wanglab/gogpt-training-data huggingface dataset:
Protein: Exportin-4 (Exp4) (Q9C0E2)
Organism: Homo sapiens (Human)
Function: Mediates the nuclear export of proteins (cargos), such as EIF5A, SMAD3 and isoform M2 of PKM (PKM2). In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO4 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Catalyzes the nuclear export of hypusinated EIF5A; a small cytoplasmic protein that enters nucleus and accumulates within nucleolus if not exported back by XPO4. Specifically mediates nuclear export of isoform M2 of PKM (PKM2) following PKM2 deacetylation by SIRT6. Also mediates the nuclear import of SOX transcription factors SRY and SOX2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16449645}. Nucleus {ECO:0000269|PubMed:16449645}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:16449645}.
Interaction partners:
- Exportin-T
- Exportin-2
- Exportin-1
- Eukaryotic translation initiation factor 5A-1
- THO complex subunit 2
- Eukaryotic translation initiation factor 5A-1-like
- Ran GTPase-activating protein 1
- Exportin-6
- Importin-13
- EEF1A lysine methyltransferase 1
Sequence:
MMAAALGPPEVIAQLENAAKVLMAPPSMVNNEQRQHAEHIFLSFRKSKSPFAVCKHILETSKVDYVLFQAATAIMEAVVREWILLEKGSIESLRTFLLTYVLQRPNLQKYVREQILLAVAVIVKRGSLDKSIDCKSIFHEVSQLISSGNPTVQTLACSILTALLSEFSSSSKTSNIGLSMEFHGNCKRVFQEEDLRQIFMLTVEVLQEFSRRENLNAQMSSVFQRYLALANQVLSWNFLPPNLGRHYIAMFESSQNVLLKPTESWRETLLDSRVMELFFTVHRKIREDSDMAQDSLQCLAQLASLHGPIFPDEGSQVDYLAHFIEGLLNTINGIEIEDSEAVGISSIISNLITVFPRNVLTAIPSELFSSFVNCLTHLTCSFGRSAALEEVLDKDDMVYMEAYDKLLESWLTLVQDDKHFHKGFFTQHAVQVFNSYIQCHLAAPDGTRNLTANGVASREEEEISELQEDDRDQFSDQLASVGMLGRIAAEHCIPLLTSLLEERVTRLHGQLQRHQQQLLASPGSSTVDNKMLDDLYEDIHWLILVTGYLLADDTQGETPLIPPEIMEYSIKHSSEVDINTTLQILGSPGEKASSIPGYNRTDSVIRLLSAILRVSEVESRAIRADLTHLLSPQMGKDIVWFLKRWAKTYLLVDEKLYDQISLPFSTAFGADTEGSQWIIGYLLQKVISNLSVWSSEQDLANDTVQLLVTLVERRERANLVIQCENWWNLAKQFASRSPPLNFLSSPVQRTLMKALVLGGFAHMDTETKQQYWTEVLQPLQQRFLRVINQENFQQMCQQEEVKQEITATLEALCGIAEATQIDNVAILFNFLMDFLTNCIGLMEVYKNTPETVNLIIEVFVEVAHKQICYLGESKAMNLYEACLTLLQVYSKNNLGRQRIDVTAEEEQYQDLLLIMELLTNLLSKEFIDFSDTDEVFRGHEPGQAANRSVSAADVVLYGVNLILPLMSQDLLKFPTLCNQYYKLITFICEIFPEKIPQLPEDLFKSLMYSLELGMTSMSSEVCQLCLEALTPLAEQCAKAQETDSPLFLATRHFLKLVFDMLVLQKHNTEMTTAAGEAFYTLVCLHQAEYSELVETLLSSQQDPVIYQRLADAFNKLTASSTPPTLDRKQKMAFLKSLEEFMANVGGLLCVK
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (A0A1D8PQ26)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Purine nucleoside phosphorylase
- Adenine deaminase
- Adenine phosphoribosyltransferase
- Adenylate kinase
