wanglab/gogpt-training-data huggingface dataset:
Protein: TSC complex subunit 2 (A0A2R8YDZ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKSRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTVASFSSLYQSSCQGQLHRSVSWADSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESQSFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV
Protein: ER lumen protein-retaining receptor (Q76NM1)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi (By similarity).
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MNIFRLIGDILHLVSMYILIMKLKKSKNCIGISCRMQELYLIVFLCRYIDLFFVFVSFYNTVMKITFILTIAYTIYLIRLKLPISQTYNRKVDNFKSEKYLIPPCLVLSLLTCKTYNLYNILWSFSIWLESVAILPQLVLLEKQREVENITSHYVITMGLYRAFYILNWIYRYFFDDKPYINVVGWIGGLIQTLLYIDFFYYFALAKWYGKKLVLPFNGEV
Protein: Melanocortin receptor 5 (MC5-R) (P35345)
Organism: Rattus norvegicus (Rat)
Function: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-opiomelanocortin
- Melanocortin 2 receptor accessory protein 2
- Agouti-related protein
Sequence:
MNSSSHLTLLDLTLNASEDNILGQNVNNKSSACEDMGIAVEVFLTLGLVSLLENILVIGAIVKNKNLHSPMYFFVGSLAVADMLVSMSNAWETITIYLINNKHVVIADTFVRHIDNVFDSMICISVVASMCSLLAIAVDRYITIFYALRYHHIMTARRSGVIIACIWTFCISCGIVFIIYYESKYVIVCLISMFFTMLFFMVSLYIHMFLLARNHVKRIAASPRYNSVRQRASMKGAITLTMLLGIFIVCWSPFFLHLILMISCPQNVYCACFMSYFNMYLILIMCNSVIDPLIYALRSQEMRRTFKEIICCHGFRRTCTLLGRY
Protein: Bone morphogenetic protein 4 (BMP-4) (Bone morphogenetic protein 2B) (BMP-2B) (P12644)
Organism: Homo sapiens (Human)
Function: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis. Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction (By similarity). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt, or SRC cascades. For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein receptor type-2
- Chordin
- Bone morphogenetic protein receptor type-1B
- Noggin
- Activin receptor type-1
- Activin receptor type-2A
- Activin receptor type-2B
- Bone morphogenetic protein 7
- Bone morphogenetic protein 2
Sequence:
MIPGNRMLMVVLLCQVLLGGASHASLIPETGKKKVAEIQGHAGGRRSGQSHELLRDFEATLLQMFGLRRRPQPSKSAVIPDYMRDLYRLQSGEEEEEQIHSTGLEYPERPASRANTVRSFHHEEHLENIPGTSENSAFRFLFNLSSIPENEVISSAELRLFREQVDQGPDWERGFHRINIYEVMKPPAEVVPGHLITRLLDTRLVHHNVTRWETFDVSPAVLRWTREKQPNYGLAIEVTHLHQTRTHQGQHVRISRSLPQGSGNWAQLRPLLVTFGHDGRGHALTRRRRAKRSPKHHSQRARKKNKNCRRHSLYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR
Protein: LD42783p (Q95TL1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLFDWLRINPEILIGCYHSNPEFVHKIMKLLNYCNIDIFTRKVYFERDLLTTANVRDSLVELFDVRANVPLTEDFAFKNFDIFQSTQITLDWETIIRERVTPQEESILRIFKMVDFGFFICKQKKFNYRFCVKTRRFTETQKKKQREEKKGGGSRRRERRTAPKTNRTKRNEGRTRRYSDRKNGIVRKSYTSNEEKDTVEECRKMPRKGYLRNRNAEKAAAVITSATGTSVAGGTSASTTTNSVIEKLNLQSSSGADEERSEAKSKKCELMGKLWLQNEVETLEEELRDSPAHVVMSPFVVVDSKALTEYNGIVKSLVRTKKCIVLIPNAVLNELDDLKKRSENVRHVIRWLEQEFKQGNRHLRAQRDNESQPLSLLKISRKMDRDASVFLQIAQFCNHLVANHADPHVSELQKSVVTYLSGDNLHEKNRQQQNFSYTGILDSIPVRYAQIQSFYAKFKANKK
Protein: Lycopene beta/epsilon cyclase protein (Q0WVA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Beta carbonic anhydrase 5, chloroplastic
- Dol-P-Glc:Glc
- Enhancer of polycomb-like protein
- Receptor protein kinase-like protein At4g34220
- TRF-like 3
Sequence:
