEKPKYEPASRPEQKKYADNLKPEGKMHIPEKDGYRPADKVKTVIRKDNLRTEGEMTFTQKEEYHHVKRPEQVKPSDNLKVEGEFYTPNKTSFTPAERPVQKKPKDNLKPEGEFYKRTDRSETDSKMVTETIKRETPKRPVDNLKLEGSMTVTRRNDYKSTANTTVDKVQRTQKINHNSSSITLGSDTTIRKTTNQMNYVSGKDAVKQVDSNGQNPVDGLIVVSTTKVTTVIGGRHKKEPETEYVKRPAKINVIENVAKNTTTTNIENTQNIHKESTSLQRNQKVIKGTEIITGTDVSSTAIESNRSHLTDKNTGDISSKVISGGSVSNNVTGETSSRVISGRNVTSNITENSTSRVMSGRNVSSDAFGETTTRVVSGRSAANNITGDTTSRVLSGSTVGHNISEDSTSRTVSGGRSSANNIVTGSTSSHMTTSKHFHHRKSEFSSEADVSNTVFHRKNVTTDSNTANGSLTSNGKMQRKSILNLHEQPSSTTTYGGERQSYSSIHRQNRDSDANATFSTERRTCNVHKENREQTVKNSSSMTRIISGGTSGSNAERSTVTRSHVSGGGGIDFSSQSHSHTGSHTSRHRGGNQQVSSLGGGIDFPSYSAHGHGAERVVTRRGNQSSISLGNEKFTGSSLYKSEYITAPKTTCAVHKIKQGAFQHTRSTQEHKFFKTSN
Protein: Synaptotagmin 1 (p65) (P21521)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:1840599}; Single-pass membrane protein {ECO:0000269|PubMed:1840599}. Synapse {ECO:0000269|PubMed:1840599}. Note=Synaptic vesicles in neurons.
Interaction partners:
- Synaptosomal-associated protein 25
- Synapsin
- Synaptobrevin
- Protein stoned-B
- Ras-related protein Rab-3
- Syntaxin-1A
- Synaptosomal-associated protein
- Neuronal synaptobrevin, isoform J
- Vesicular glutamate transporter, isoform A
- Complexin
Sequence:
MPPNAKSETDAKPEAEPAPASEPAADLESVDQKLEETHHSKFREVDRQEQEVLAEKAAEAASQRIAQVESTTRSATTEAQESTTTAVPVIKKIEHVGEVVTEVIAERTGLPTWGVVAIIILVFLVVFGIIFFCVRRFLKKRRTKDGKGKKGVDMKSVQLLGSAYKEKVQPDMEELTENAEEGDEEDKQSEQKLGRLNFKLEYDFNSNSLAVTVIQAEELPALDMGGTSDPYVKVYLLPDKKKKFETKVHRKTLSPVFNETFTFKSLPYADAMNKTLVFAIFDFDRFSKHDQIGEVKVPLCTIDLAQTIEEWRDLVSVEGEGGQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIAIMQNGKRLKKKKTSIKKCTLNPYYNESFSFEVPFEQIQKICLVVTVVDYDRIGTSEPIGRCILGCMGTGTELRHWSDMLASPRRPIAQWHTLKDPEETDEILKNMK
Protein: Solute carrier family 4 (Anion exchanger), member 1, adaptor protein (Q5BKS1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRFGGSTRLFILQGPEEDREAESELTVTQLKELRKQQQILLEKKMLGEDSDEEEEANTTEGKSSRSGQDDELGCTWGMGEDAVEDEAEENPIALDFQQDREAFYIKDPKKALQGFFDREGEELEYEFDEQGHSTWLCRVRLPVDDSTGKQLVAEAIHSGKKKEAMVQCSLEACRVLDTLGLLRQEAVSRKRKAKNWEDEDFYDSDDDTFLDRTGLVEKKRLNRMKKAGKLDEKPETFESLVAKLNDAERELAEISERLKASSKVLSEPSSQDSLDAFMSEMKSGSTLDGVSRKKLHLRTFELRKEQQRLKGLIKLVKPAEIPELKKTELQTTNAENKTKKLALPLFGAMKGGSKFKLKTGTVGKLPPKRPELPPALMQMKDEPEVEEEEEEEEEEEEKVKEEHEERVEDGGVRLLQEPELELEAAVEHPSAPSEPSCSKETKSHAAPANEYKQDRDEPKKKKSPGPGKFPPILSSKYPEDDPDYCIWVPPEGQSGDGRTHLNDKYGY
Protein: Glycine Rich Secreted Protein (Q21073)
Organism: Caenorhabditis elegans
Interaction partners:
- Basic proline-rich protein
- BRO1 domain-containing protein
- RNA helicase
Sequence:
MYSKAVLLALLVCSALAAPKAKKNQTGNEQNQQSQSGQRQTGQGQQVGSQQGFGGMQGGFGGQSGFGGGSSQGGFGGFGQQGGFGGNSQGGFGGQQGGFSGNSPGGFEGQQGGFGGFGQQVGFGGQGGFGGNSQGGFGGQQSGFGGQGQQSGFGGGFGGNSQNGFPAQRPSQQSGFGGQGMQSGFGMNSQQGDFGGQGQQSGFEGNTQGHSQGGFGGQSSSGFGGQQGGQGGQGGFGGSTRTGGMQGGQGGQSGSSGFGGFGGLGQEGQQGGQEGSNGNNNQGF
Protein: Calbindin (Calbindin D28) (D-28K) (PCD-29) (Spot 35 protein) (Vitamin D-dependent calcium-binding protein, avian-type) (P12658)
Organism: Mus musculus (Mouse)
Function: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
Interaction partners:
- Parvalbumin alpha
- Glutamate decarboxylase 1
- Protein S100-G
- 45 kDa calcium-binding protein
- Somatostatin
- RNA binding protein fox-1 homolog 3
- Pro-neuropeptide Y
- Glial fibrillary acidic protein
- Caspase-3
- Tyrosine 3-monooxygenase
Sequence:
MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKSFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNITTYKKNIMALSDGGKLYRTDLALILSAGDN
Protein: G1/S-specific cyclin-D3 (P30281)
Organism: Homo sapiens (Human)
Function: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Shows transcriptional coactivator activity with ATF5 independently of CDK4.