- Adenylosuccinate lyase
- AMP deaminase
- GTP:AMP phosphotransferase, mitochondrial
- Phosphodiesterase
- 3'\5'-cyclic-nucleotide phosphodiesterase PDE1
- Adenylate kinase isoenzyme 6 homolog HBR1
Sequence:
MSSYKLVCLGNPLLDLQAKVEKDYLQKYDLKDNDAILADPKHMPIFEELIKRDDLVLVAGGAAQNTARGAQYILPPNSVVYFGSVGKDIYAERLNQANEEYGLTTKYQIQDDIATGKCAALIHNHDRSLVTDLAAANHFTPDHLQKPENWEIVEKAGFYYIGGFHLTVSPPAIKLLGEHASKTNKPLVLNFSAPFIAQFFKQQLDEVLPYVDYVIANESEAAAYAESHDLKTTDVVEIAKEVAKLPKENKQIPRTVIFTQGLEPTITVTYDATKDSFDVQQYPVKELAKEKVVDTNGAGDAFAAGFVASLVEGKDLPQSVDVGQWAAALSIQEVGPSFPFPKQTYSN
Protein: V-type proton ATPase 116 kDa subunit a 2 (V-ATPase 116 kDa subunit a 2) (Immune suppressor factor J6B7) (ISF) (Lysosomal H(+)-transporting ATPase V0 subunit a 2) (ShIF) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2) (P15920)
Organism: Mus musculus (Mouse)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:16415858}; Multi-pass membrane protein {ECO:0000269|PubMed:16415858}. Endosome membrane {ECO:0000269|PubMed:16415858}. Note=In kidney proximal tubules, detected in subapical early endosomes.
Interaction partners:
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit H
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
Sequence:
MGSLFRSESMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEITRADIPLPEGEASPPAPPLKHVLEMQEQLQKLEVELREVTKNKEKLRKNLLELVEYTHMLRVTKTFLKRNVEFEPTYEEFPALENDSLLDYSCMQRLGAKLGFVSGLIQQGRVEAFERMLWRACKGYTIVTYAELDECLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHIYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVCSRVVQVRKMKAIYHMLNMCSFDVTNKCLIAEVWCPEVDLPGLRRALEEGSRESGATIPSFMNTIPTKETPPTLIRTNKFTEGFQNIVDAYGVGSYREVNPALFTIITFPFLFAVMFGDFGHGFVMFLFALLLVLNENHPRLSQSQEILRMFFDGRYILLLMGLFSVYTGLIYNDCFSKSVNLFGSGWNVSAMYSSSHSPEEQRKMVLWNDSTIRHSRTLQLDPNIPGVFRGPYPFGIDPIWNLATNRLTFLNSFKMKMSVILGIFHMTFGVVLGIFNHLHFRKKFNVYLVSVPEILFMLCIFGYLIFMIIYKWLAYSAETSREAPSILIEFINMFLFPTSKTHGLYPGQAHVQRVLVALTVLAVPVLFLGKPLFLLWLHNGRNCFGMSRSGYTLVRKDSEEEVSLLGNQDIEEGNSRMEEGCREVTCEEFNFGEILMTQAIHSIEYCLGCISNTASYLRLWALSLAHAQLSDVLWAMLMRVGLRVDTTYGVLLLLPVMAFFAVLTIFILLVMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFSLLSSKFSNDDSIA
Protein: Translation initiation factor eIF2B subunit delta (eIF2B GDP-GTP exchange factor subunit delta) (G5EFF9)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit 2
- protein-synthesizing GTPase
- SUI1 domain-containing protein
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Major facilitator superfamily
Sequence:
MSDKNINTDKKHPADKLKETFEKLNNEVKLLGMILGVKSENNQQVVPPTTAEEPAQGEDKNQYHKDVTAEDKKARKAAKAAEKKARAEKSVANKAAAAAGSTQNQGQKKEKPPKEHSAVPSESTTKLIEENAQLTKTTEQLAAKMETLVIEDVKINGSLKPAIKKSTGVEKNVRHVHNVIMPSVVTFDLPKNQTKTLPSASDSDEAVASEIESTAIAQLDDATSFVHIHPAFLTLMAKAELEKIPDVETVCIQFIAAFKEFLRDWTVEREKNNINASTFGHDLDLAIRPQLAHMTQNGHWPLPFALGNTVRLLKRTIKRLEESTNMKCEEELQVYLEDTLAINFCHAYKAISQLLVRKIQQFKKVVVFDWCPVVNHVLLEAKQQIPDMQLSVIDANSNGRGTRHVKSFVDQGYNVKYVTMKGASWASLASGVLILGCSAIFANGAVAARKGALAVVLCANHYNIPVIVVAEHFKFIDKGQVYQRVALLGRQNIECIQSDLVTAVVTDLRILGPTSAPAVLKAKALTDMA
Protein: Ribose-5-phosphate isomerase A (EC 5.3.1.6) (Phosphoriboisomerase A) (PRI) (Q58998)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Interaction partners:
- Bifunctional enzyme Fae/Hps
- Ribulose-phosphate 3-epimerase
- Ribose-phosphate pyrophosphokinase
- Putative transketolase C-terminal section
- AMP phosphorylase
- Putative transketolase N-terminal section
- Uncharacterized protein MJ0644
- Succinate--CoA ligase subunit alpha
- 5'-nucleotidase SurE
- Pyridoxal 5'-phosphate synthase subunit PdxT
Sequence:
MSNEDLKLKVAKEAVKLVKDGMVIGLGTGSTAALFIRELGNRIREEELTVFGIPTSFEAKMLAMQYEIPLVTLDEYDVDIAFDGADEVEETTLFLIKGGGGCHTQEKIVDYNANEFVVLVDESKLVKKLGEKFPIPVEVIPSAYRVVIRALSEMGGEAVIRLGDRKRGPVITDNGNMIIDVFMNIDDAIELEKEINNIPGVVENGIFTKVDKVLVGTKKGVKTLKK
Protein: Jun dimerization protein 2 (Q78E65)
Organism: Rattus norvegicus (Rat)
Function: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1, such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. May control transcription via direct regulation of the modification of histones and the assembly of chromatin (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor Jun
- Transcription factor JunD
- Cyclic AMP-dependent transcription factor ATF-2
Sequence:
MMPGQIPDPSVTAGSLPGLGPLTGLPSSALTTEELKYADIRNIGAMIAPLHFLEVKLGKRPQPVKSELDEEEERRKRRREKNKVAAARCRNKKKERTEFLQRESERLELMNAELKTQIEELKLERQQLILMLNRHRPTCIVRTDSVRTPESEGNPLLEQLDKK
Protein: BRO1 domain-containing protein (Enhancer of glp-1) (G5EBN5)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
Sequence:
MEALPIMPMLAPQSRSSTLSYDNIPNFDFRLRMKEYILLTFNADPHDYDSAFDELTQMKFEANVPTPSVEQTLKLKRYYGQLCMMQKRFPMGAGEQLETPFAWHDGLIDIRSAQSEVTICDIEFEKASVMFNIGACHAQYAAEQTRDTQDCIKAAFMHFQYAAYAFEQLNSFRNSDIFYPSVDLDANVISFYYKVMIAQAQECLVQKSLLDNRSAIVIAKLSLWLQEAYDSAAKIVDEWSVNIPESVQRYYAKICSLKSAMYAVIAYMSFGDNLEKEDKKMGWRLQYYNIANKYMELLSSNHSKMRERYPELFVTSSFLFDVISAKQRNAEKENDFIYHDRVPKQEDAIDAVQKDGGGAMCKVKTLSFDPLDPSVCGCDLFGKLLPTFVQDAVKKYSDDKDQALREIKECVRSYDEHLNYQLQLAEFDKLRFMLNEGKRSREAWFEISEDLMKRNADMTSYPDCVPNLIDKMGESSDTARVAEAKLNTLLSKLRAIDLQKSSIRSDEGFILIQKELERLAEHLEQAKAHNVSLNKAIAQHSANLQLLTLPCREMWMKIVPPEQQGEMRNGSSPEELQVRKMIEKVMEMQAQRRKLVEQFEADLKADNISNKLMGTNERGAEEIMKSELTKHTNIQQLIRLNITAQDAILRAFADANADFFEERLAMSTKKEEYEKRVSELCASYEVYRDVSKKVDEGEQFYRQLMARCDQFAIPVHAMEEQYREEMEKKERAKKEAEHHLNQIRMSRDAQNALMDFGGGRGGGAPGARAQQQAYQPSRGAAGAGAGAPRGPRLGDFMDSYRARKQAPQAQIPEDQGPPSPTPSSICDFPVQSQRSQRFGAFEGAQGAPGAQRGYQGPHSPVPGALTGSQASGPFGAPPGAPHGYGAPLQAPPQAPYGYDPSRYQDPSTYPAPPPILPGSAAYEHAIRPYPGDTGSYQVPRIVPGAQYGAQAGSGAYFGAQFGAQGAQGAHFGAQGVQFGAQGAQGAHFGAQGAQGAQFGAQGAQGEQFGAQGAQGAHFGAQGAQGAHFGAQGAQGTQFGAQGAQGPPPASYGAPTPPQASYGPAPGAHGYQNGAQGPPGAEVGAQGPPGAHFGAHGASAPPPTSYGAPTPQRPPQASYGAAPGAQGPPGGQFEAHGAAALPPTSHGAPTPQGPFGAAPGAQFGAQGPYGQQGARYEAQKSPGAAIFGAPGAPPQHQGSFGAQFGVPPPQNSAPGAQFGAKPEASSHAPTPPPQPHPSYQAPAPPPALSVFQHSPQGAPITAPPPASSHHEHIAAPQARFTPTPGAPSPWHATPAELKTPWNTTPQYHAPPGAQAAAPEAPAAPAPGAPAARSNVDLLSDLLGDFNLPPQPIQPTVHSTQQLQHQAPQQQEMSDFRIAAATLNPPPESVKPVKPAAAVQPMPQMTAQQVPAHGAQETPILKSSELSSSASTSSSITELSDPSKFQLGVGNVQKLEKRMLHQSFRNQGPPPPMNQSDPLNQIDAFSSFMTPRHQ
Protein: CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B) (P21272)
Organism: Rattus norvegicus (Rat)
Function: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA (By similarity). Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (By similarity). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P17676}. Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033}.
Interaction partners:
- PR/SET domain 16.
- CCAAT/enhancer-binding protein alpha
- DNA damage-inducible transcript 3 protein
- CCAAT/enhancer-binding protein gamma
- Histone deacetylase 1
- Mitogen-activated protein kinase 14
- Cyclic AMP-dependent transcription factor ATF-4
- Runt-related transcription factor 2
- mitogen-activated protein kinase
- CCAAT/enhancer-binding protein delta
Sequence:
MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAAADFAAPAPAHHDFLSDLFADDYGAKPSKKPSDYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKAVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC
Protein: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.9) (Q7T2C2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
Interaction partners:
Sequence:
MLLRKVTSPAICSSVLRLQPAITGAQRQSGALVGVQNVRLYASQTAEAVLDKNVVSRDTTATAETVDKAVVSVESKSFAVNMFKGQISTSQVFPYPSVLNEEQSQFLRELVGPCSKFFEEVNDPMKNDALEKVEEHTLQGLKEMGAFGLQVPADLGGVGLTNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGNPQQKEKYLPKLATGENIAAFCLTEPASGSDAASIKTTAVRSPCGQYYTMNGSKIWISNGGTAEIFTVFAKTPVKDEKTGEMKDKITAFIVERSFGGVSSGPPEKKMGIKASNTAEVYFENVRVPADCVLGEVGGGFKVAMNILNNGRFGMAAALSGTMKGVITKAVDHAANRTQFGNKIHNYGAIQEKMARMAMLQYVTESMAYMVSGNMDSGATEFQIEAAISKIFASEAAWLVTDECIQVMGGMGFMKDAGVERVLRDLRIFRIFEGTNDILRLFVALNGFQNAGNQLKSLQKALKNPLGNAGMLAGEITKRAKRRAGLGSGLTLQGTVHPELNHSGELTVKAIEQFGAVIEELLLKHGKKIIDEQFVLKRVADCAIDLYAMVVVLSRASRSLNQGHSSAQHEKMLCETWCTEAHERVMQDIKFLRSGTSKQTFKNLRAISAAVVENGGVVAPHPLGF