MVVLQIHQFNGFVSSVSRAQTNQGRRRASTTVCVQTQLAPSLTQKIMESISVGGEAGGAGGAYSYNALKRLDNIWSNICTQPTGPQETQQIVSRVSGFSQDYSMGNNLVGTFDIVVCGGTLGIFLATALCAKGLRVAVVERNAIKGRDQEWNISRKEMKELTEVRVLTEDEIEEVIAAKFNPNRCGFENLGDIWVEDILNLGVSPAKLVETVKQRFISLGGVILEDSSLSSIVIYNDLAVMQLSKGDTLSSRLVIDAMGNFSPILKQIKRGRKPDGMCLVVGSCAHGFKENSSSDVIYSSSSVTRVADSNVQLFWEAFPAGSGPLDRTTYMFTYTEPQSTSPSLEDLLEEYWKLMPKYQGVSLDELEILRVVYGIFPTYRNSPLPAAFDRVLQFGDASGIQSPVSFGGFGSLTRHLGRLSNGIYDAIDGDLLDSDSLSKLNPYMPNLSASWLFQRAMSAKQQLDVSRGFTNELLHVNFSCMQRLGDPVLRPFLQDIIQFGPLAKTLGLVMLTKPQIIPSIFRQVGIPVLLDWSVHFFMLGLYTLLSAYIDPLLRPSLEGLPSKTRFEWKRCLEAWKYGAGLDYEL
Protein: Ribosomal protein S3A (D6RAS7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVR
Protein: Lipid phosphate phosphatase 2 (AtLPP2) (EC 3.1.3.-) (Phosphatidic acid phosphatase 2) (AtPAP2) (Prenyl diphosphate phosphatase) (Q9XI60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a general 'housekeeping role' in lipid metabolism. Exhibits both diacylglycerol pyrophosphate (DGPP) phosphatase and phosphatidate (PA) phosphatase activities with no preference for either substrate. May play a role downstream of the ABA signaling pathway during seed germination and in stomatal movement in leaves.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidate phosphatase PAH1
- Phosphatidate phosphatase PAH2
- Diacylglycerol O-acyltransferase 2
- Phospholipid:diacylglycerol acyltransferase 1
- Choline/ethanolaminephosphotransferase 2
- Choline/ethanolaminephosphotransferase 1
- Diacylglycerol O-acyltransferase 1
- Putative phospholipid:diacylglycerol acyltransferase 2
- Diacylglycerol O-acyltransferase 3
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
Sequence:
MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPFAVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFHNVTKNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQFFPPPYDPDGWGPHAYFQMLADSRNDVQDSAGMNHLSVRQTELESVR
Protein: Histone H2B (Q389S0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000451}.
Interaction partners:
- Histone H2A
- Histone H3 variant
- Histone H3, putative
- Histone H4
- Histone H4
- Histone H2A
- Cell division control protein 73 C-terminal domain-containing protein
- SET domain-containing protein
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MATPKSTPAKTHKEAKKTRRQRKRTWNVYVSRSLRSINNQMSMTSRTMKIVNSFVNDLFERIAAEAATIVRVNRKRTLGARELQTAVRLVLPADLAKHAMAEGTKAVSHASS
Protein: Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase beta (EC 3.1.4.35) (EC 3.1.4.53) (Q8I6Z7)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively. By regulating cAMP levels during the asexual blood stage and, thus PKA activation, required for merozoite invasion of erythrocytes and for the parasite development immediately following invasion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30794532, ECO:0000305|PubMed:18590734}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30794532}; Multi-pass membrane protein {ECO:0000255}. Note=In early schizonts, localizes to the endoplasmic reticulum (PubMed:30794532). Transported to an apical location and then subsequently discharged to the plasma membrane of merozoites within mature schizont (PubMed:30794532). {ECO:0000269|PubMed:30794532}.