Subcellular location: Nucleus {ECO:0000269|PubMed:15358120}. Cytoplasm {ECO:0000269|PubMed:15358120}.
Interaction partners:
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1B
- Retinoblastoma-like protein 2
- Cyclin-dependent kinase 4 inhibitor C
- Cyclin-dependent kinase inhibitor 1C
- Retinoblastoma-associated protein
- Proliferating cell nuclear antigen
Sequence:
MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQREIKPHMRKMLAYWMLEVCEEQRCEEEVFPLAMNYLDRYLSCVPTRKAQLQLLGAVCMLLASKLRETTPLTIEKLCIYTDHAVSPRQLRDWEVLVLGKLKWDLAAVIAHDFLAFILHRLSLPRDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVQGLGACSMSGDELTELLAGITGTEVDCLRACQEQIEAALRESLREASQTSSSPAPKAPRGSSSQGPSQTSTPTDVTAIHL
Protein: U6 snRNA-associated Sm-like protein LSm6 (Q9UUI1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- LSM1-LSM7 complex subunit lsm1
- LSM complex subunit lsm4
- LSM complex subunit lsm2
- LSM complex subunit lsm5
- LSM complex subunit lsm7
- LSM complex subunit lsm3
- LSM2-LSM8 complex subunit lsm8
- Small nuclear ribonucleoprotein Sm D2
- U4/U6 snRNA-associated-splicing factor prp24
- U4/U6.U5 tri-snRNP-associated protein snu66
Sequence:
MDSSPNEFLNKVIGKKVLIRLSSGVDYKGILSCLDGYMNLALERTEEYVNGKKTNVYGDAFIRGNNVLYVSALDD
Protein: Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) (Q61221)
Organism: Mus musculus (Mouse)
Function: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15225651}. Nucleus {ECO:0000269|PubMed:15225651, ECO:0000269|PubMed:21546903}. Nucleus speckle {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in the nucleus and speckles (PubMed:21546903). Cytoplasmic in normoxia, nuclear translocation in response to hypoxia (By similarity). {ECO:0000250|UniProtKB:Q16665, ECO:0000269|PubMed:21546903}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Egl nine homolog 1
- Histone acetyltransferase p300
- von Hippel-Lindau disease tumor suppressor
- Aryl hydrocarbon receptor nuclear translocator 2
- Aryl hydrocarbon receptor nuclear translocator
- Endothelial PAS domain-containing protein 1
- Elongin-C
- Cullin-2
- Prolyl hydroxylase EGLN3
Sequence:
MEGAGGENEKKKMSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGGLDSEDEMKAQMDCFYLKALDGFVMVLTDDGDMVYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGPVRKGKELNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTESVLKPVESSDMKMTQLFTKVESEDTSCLFDKLKKEPDALTLLAPAAGDTIISLDFGSDDTETEDQQLEDVPLYNDVMFPSSNEKLNINLAMSPLPSSETPKPLRSSADPALNQEVALKLESSPESLGLSFTMPQIQDQPASPSDGSTRQSSPERLLQENVNTPNFSQPNSPSEYCFDVDSDMVNVFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESNSPSPPSMSTVTGFQQTQLQKPTITATATTTATTDESKTETKDNKEDIKILIASPSSTQVPQETTTAKASAYSGTHSRTASPDRAGKRVIEQTDKAHPRSLNLSATLNQRNTVPEEELNPKTIASQNAQRKRKMEHDGSLFQAAGIGTLLQQPGDCAPTMSLSWKRVKGFISSEQNGTEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
Protein: Glyceraldehyde dehydrogenase medium chain (EC 1.2.99.8) (Glyceraldehyde dehydrogenase subunit B) (Glyceraldehyde dehydrogenase subunit beta) (Q4J6M6)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10095793}.
Interaction partners:
- Glyceraldehyde dehydrogenase small chain
- Glyceraldehyde dehydrogenase large chain
- Carbon monoxide dehydrogenase small chain
- Carbon monoxide dehydrogenase large chain
- Carbon monoxide dehydrogenase
- 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- Carbon monoxide dehydrogenase large chain
- Carbon monoxide dehydrogenase large chain
- Aldehyde oxidase and xanthine dehydrogenase
- Carbon monoxide dehydrogenase large chain
Sequence:
MYPPEFSYVRAESLQEALKFLEGNDNTRPLAGGQSLIPMLKLRVLSPDYILDINRLNELNYVKTSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSASGSRSVKALDFFKGPFTTDTNKGELVTQIEVPVLDGYKTVYKKVVRRAGDYALASVALAIKLKGNEIEDIKLAYGGVHDKPFRAMEVEKNVIGKKLNDDLVKDIASKVSSQINPPSDHRGSSWYRREVVKVLTMKAFKEVA