Protein: Rhoptry-associated protein 2 (Q8I484)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGLKFYVLVFLILCLKNVVKGDKCETEFSKLYPESNSLTGLIYAHTANVHKLSMWVYFIYNHFSSADELIKYLEKTNINTLENSDHTCFARAVTLYLFYYYLKDIKSMLSTDDYQSFFKNKFKDINPLFINDFILILNDKKFMENLDLYIMKESEREHLVIKKNPFLRVLNKASTTTHATYKSNPYFIVGSRVHTPYKDYLGDFNKYTEISVLNYVRDYNFLIYAGSRENYYNSDIAGPARSVNNVISKNKTLGLRKRSSSLALVGTNNNDPIFAYCEKDNKSEYYGTPDDLITSFFSIIKTKMLNSHKTFLRQFDYALFHKTYSIPNLKGFRFLKHLFQKKNLVNFVGMYENHVSTEINFLAEDFVELFDVTMDCYSRQYSNRAAENFKAIRELNVL
Protein: LD25378p (Minidiscs) (Minidiscs, isoform C) (Minidiscs, isoform D) (Q9Y1A7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- alpha-glucosidase
- Amino acid transporter protein JHI-21
- GH08870p
- Amino acid transporter
- Amino acid transporter
Sequence:
MARVQASDSLIPRQVFEVPPAEPNNSTADSGSQGSGVKLKKQIGLLDGVAIIVGVIVGSGIFVSPKGVLKFSGSIGQSLIVWVLSGVLSMVGALCYAELGTMIPKSGGDYAYIGTAFGPLPAFLYLWVALLILVPTGNAITALTFAIYLLKPFWPSCDAPIEAVQLLAAAMICVLTLINCYNVKWVTRVTDIFTGTKVVALLVIVGAGVWWLFDGNTEHWDNPFSGGLQDPGYIALAFYSGLFSYSGWNYLNFVTEELKDPYRNLPKAICISMPVVTVIYMITNIAYFSVLSPDEILSSDAVAVTFGDKMLGYMSWIMPFAVACSTFGSLNGAIFASSRLFFVGARNGHLPAAISLINVNCLTPVPSLIFLGVLTLLLLFIEDVYVLINYVSYVEALFTLISVSGLLWMRYKQPKTERPIKVNLALPIIYLIVCLFLVIFSCTQTPYVVGIGTIIILSGIPVYYLTIHKPVKWLADTSQAINLWCSKFFICMPNQEKFD
Protein: Down syndrome cell adhesion molecule 1, isoform BD (Q0E9K1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVNQFYEAEIMTEYVIRGNAAVLKCSIPSFVADFVRVESWIDDEGNVLSFSDNYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGRVSPKFPNTLTSSSFTGDEGSSQTLLCPAQAYPAPLFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKLAPLPVNSPLYVGDYYQLTCAVVHGDAPFNITWYYNNEPAGDLAGVTILMHGRRSSSLNIESVGGDHAGNYTCKGANRAGETTAETHLSVKVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: von Willebrand factor A domain containing 3B (H0YEM4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKTAFADKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGEFHFYNFGCKDPTPPEAVQNEDLTLLVKEMEQGHSDLEKMQDLYSESLIMDWWYNAEKDGDSKHQKEICSMISTPEKCAKPQSDVDSTQTSSLNMLKGPWGLSDQKVQKKKVLHAESTKTSLLRSQMSSLRSSACSERKDGLSNASSRRTALSDKEMSILLAEEWLDDKSSEKVTREGSQVYDHDSSDVSSENWLKTYGLVAKKLTLMDALSVAAVPHSSTYVPVLDKHVVSKVFDEVFPLAHVCNDTNKMTLINPQGAKLNIYKRKVEQAIQSYEKRLNKIVWRALSQEEKEKLDANKPIQYLENKTVLNQALERLNWPISLKELSMLESEILAGKMYIQQAMELQEAAKKNYANKAPGEQQKLQGNPTKKTKSKRPDPLKGQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMPCPLLQVGDYVFAKIVIPKGFDFYVPAIVIALPNKHVATEKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHIKSPPIPEDPEVEDVEARNSAFLFWPLKEADTQDSREPRREKPRRKKRPAKQPLQQAAPSDSDGSSHGISSHGSCQGTHPEPRVWVMGGEHNIAYLRNTLKSLSRIVHLTSSFRFWACLGSSAAKTLTSLSNAELCFPRQPTSTSPRPGV