Interaction partners:
- cGMP-specific 3',5'-cyclic phosphodiesterase delta
- AMP deaminase
- cGMP-specific 3',5'-cyclic phosphodiesterase alpha
- Inosine triphosphate pyrophosphatase
- Adenylate kinase 1
- GTP:AMP phosphotransferase
- Adenylate kinase 2
- Adenylosuccinate lyase
- Guanylate cyclase beta
- Hypoxanthine phosphoribosyltransferase
Sequence:
MGKVEDFEEHNKNSNQDIEKNVGNRRRSNSNTINDQNENINKNKAIVTKKSFIMNLLRNKEKTKVEQNDDNIVENMNERKNSLKDMSLISDNVEKDNKVKKKNSYLKNLNILGKTKSIEFSFPSNILNNARKNIQEIDEESPLTSNSLRTYKEGISEDNRQNQRNADNNSLNWSTSNINTECNSEFSNIEVKVLKTEKSNSVKLKDNIIDIPNDKNKKELQEINIKNTNKDSYKNLYLKVRNSISFNDNIKIDDENKNDKNNIIDNYNNYDDINSSNEITIDGLNHDDNIKKIDNINNFDNKHDDNLQDHHQNHVHHTFRSSRKSLGNIKSNNTNIKLNNDKNFDTNINKRSILEKYFYDIWKRNITIKKEIYSLSSKNPPNPLKSTFADACQNESSEKELLKKIPLKFNDDSIESLYVLNLNNWISSRMIIIGIVMLILSFIIWPLTTWSLKTSTWGRETYIIILFHTLMAINTLILIFFIIIGSTELCKYSECMSYVLFSLMVALWGLWNIAIGLTLEYNPNLSEMPTTTYELEMIYVLTYIYGFLPLVIIDIFFPSRTKYNWIIHLIFIFLNSSSIILVGSAKPDFVPEIYVVFRILAYTTLCIFLYIGSYTSELQIRYVFYNLLVAGYKLDKIESDMKNKTSNKKISTGIEDLINMLKECTKVILELENETDTNFNVHTKTSYCSNILEQCLSTLTKSDNLYNIDYNVLENPENKKFIEAYVSKSKSNFAGEEVPKGVDFKLNKSFSNNDCISTDKVDLDKKQIKKFLKQINISQLTKMIQFIDNKLLSDWDFNCLTYFDESEYPFFDINLSLICTIDHNIPINIIINFLCFVEKQYNNVPYHNTIHATMVTQKFFCLAKKLGIYDDLEYKIKLVMFISGICHDIGHPGYNNLFFVNSLHPLSIIYNDISVLENYHASITFKILQLNQCNILKNFSEKDFRMMRSYIIELILSTDMKHHFEIISKFRIRRENEDFDYIKNSDDLLILTKMIIKSADISHGSVSWSEHYCWCQRVLSEFYTQGDEELKNKMPLSPLCDRTKHNEVCKSQITFLKFVVMPLFEELSHIDNNKFIKSFCLKRLNSNCIMWDTLMKEEKTIEVYDPAAVKLKDKKKKKVDKKKKSYIDLTLFFIKNVSD
Protein: Potassium voltage-gated channel subfamily C member 3a (Potassium voltage-gated channel, Shaw-related subfamily, member 3a) (Voltage-gated potassium channel Kv3.3a variant 2) (E1AZA5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLSSVCVSSFKGRKGGNKSSNKACYSADMTCPSDSEKIVINCGGIRHETYRSTLKTLPGTRLSWLTEPDAFSNFDYDPKSDEFFFDRHPNTFAFILNYYRTGKLHCPSDVCGPLFEEELAFWGIDETDVEACCWMNYRQHRDAEEALDSFETPEPDPPEDDPALTGGADGDLKRLCLQEDGRNPSRWSTWQPWVWALFEDPYSSKYARYVAFGSLLFILISISTFCLETHEAFNTIYNKTENVTVGNVTREEVVFEVVTDNWLTYVEGVCVVWFTIEVFTRVIFCPDKAEFFKSSLNIIDFVAILPFYLEMALSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGADPDDPTASAHTAFKNIPIGFWWAVVTMTTLGYGDMYPETWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKNKHIPRAPQPGSPNYCKPDALAMATASPHRIMGNVLGSMVVSGSMAGDCPLAQEEIIEINRADSKQNGDAANAALANEDCPTIDQVLGPDDRSPATGGLGTGTGRERYPHDRACFLLSTGEFRTTDSNVRKAAGYEKSRSLNNISGMTGAPLRLTPITPINNPPYEPYESPGPLRRCRSPIPSIL
Protein: Flagellar L-ring protein (Basal body L-ring protein) (P0A6S0)
Organism: Escherichia coli (strain K12)
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular location: Cell outer membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar basal-body rod protein FlgF
- Flagellar hook protein FlgE
- Flagellar hook-associated protein 3
- Flagellar M-ring protein
- Flagellar basal-body rod protein FlgC
- Flagellar P-ring protein
- Flagellar basal-body rod protein FlgG
- Flagellar hook-associated protein 1
- Peptidoglycan hydrolase FlgJ
- Flagellar motor switch protein FliM
Sequence:
MQKNAAHTYAISSLLVLSLTGCAWIPSTPLVQGATSAQPVPGPTPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTNFGFDTVPRYLQGLFGNARADVEASGGNTFNGKGGANASNTFSGTLTVTVDQVLVNGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNTVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM
Protein: Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (EC 3.2.2.6) (X-linked interleukin-1 receptor accessory protein-like 1) (P59823)
Organism: Mus musculus (Mouse)
Function: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK (By similarity). Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans-synaptically binding to PTPRD.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, axon {ECO:0000269|PubMed:21940441}. Cell projection, dendrite {ECO:0000269|PubMed:21940441}. Note=May localize to the cell body and growth cones of dendrite-like processes.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Interleukin-1 family member 10
- Neuronal calcium sensor 1
- Receptor-type tyrosine-protein phosphatase S
- Leucine-rich repeat and fibronectin type-III domain-containing protein 4
- Leucine-rich repeat-containing protein 4B
- Stress-activated protein kinase JNK
- SLIT and NTRK-like protein 3
- SLIT and NTRK-like protein 1
- NT-3 growth factor receptor
Sequence:
MKAPIPHLILLYATFTQSLKVVTKRGSADGCTDWSVDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLTVGENDTGLCYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKAWRPSIVFKRDTLLIKEVKEDDIGNYTCELKYGGFVVRRTTELTVTAPLTDKPPKLLYPMESKLTVQETQLGGSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSCYVENGNGRRHASVLLHKRELMYTVELAGGLGAILLLLICSVTIYKCYKIEIMLFYRNHFGAEELDGDNKDYDAYLSYTKVDPDQWNQETGEEERFALEILPDMLEKHYGYKLFIPDRDLIPTGNIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVTGEIKVILIECSELRGIMNYQEVEALKHTIKLLTVIKWHGPKCNKLNSKFWKRLQYEMPFKRIEPITHEQALDVSEQGPFGELQTVSAISMAAATSTALATAHPDLRSTFHNTYHSQMRQKHYYRSYEYDVPPTGTLPLTSIGNQHTYCNIPMTLINGQRPQTKSNREPNPDEAHTNSAILPLLPRETSISSVIW
Protein: B-cell lymphoma/leukemia 11B (BCL-11B) (B-cell CLL/lymphoma 11B) (COUP-TF-interacting protein 2) (Radiation-induced tumor suppressor gene 1 protein) (mRit1) (Q99PV8)
Organism: Mus musculus (Mouse)
Function: Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals. Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of receptors CCR7 and CCR9, which direct the movement of progenitor cells from the bone marrow to the thymus (By similarity). Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4(+) T-lymphocytes. Tumor-suppressor protein involved in T-cell lymphomas. May function on the P53-signaling pathway. Repress transcription through direct, TFCOUP2-independent binding to a GC-rich response element.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- COUP transcription factor 1
- BCL11 transcription factor A
- B-cell CLL/lymphoma 7 protein family member A
- SWI/SNF complex subunit SMARCC2
- Actin-like protein 6B
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- Actin-like protein 6A
- AT-rich interactive domain-containing protein 1A
- SWI/SNF complex subunit SMARCC1
Sequence:
MSRRKQGNPQHLSQRELITPEADHVEATILEEDEGLEIEEPSSLGLMVGGPDPDLLTCGQCQMNFPLGDILVFIEHKKKQCGGLGPCYDKVLDKSSPPPSSRSELRRVSEPVEIGIQVTPDEDDHLLSPTKGICPKQENIAGPCRPAQLPSMAPIAASSSHPPTSVITSPLRALGVLPPCFPLPCCGARPISGDGTQGEGQMEAPFGCQCELSGKDEPSSYICTTCKQPFNSAWFLLQHAQNTHGFRIYLEPGPASTSLTPRLTIPPPLGPETVAQSPLMNFLGDSNPFNLLRMTGPILRDHPGFGEGRLPGTPPLFSPPPRHHLDPHRLSAEEMGLVAQHPSAFDRVMRLNPMAIDSPAMDFSRRLRELAGNSSTPPPVSPGRGNPMHRLLNPFQPSPKSPFLSTPPLPPMPAGTPPPQPPAKSKSCEFCGKTFKFQSNLIVHRRSHTGEKPYKCQLCDHACSQASKLKRHMKTHMHKAGSLAGRSDDGLSAASSPEPGTSELPGDLKAADGDFRHHESDPSLGPEPEDDEDEEEEEEELLLENESRPESSFSMDSELGRGRENGGGVPPGVAGAGAAAAALADEKALALGKVMEDAGLGALPQYGEKRGAFLKRAGDTGDAGAVGCGDAGAPGAVNGRGGAFAPGAEPFPALFPRKPAPLPSPGLGGPALHAAKRIKVEKDLELPPAALIPSENVYSQWLVGYAASRHFMKDPFLGFTDARQSPFATSSEHSSENGSLRFSTPPGDLLDGGLSGRSGTASGGSTPHLGGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQIGKEVYRCDICQMPFSVYSTLEKHMKKWHGEHLLTNDVKIEQAERS
Protein: Trafficking protein particle complex subunit (Q9VLI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU366065}. Golgi apparatus, cis-Golgi network {ECO:0000256|RuleBase:RU366065}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- FI18195p1
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit
- Probable trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 11
- Protein brunelleschi
- Trafficking protein particle complex subunit 10
Sequence:
MIIYGVYIVSKSGGLIFNLDNNVPRIEHEKTFTYPLDLVLDYDSKKVSVSFNRKDGINVGHVLVAVNGMPVNGVTLDDGRDVRTTLDAPENYPINLKFSRPKMTTNEKIFLASMFYPLFAIASQLSPEPKSSGIEILEADTFTLHCFQTLTGIKFIIISETGLNGIDLLLRKVYELYSDYVLKNPFYSLEMPIRCELFDNKLQELLAQVEKTGISNIDK
Protein: PML nuclear body scaffold (A0A0D9RNP7)
Organism: Chlorocebus sabaeus (Green monkey) (Simia sabaea)
Interaction partners:
- Retinoic acid receptor alpha
- Small ubiquitin-related modifier
- Death domain-associated protein 6
- SUMO-conjugating enzyme UBC9
- Uncharacterized protein
- Cellular tumor antigen p53
- SP100 nuclear antigen
- E3 ubiquitin-protein ligase RNF4
- Potassium channel tetramerization domain containing 2
Sequence:
MEPAPARSPRPQQDPARPHAPTMPPPETPSEGRQPSPSHSPTEQAPSPEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEESGLQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCIRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSGHSELKCDIRAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRARVRQMVAHLQAQERELLEAVDARYQRDYKEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHSFLRQALCHLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGTDADVSKKASPEAASTPRDPTDVDLPEEAERVKAQAQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCIQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPNPRSPVIGSEVFPPNSNHVASGTGEAEERIVVISSSEDSDAENSCTEPMETAEPQSSPAHSSPAQSLLRAQGASSLPRGTHHPPAWPPRQPTEQAAVPNAEPHSQPPDHQEHPAVHRGIRYLLYRAQRAIRLRHALRLHPRLHRVPTRAWTPHVVQASTPATTGPLNHLANAQEHPAQLQRGICPPCRIRGTVRSRSRSLRGSSYLSQWLNHFFSLPLSSMNSQLNNSSMVGAGGGRAQTLGTGVSPGDSVRGAMEASQVQVPLEASPVTFPPPCPPERPPISPVPGARQAGL
Protein: Uncharacterized protein (A0A1D8PKU6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MCCILEIFAVTGSYDNKKYLTDTYLINFHIDSLDLTKLIDSSRITKRDGVGSKMVSINPRQGTPTKRAPAESGWYYVPGGSNTQSGPSATASSGGNAVASGSAINWWSPVESGSATSSGSGSGSTSSGSSGSDSSNSGSTSGGYYTTVSQAVHSLLSNVNPQVLGMAQVYSVGFWGYCRGYVIQDDSKKTKKFDNSNVNYTWCSEPKVSFFFNPVEIFKKEMNNTLYGIQVDSQAAGIGQLSYTQKSELKVLIDHLDIDELNLPGNINGKLQQLHNLTNASFGLLMAVAVLSFVSVLIQMLAFCFSPEKCCLSFLNFLFECIIGLIAFVGAVVVTATYSYVKAQVNGNSDTFGVKSFLSINFYAFVWSAVIVCILVVFFNLLGHCCGLFGTRRHYRTVRNPQPDAEQHKEETESD
Protein: Beta-galactosidase BoGH2A (Beta-gal) (EC 3.2.1.23) (Glycosyl hydrolase family protein 2A) (BoGH2A) (A7LXS9)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides in xyloglucan degradation, converting 'L' units to 'X' units.
Subcellular location: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Cell inner membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
Interaction partners:
Sequence:
MMIGKLKYLMLGGCLILGSCLALGGCLMLLGACSSSSLVSPRERSDFNADWRFHLGDGLQAAQPGFADNDWRVLDLPHDWAIEGDFSQENPSGTGGGALPGGVGWYRKTFSVDKADAGKIFRIEFDGVYMNSEVFINGVSLGVRPYGYISFSYDLTPYLKWDEPNVLAVRVDNAEQPNSRWYSGCGIYRNVWLSKTGPIHVGGWGTYVTTSSVDEKQAVLNLATTLVNESDTNENVTVCSSLQDAEGREVAETRSSGEAEAGKEVVFTQQLTVKQPQLWDIDTPYLYTLVTKVMRNEECMDRYTTPVGIRTFSLDARKGFTLNGRQTKINGVCMHHDLGCLGAAVNTRAIERHLQILKEMGCNGIRCSHNPPAPELLDLCDRMGFIVMDEAFDMWRKKKTAHDYARYFNEWHERDLNDFILRDRNHPSVFMWSIGNEVLEQWSDAKADTLSLEEANLILNFGHSSEMLAKEGEESVNSLLTKKLVSFVKGLDPTRPVTAGCNEPNSGNHLFRSGVLDVIGYNYHNKDIPNVPANFPDKPFIITESNSALMTRGYYRMPSDRMFIWPKRWDKSFADSTFACSSYENCHVPWGNTHEESLKLVRDNDFISGQYVWTGFDYIGEPTPYGWPARSSYFGIVDLAGFPKDVYYLYQSEWTDKQVLHLFPHWNWTPGQEIDMWCYYNQADEVELFVNGKSQGVKRKDLDNLHVAWRVKFEPGTVKVIARESGKVVAEKEICTAGKPAEIRLTPDRSILTADGKDLCFVTVEVLDEKGNLCPDADNLVNFTVQGNGFIAGVDNGNPVSMERFKDEKRKAFYGKCLVVIQNDGKPGKAKLTATSEGLRQAVLKISAEEL
Protein: Girdin, isoform C (M9PDY5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAGTATATPMEIDEFVNSSIISWLESCLPRAELLAGYTSLLDGHIIHSVWLQIDPEPQNNPSELNDLNGKSLSIARAKNFECVVRNLKSFFEEELGQTILVLPDAFTLGHHPESKNGLEQMKTLLTLLLGAAVQCPNKELFIARIKELDLETQHAIVGLIKQVTDSHSLVLTEDSLERLTPQSMYTHILRLTKERDVMYLKWIDLACVETEMTASDNLVECGQGVSVTRSPSNGTATSTPSSSSNSESNHLAVECADLRSKNRKLRQELEEKSENLLELREELDDKKARFDKLRQESQEWFTEAKRASAYRDEVDILRERAERADRLEVEVQKYREKLGDSDFYKSRVEELREDNRVLLESKEMLEEQLQRYRKRSEHAISLESEIIKYKQKINDMALERDVDRSKLEELLEENSQLQLVARNLNSTMDLDKSFSENEDDCNSGDNSLSEQLTNNAQTRALKLELENRRLTAALEQLKESSFHESTSKMLELEKEKKKLSLKIEQMQENINRLTQQNVELEGVFKNALEENKKLQDAVDNRQKSYDRQSLEREADRQKLSDAEQHVETLNKEKQRIQTLNESIQRRADDLERLAESKTKELEQYLEKSRQYELTKQKLYEIEARVSTYERENASLLKEVSKLKEGSEQKSVQLDDSINRLDVQSKELQKLGKALEDSEQVHQKLVELEKQNQELASQRIIDQEMISTLRNDLVTGTLVTKKVRNNLEKLGLADEEPGELNVEHVVEKLVRNPETFKTVREIMLNVTREQLEEEEREGGVKSDMCVLCHRQEIFTVEKNIELAATPAPAPAQPSSQELRFEHKVRLSPARESAELTRIKDSNTQLQTENARLSVDVAALGSQITSLNTQHVALQLANSQLAAEKDSLLKEIDSLQQEHKHALQDQVTLQCLHDQLSAEYESLNKDKEQLKAAVRDLRQELRDTREQQSALEQRIEELTIQNSNMKTCSEDLSILRTEHSKLTDDFRNLFATSDRFKNEYKNIQEQYKMVRMEHSSLKLQNTELSGELNAKSDQVRCLQMEYSKVQQRCEMLIQNNAELDSERKALMDNVSQLLSQYQELLAISLEDKKHFHEEEKNYTERVHSLKRQKEKLEEKIMEHYKKSETTVHKKKPFASMLVRRVKKASSDLMNKVPSRNRRSWVDDARTNSQFVIGSESGGNESDNSNEEPLSIASDTHLLQRNVPLRQSLQRDLLDNSIQRGGAVRSSLQAQKRTDLNNSRRNSVHGLEAPDVTGSSLTLGTAGSRRTVYLIDEHQKLPDGSTPGATQSQSVGGSGSVNAAPPTPAEPQTPQKSTENNAPVGPATFLMYNRINTTIGGASNSGDQSPLLQASGSVSGTTMQDDKSARKRTEDKSNSIWYEYGCV