Protein: NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (54 kDa vimentin-interacting protein) (VIP54) (90 kDa SH3 protein interacting with Nck) (AF3p21) (Dia-interacting protein 1) (DIP-1) (Diaphanous protein-interacting protein) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-interacting protein) (Q9NZQ3)
Organism: Homo sapiens (Human)
Function: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis.
Subcellular location: Nucleus. Note=Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes.
Interaction partners:
- SH2/SH3 adapter protein NCK1
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 3
- Actin-related protein 2
- Actin nucleation-promoting factor WAS
- Actin-related protein 2/3 complex subunit 1B
- BAR/IMD domain-containing adapter protein 2
Sequence:
MYRALYAFRSAEPNALAFAAGETFLVLERSSAHWWLAARARSGETGYVPPAYLRRLQGLEQDVLQAIDRAIEAVHNTAMRDGGKYSLEQRGVLQKLIHHRKETLSRRGPSASSVAVMTSSTSDHHLDAAAARQPNGVCRAGFERQHSLPSSEHLGADGGLYQIPLPSSQIPPQPRRAAPTTPPPPVKRRDREALMASGSGGHNTMPSGGNSVSSGSSVSSTSLDTLYTSSSPSEPGSSCSPTPPPVPRRGTHTTVSQVQPPPSKASAPEPPAEEEVATGTTSASDDLEALGTLSLGTTEEKAAAEAAVPRTIGAELMELVRRNTGLSHELCRVAIGIIVGHIQASVPASSPVMEQVLLSLVEGKDLSMALPSGQVCHDQQRLEVIFADLARRKDDAQQRSWALYEDEGVIRCYLEELLHILTDADPEVCKKMCKRNEFESVLALVAYYQMEHRASLRLLLLKCFGAMCSLDAAIISTLVSSVLPVELARDMQTDTQDHQKLCYSALILAMVFSMGEAVPYAHYEHLGTPFAQFLLNIVEDGLPLDTTEQLPDLCVNLLLALNLHLPAADQNVIMAALSKHANVKIFSEKLLLLLNRGDDPVRIFKHEPQPPHSVLKFLQDVFGSPATAAIFYHTDMMALIDITVRHIADLSPGDKLRMEYLSLMHAIVRTTPYLQHRHRLPDLQAILRRILNEEETSPQCQMDRMIVREMCKEFLVLGEAPS
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2-1) (OGDC-E2-1) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1) (E2K-1) (Q9FLQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Biotin/lipoate A/B protein ligase family
Sequence:
MMLRAVFRRASIRGSSSASGLGKSLQSSRVAVSAQFHSVSATETLVPRGNHAHSFHHRSCPGCPDCSRTIINGYQGTALQRWVRPFSSDSGDVVEAVVPHMGESITDGTLAAFLKKPGDRVEADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGNKVARISTSADAVSHVAPSEKAPEKPAPKPSPPAEKPKVESTKVAEKPKAPSPPPPPPSKQSAKEPQLPPKDRERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFLEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRDADKMNFADIEKTINGLAKKATEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVQRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRIKDVVEDPQRLLLDI