wanglab/gogpt-training-data huggingface dataset:
Protein: Myb-like protein X (mRNA, clone: RAFL24-22-E06) (Q67YL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKKTSTRSQRGSKGIKGKHVLQICVLLGVCIWLIYQVKYSHDKKKEFYEKDVEKSTVLLSEVEDGVVKLGRKDLLPKNYNQKENEKHVEEDEDEEEISHGGEEKEKKSKVENGNHEEEVEKDEEEEVAEDDEEDKNKQGEEVAEEDEEENKHEEDEIDEQDQSKNAGDTDKDDETLEEEKESGMSENDEKEKETNHADEIDMTVDEAREEHYKADDASSAVSHESRILNTEKLKESSNETAQENNPNGATSEVEIQKEPDLKLGEAENTNFVNKTTTDVKDGDSESSSSETKSAVTESQSETVNGNSTVALFEASEFVKNETEIMRDRSQGDGALPAGFSEPQPPVLELEKNRNESDPDIPISADITNKDFIQDESRNSTSESSLLENIAGSNTTEVNENSRSEGDDDESGEKESSNIFSTELTEEADNTSGTSISQEEMDALTDPQTLPDIRIEGNEEDEEEAIGAERKKL
Protein: VPS29 protein (Q8N0S8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVRAAVAATKAWLSGGVLRCWEPWGGRGRGIGKSRRPRRQGPGAGLGKAQKRSREGRERPPLGAAGLGLVSRPQGARGHPRGKKAPLAARPVTRHARPSQGRPLVLYLECSGDRGTVLRFQTVPTRFPQKAPPAGWGVVVEAGLSDAEQEVASRISYPFNFAI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VJ30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein numb
- Adaptor protein complex 2, mu subunit, isoform A
- AP-2 complex subunit alpha
- GH06923p
- Drebrin-like protein
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- RalA-binding protein 1
- AP complex subunit beta
- AP complex subunit sigma
Sequence:
MKKILSKFERNENSRLENPPNSSSSSSSNEKNSFVGKVFTVGRVTVTVEDVLAEGGFAMVFLARGNGGGSSSATKYALKRMYVNNEHDLNVAKREIQIASNLSGHKNIIGYVDSSITPTGNGVCEVLLLMPYCKHHMLAMMNARLHVGFTEPEVLNIFCDIAEAVSRLHYCQTPIIHRDLKVENILQTDAGNFVLCDFGSATAKTLNPQQHGVTVVQEEIQKYTTLSYRAPEMIDLYGGKSITTKADIWALGCMLYKLCFFSLPFGESTLAIQNGQFSIPDSSKYSKGMHQLIKYMLEPDMEKRPNIWQVCEVAFRLAGKDNPVQNLHKTPIPNFDLLVVPPFESEAKRISAAASKAAKAQNVSVVEAGTSVAPRSRPKGSSSVHGGNPLGLGLPPSPSPRQNITSPQPQPQPVVEQFQANFPAMPPAVPPPPQAVTPAAPAASKLFESSGYPDPFNEPAAAVIPTEFLPAAEEPNKEEVPQDLNVIAGTPTKSMLTPPKPSGGGGHRRNVSDTSAFNKTFANETSQFLAPFNNNLAAMGDGQQTLASAASNPGIYASSTANSAAVSISELMKPGQTAVEKRVEAWNPFEEEQPFSQMTEDHIFEAEFDKIRQRGSQGSITAKSASTTSTLTPTEQIPSAVVAPVTAAPGAVPPPPIAAAVSPYPSQVSEDPFGSAPFSLPPGLREKASSLRKTGAKFIGVSSGGTGGGVATPIGLVAGGANTATSSNSSKWMLSPTLEVSSEEKTSLISKLKTDSECGIPGAVGGAGEGVSGYVKLPVEDRNKYEKLRSKDQPTSDDSDSEASEFFQQDSDEGGGGIFRQMQMVTSNLPETIHKIQQVAYHKVDKTAHLPIVKKLRDKTKKPTTAAHQAAQQLNLMAAAVAAQAEEAAKAAESDGDSIGSASDLRAEDDDLFDENPRQTQAKQRRPLPTEMDGISESVKTCSSSAYHAECESVTTHEDDVRSRVVVKVRMRKKDRALVTATGDPSAPSEELSPTSSDLLHKFGDRPLLLDDELDYGSGESKSSTESPVAPILPTNPDVQESEEDVFALAPFKLPVGVPLKRKTKPKAKPKPSEPEMWTSTPVKSAAVGDPSTNFASFPAQLTPTNNVGNSAQLDEFNEPIFNPFQENAQNTQSGETNQCDLFGLEPFPQVIRTIEQNPQHHQIHQFPSHNNNNNVIKVPASVSVALPASVPVSVSVNSSAPQLVTINHSIIINKTPEPPMNYNNNNNNQTAKSSGTSSVYVNVPSFSSMSTSSCSINQPQSSPAAVIPVQAPLPVPVPAPVSVPAVPVPIPAVVTHLRPLLPIADNAYVQISQDRCSDFTPDDEEEPVVLRDADVVADGIGIPTPAKPKKEKSNLAVRVLPGKLTQKVKGHSYKKVSAAALGSTSSLSSGSKQKHQRLQYQSHDDDDDEQDQDENRGAGGGRNFQSNTIQNSAKTGFSNMSFEDFPSDQEMDRLSRTIPFEVVRNEKMLLEAEKKFGSLKRRNNLFS
Protein: CDK5 and ABL1 enzyme substrate 1 (Cables1) (A7YX81)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASALQMKPSSLEHTRKRVIDPRRRQAALSFLSNISLDGRPVQDDGDIQAEEEEDASRTRESLVCAVGQQALAAAANQALSTARAAGFMAGTVATSAAAAAPPPPDPDGDAQLLQSAFSSPFSAVPPATRGRLQTYTQGILPVSYARQSSQNYCCLEGGQIANSALELQRSRRRLISQRSSLETLEDIEENAPLRRCRTLSGSPRPKSFKKVHFIKNTRQHDMRNGRIVLISGRRSFYSVFSVLPYRDCSQTGDVKAESGRQRHPSGGMSAKEMVIGLEGVELGADGKTVSYAQFLYPTNVLGRRNTIDSTSSFSQSRNASHRSLILARANSNQSSLDTGNELGDFREYDPNLLDDPQWPCGKHKRVLIFPSYMTTVIEYVKPSDLKKDMNETFKEKFPHIRLTLSKIRSLKREIRKLTQEEFGYEESTVAMAFVYFEKLVLQGKLNKQNRKLCAGACVLLAAKIGGDLKKHEVKLLIDKLEERFRVNRRELIAFEFPVLVALEFNLHLPEHEVMPHYRRLLQNS
Protein: Protein YCF54, chloroplastic (Protein LOW CHLOROPHYLL ACCUMULATION) (Q9LVM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Tetrapyrrole-binding protein, chloroplastic
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Protein TAB2 homolog, chloroplastic
- At2g23670/F26B6.32
- Geranylgeranyl diphosphate reductase, chloroplastic
- Magnesium-chelatase subunit ChlD, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
Sequence:
MWSVTGALTVAVPPTAAACRTKPFLISSSFPKQTKKLHLSSPSLSLPSSHFSSSFKTAATSIEQQSSVNKGESTKYHFLVANAKFMLDEEEHFQEQLFERLRYFGERELVQDFWLVIEPKFLDNFPKITQRLRRPAVALVSTNGTWITFMKLRLDRVLYDSFEATSLDEALASNPTTLEFDKPKNWVAPYPKYEPGWWDTFLPKVTQESAV
Protein: Stage V sporulation protein T (P37554)
Organism: Bacillus subtilis (strain 168)
Function: Transcriptional factor that regulates positively or negatively the expression of a large number of forespore-specific sigma G-dependent genes. May provide a mechanism of feedback control that is important for forespore development. SpoVT levels during spore formation have a major impact on the germination and the resistance of the resultant spores.
Interaction partners:
- Stage III sporulation protein D
- RNA polymerase sigma-G factor
- Stage 0 sporulation protein A
- RNA polymerase sigma-F factor
- Stage II sporulation protein R
- Stage V sporulation protein AD
- Anti-sigma F factor
- Spore protein YabP
- Translocation-enhancing protein TepA
- Stage III sporulation protein AA
Sequence:
MKATGIVRRIDDLGRVVIPKEIRRTLRIREGDPLEIFVDRDGEVILKKYSPISELGDFAKEYADALYDSLGHSVLICDRDVYIAVSGSSKKDYLNKSISEMLERTMDQRSSVLESDAKSVQLVNGIDEDMNSYTVGPIVANGDPIGAVVIFSKDQTMGEVEHKAVETAAGFLARQMEQ
Protein: Peroxisomal coenzyme A diphosphatase NUDT7 (EC 3.6.1.-) (EC 3.6.1.77) (Nucleoside diphosphate-linked moiety X motif 7) (Nudix motif 7) (P0C024)
Organism: Homo sapiens (Human)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Cleaves CoA, CoA esters and oxidized CoA with similar efficiencies (By similarity). Preferentially hydrolyzes medium-chain acyl-CoAs and bile acid-CoAs (By similarity). Has no activity toward NDP-sugars, CDP-alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester (By similarity). May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand (By similarity). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:Q99P30}.
Interaction partners:
- Acyl-coenzyme A diphosphatase NUDT19
- NAD-capped RNA hydrolase NUDT12
Sequence:
MSRLGLPEEPVRNSLLDDAKARLRKYDIGGKYSHLPYNKYSVLLPLVAKEGKLHLLFTVRSEKLRRAPGEVCFPGGKRDPTDMDDAATALREAQEEVGLRPHQVEVVCCLVPCLIDTDTLITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGHRFINHIFEYTNPEDGVTYQIKGMTANLAVLVAFIILEKKPTFEVQFNLNDVLASSEELFLKVHKKATSRL
Protein: Urokinase plasminogen activator surface receptor (U-PAR) (uPAR) (Monocyte activation antigen Mo3) (CD antigen CD87) (Q03405)
Organism: Homo sapiens (Human)
Function: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12376466}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:12376466}. Note=Colocalized with FAP (seprase) preferentially at the cell surface of invadopodia membrane in a cytoskeleton-, integrin- and vitronectin-dependent manner. {ECO:0000269|PubMed:12376466}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15677461}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P49616}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000250|UniProtKB:P49616}.
Interaction partners:
- Urokinase-type plasminogen activator
- Vitronectin
- Plasminogen activator inhibitor 1
- Plasminogen
- Plasminogen activator inhibitor 2
- Epidermal growth factor receptor
- Sushi repeat-containing protein SRPX2
- Integrin beta-2
- C-type mannose receptor 2
- Integrin alpha-M
Sequence:
MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT
Protein: Molybdate-binding protein MolA (Molybdate/tungstate-binding protein MolA) (P44206)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Part of the ABC transporter complex MolBCA involved in molybdate import. Functions as a low-affinity molybdate transporter. Binds to both molybdate and tungstate, but not to sulfate or phosphate.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Molybdate import system permease protein MolB
- Molybdate import ATP-binding protein MolC
- Uncharacterized ABC transporter ATP-binding protein HI_1272
- Uncharacterized protein HI_1469
Sequence:
MKLKSLLIACLLSSLSFSALADRIITDQLDRKVTIPDHINRAVVLQHQTLNIAVQLDATKQIVGVLSNWKKQLGKNYVRLAPELENMAMPGDLNSVNIESLLALKPDVVFVTNYAPSEMIKQISDVNIPVVAISLRTGEVGEKGKLNPTLTDEDKAYNDGLKQGIELIAEVFEKKQQGDELVKAAFANRKLLADRLGDVSADKRVRTYMANPDLGTYGSGKYTGLMMEHAGAYNVAAATIKGFKQVSLENVLEWNPAVILVQDRYPDVVPQILNDQGWANIQALKDKKVFLMPEYAKAWGYPMPEALALGEVWLAKALYPQRFQDVDLDKMVNDYYQKFYRTSYKPDNAAR
Protein: Zinc finger and BTB domain-containing 4 (Zinc finger and BTB domain-containing protein 38) (A0A0R4INF0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- E3 ubiquitin-protein ligase RBBP6 isoform 1
- Dymeclin.
Sequence:
MKHRNKHIRGDRMGEGTEEANSAKTTRISLSFPLSAGLPGFSAQKHCSSSPPTSSSDVHSKDGLDGTAWMEETYRDKQLSKTSSKTDRLPCSSSSFPVDLTAPVSKNCKSSLSVSVDGSGSRYPASPLQHSNKMDSPKETAGVSLNNGYKEHSTTETAHILFNLSARAYQDQGVKDPENSKGKKRKANSLHVELSLPLPSINPHSSSSTPPPHSPSSVSLTSSPLTHPTASFHDSFRAVPKPELLCGVCHRLFSTASSLTVHMRLHRGGRVLSCRHCGKAFIHNKRLQSHEATCRQGLPAFPVPPKEEPLEEGEVEGERTDEAAEPEQLGQETRPGQPAKKVRDLTARHAEALTCGDTLGDDDHFVKVVDGHIIYFCSVCERSYMTLSSLKRHSNVHSWRRKYPCHFCDKVFALAEYRTKHEVWHTGERRYQCIFCWEAFPTYYNLKTHQKAFHGINPGLISSEKTANGGYKQKVNALKLYRLLPMRSLKRPYKTYSQPMADGLLTSDSTDNLHLSVDGSLPQPLDTKKLESFLKDLQNQDIKAETEGFPIRLDIEQGTEIASPQTDMTLEAGQVEDSDLWPSGNNNDKGQTPKCPERAVSSVIAFARSKPSVIMHSTAVSSSVIVHRNKTDSEERKRSPEKHQLAKTIKKHSQKEPTEAYREWNAVGLDPEVSKIRHPTEKLHKGRKVHHKTESSKTIPLAVGSEVKGSGPLCQITVRIGEEAIVKRSISETDLRRDKSPTRSKPKKSNLLQDKQREQRHTHHHQRKHRNSNQEGKEREPKRKSSKVKTKVRKYFFRQEVREDRNDHDVEDNLWRPYYSYKPKRKALHIQGAKAWKRKMHYKRSLRPMRRAERLMKNHLNKDAEDEDADEREEKRQKEKTEQKEVSDPVKTEVKEMPHSFPVSLRTEQKEKEKGTNGKPNLPLPSTVPQATPNPTHTASSIIKQRWSEDQASECGTCGRWFSSPRKRDKHEMTHLFEFVCMHCRAPFPSQFKLEEHQRSQHPKNKPLSAPTFYTSQSSKGEVEMKVADDDGVNGRSIEKGSPVRLGRRPLIRYTCSKCDKVCKTSAALNCHLKRHELGSLTEVEDAHEKQDMPSYTPPAVDTIPSLGLDTNCEQVQPVSVIYYSKPECQNTDNELGEKMEEHQRVRDCESPKVTKNEKVHSPRCAQFSQVIHSPTLERFNVISPNLPSVLVMNGAECLDYRTPEKQNLEKLDQQKRSQTPSNRQIQVSQMLTEPQIRRETTPSVPISLKTGRGYAFTDCDKNPNQDFSDLQDAQDLRIFPQSSSQAQDLSMPTTLAKKRELDEQIKHPSNILKAQSCNEEVSLLVPKEEPLSPIPSPTCSVIQTTPKGLSQRYSKSTCHSPEPLDLQLRPQLDHNQSHRGRHNSEKQGLMLPANSAGIIDPSSPALLNPQVPAAEPELKDITSGTHTEHHRVSGYPVQEYSLPMVIPGGYCSGKNQEEQILMSYPAGPLPFPPLGKMVPHADSTKLPFYPDPYHLLYGPQLLPYPYNLAALPMALNMMASGDKEPLPFLPFFNYAAAAAPLTGTLPHPLVMNPSLYNSGGSSSTKQDNP
Protein: Endophilin-A2 (EEN fusion partner of MLL) (Endophilin-2) (Extra eleven-nineteen leukemia fusion gene protein) (EEN) (SH3 domain protein 2B) (SH3 domain-containing GRB2-like protein 1) (Q99961)
Organism: Homo sapiens (Human)
Function: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, podosome {ECO:0000269|PubMed:23285027}. Note=Associated with postsynaptic endosomes in hippocampal neurons. {ECO:0000250}.
Interaction partners:
- Synaptojanin-1
- Endophilin-A1
- Endophilin-A3
- Programmed cell death 6-interacting protein
- Synaptojanin-2
- E3 ubiquitin-protein ligase CBL
- Leucine-rich repeat serine/threonine-protein kinase 2
- Rho GTPase-activating protein 8
- E3 ubiquitin-protein ligase CBL-C
- E3 ubiquitin-protein ligase CBL-B
Sequence:
MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ
Protein: RelA-associated inhibitor (Inhibitor of ASPP protein) (Protein iASPP) (NFkB-interacting protein 1) (PPP1R13B-like protein) (Q8WUF5)
Organism: Homo sapiens (Human)
Function: Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15489900}. Nucleus {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:15489900}. Note=Predominantly cytoplasmic but also nuclear. {ECO:0000269|PubMed:15489900}.
Interaction partners:
- Cellular tumor antigen p53
- Transcription factor p65
- Hypoxia-inducible factor 1-alpha inhibitor
- Cyclin-dependent kinase 1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Microtubule-associated protein RP/EB family member 1
- Kelch-like ECH-associated protein 1
- Tumor protein p73
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Sequence:
MDSEAFQSARDFLDMNFQSLAMKHMDLKQMELDTAAAKVDELTKQLESLWSDSPAPPGPQAGPPSRPPRYSSSSIPEPFGSRGSPRKAATDGADTPFGRSESAPTLHPYSPLSPKGRPSSPRTPLYLQPDAYGSLDRATSPRPRAFDGAGSSLGRAPSPRPGPGPLRQQGPPTPFDFLGRAGSPRGSPLAEGPQAFFPERGPSPRPPATAYDAPASAFGSSLLGSGGSAFAPPLRAQDDLTLRRRPPKAWNESDLDVAYEKKPSQTASYERLDVFARPASPSLQLLPWRESSLDGLGGTGKDNLTSATLPRNYKVSPLASDRRSDAGSYRRSLGSAGPSGTLPRSWQPVSRIPMPPSSPQPRGAPRQRPIPLSMIFKLQNAFWEHGASRAMLPGSPLFTRAPPPKLQPQPQPQPQPQSQPQPQLPPQPQTQPQTPTPAPQHPQQTWPPVNEGPPKPPTELEPEPEIEGLLTPVLEAGDVDEGPVARPLSPTRLQPALPPEAQSVPELEEVARVLAEIPRPLKRRGSMEQAPAVALPPTHKKQYQQIISRLFHRHGGPGPGGPEPELSPITEGSEARAGPPAPAPPAPIPPPAPSQSSPPEQPQSMEMRSVLRKAGSPRKARRARLNPLVLLLDAALTGELEVVQQAVKEMNDPSQPNEEGITALHNAICGANYSIVDFLITAGANVNSPDSHGWTPLHCAASCNDTVICMALVQHGAAIFATTLSDGATAFEKCDPYREGYADCATYLADVEQSMGLMNSGAVYALWDYSAEFGDELSFREGESVTVLRRDGPEETDWWWAALHGQEGYVPRNYFGLFPRVKPQRSKV
Protein: Capsid protein (Q77CC0)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Interaction partners:
Sequence:
MAQPEAFEVEIVLPGDLSHGDLAALQKCEGKVVFFTTLRRRVPLADVALASFSVNGVAPDTLGLMAAYRCRFPAVVLRVAPGRMMAAPLGVGPMPRGAFLQNTGPFDLCNGDAVCLLPPLLGPARALALASAGAELLFPMTVPLPQARALVARVVARAVEALGDRAAAARARAADVMYHNGRRYQVTPDVLCREGADAAARTLVLNMVFNVNEGSLLLLSLIPNLLTQGLQDGVANAIVQLGSASREAGQLLRLEPAEPRQDGGRRFCLYGALAAWISSATRLGDAVGARPLAKVCTFDGPSVVRVGEKAPIVVPL
Protein: CSC1-like protein ERD4 (Hyperosmolality-gated Ca2+ permeable channel 3.1) (AtOSCA3.1) (Protein EARLY-RESPONSIVE TO DEHYDRATION STRESS 4) (Q9C8G5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a hyperosmolarity-gated non-selective cation channel that permeates Ca(2+) ions. Mechanosensitive ion channel that converts mechanical stimuli into a flow of ions.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable methyltransferase PMT21
- Protein EARLY-RESPONSIVE TO DEHYDRATION 7
- AT5g45310/K9E15_9
- Ureide permease 4
- RPM1-interacting protein 4
- Hyperosmolality-gated Ca2+ permeable channel 4.1
Sequence:
MEFGSFLVSLGTSFVIFVILMLLFTWLSRKSGNAPIYYPNRILKGLEPWEGTSLTRNPFAWMREALTSSEQDVVNLSGVDTAVHFVFLSTVLGIFACSSLLLLPTLLPLAATDNNIKNTKNATDTTSKGTFSQLDNLSMANITKKSSRLWAFLGAVYWISLVTYFFLWKAYKHVSSLRAQALMSADVKPEQFAILVRDMPAPPDGQTQKEFIDSYFREIYPETFYRSLVATENSKVNKIWEKLEGYKKKLARAEAILAATNNRPTNKTGFCGLVGKQVDSIEYYTELINESVAKLETEQKAVLAEKQQTAAVVFFTTRVAAASAAQSLHCQMVDKWTVTEAPEPRQLLWQNLNIKLFSRIIRQYFIYFFVAVTILFYMIPIAFVSAITTLKNLQRIIPFIKPVVEITAIRTVLESFLPQIALIVFLAMLPKLLLFLSKAEGIPSQSHAIRAASGKYFYFSVFNVFIGVTLAGTLFNTVKDIAKNPKLDMIINLLATSLPKSATFFLTYVALKFFIGYGLELSRIIPLIIFHLKKKYLCKTEAEVKEAWYPGDLSYATRVPGDMLILTITFCYSVIAPLILIFGITYFGLGWLVLRNQALKVYVPSYESYGRMWPHIHQRILAALFLFQVVMFGYLGAKTFFYTALVIPLIITSLIFGYVCRQKFYGGFEHTALEVACRELKQSPDLEEIFRAYIPHSLSSHKPEEHEFKGAMSRYQDFNAIAGV
Protein: Mid-cell-anchored protein Z (Q8DR55)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Early cell division protein that marks the future cell division site and supports proper FtsZ ring positioning.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01941, ECO:0000269|PubMed:25470041}; Single-pass membrane protein {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_01941}. Note=In newborn cells, forms a ring positioned at mid-cell. Soon after cell division starts and the cells begin elongating, the ring splits into two rings that, as elongation proceeds, move along and mark the future division sites (PubMed:25470041, PubMed:25550321). Targeting to mid-cell does not depend on StkP and/or phosphorylation state (PubMed:25550321). {ECO:0000269|PubMed:25470041, ECO:0000269|PubMed:25550321}.
Interaction partners:
- Cell division protein FtsZ
- Serine/threonine-protein kinase StkP
- Cell division protein DivIVA
- Cell cycle protein GpsB
- Cell division protein FtsA
- YihY/virulence factor BrkB family protein
- THUMP domain-containing protein
- Endolytic murein transglycosylase
- Protein phosphatase PhpP
- Cell division protein SepF
Sequence:
MSKKRRNRHKKEAQEPQFDFDEAKELTVGQAIRKNEEVEAGVLPEDSILDKYVKQHRDEIEADKFATRQYKKEEFVETQSLDDLIQEMREAVEKSEASSEEVPSSEDILLPLPLDDEEQGLDPLLLDDENPTEMTEEVEEEQNLSRLDQEDSEKKSKKGFILTVLALVSVIICVSAYYVYRQVARSTKEIETSQSTTANQSDVDDFNTLYDAFYTNSNKTALKNSQFDKLSQLKTLLDKLEGSREHTLAKSKYDSLATQIKAIQDVNAQFEKPAIVDGVLDTNAKAKSDAKFTDIKTGNTELDKVLDKAISLGKSQQTSTSSSSSSQTSSSSSSQASSNTTSEPKPSSSNETRSSRSEVNMGLSSAGVAVQRSASRVAYNQSAIDDSNNSAWDFADGVLEQILATSRSRGYITGDQYILERVNIVNGNGYYNLYKPDGTYLFTLNCKTGYFVGNGAGHADDLDY
Protein: Speedy protein E4 (A6NLX3)
Organism: Homo sapiens (Human)
Interaction partners:
- Cyclin-dependent kinase 1
- Cyclin-dependent kinase 2
- M-phase inducer phosphatase 3
Sequence:
MASGQARPPFEEESPQPSTTVRSPEVVVDDEVPGPSAPWIDPSPQPQSLGLKRKSEWSDESEEELEEELELERAPEPEDTWVVETLCGLKMKLKRKRASSVLPEHHEAFNRLLGDPVVQKFLAWDKDLRVSDKYLLAMVIAYFSRAGLFSWQYQRIHFFLALYLASDMEEDNQAPKQDIFSFLYGKNYSQRPLFHKLRYQLLCSMRWRTWVSPEEMEEIQAYDPEHWVWARDRTLIS
Protein: Basigin, isoform A (Basigin, isoform B) (Basigin, isoform C) (Basigin, isoform D) (Basigin, isoform E) (Basigin, isoform F) (Basigin, isoform H) (Basigin, isoform I) (LD05560p) (LD19437p) (Q8IPG9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEAKFLASALSFLSIFLAIYAQSLDKLVPNYDNAEHQMKFYDIRSPLVLSCNVKDGTPGGVLIWKKNGTAVTDVPSLRGRFKLIADENKFIIDKTDTNDDGKYSCEFDGVSKEIEVIARVVVRVPSNTAVVEGEKMSVTCSVVGTKPELTWTFANVTLTNATDRFILKPDDNGVPNAILTLDNVTLDDRGEYKCIGRNAANVYGGNTTTPASDVTTVRVKGKFAALWPFLGICAEVLILCIIILIYEKRRNKSELEESDTDPQEQ
Protein: Uncharacterized protein, isoform B (A0A0B4KF97)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDRDSDAVSDAGPRLSQQRGQRNRRIIMRIEFKDSEDSASDQDRDDRPSCSAATRLRRSTRRQEVASHSDSDSVPRKSTRKLRNRYGPRSDCSSSGSDIDQLPTRTRKRKKVESSDEEEPERTPNAVGRIQPMPADPDDGFSSDISSNDLLEKCPICLLTFRQQEIGTPATCEHIFCAACIDAWSRNVQTCPIDRIEFDRIIVRDSYASRRVVREVRLDLSKSNTELVVDDEADTAALSEEEVTNCEICESPDREDVMLLCDSCNQGYHMDCLDPPLYEIPAGSWYCDNCIDSDDEDDNEQLELADDLDQLYEDIRGMGLPETRLRVREVQEPPRILRTRQNERIRAAVLRRTRSGATSAEDSTLTRTRTRTTTTTTTTTTTTRRTTTSTKKRPVQRRRRRRTRYRTYVVEYDLNNFDEKFALKTSKKVIRRRRRRRRRGVATASSEGPGRRLSASKRLAEQMGVKSEGFQSSHLSGGTASSFSLFGNANDLEYFSDSEPDAVSQISSAGLGSTAVQTSVRIGSIGAPRIRKALLQGKARIAAPPTAPTSAPAADILSSILDLQDRWHDASRNLGEVHIRADGTLNIPQRPAPTATEAPLPKAGTSKTEKHLTQAPLYQQGGGGPNYNRGGGAGSSDSYNNRYSGNTSYRGGGGGGAGGSSGGSGVPSSSGEASSRHLTGEGDGQGGGGFGNQNFSSSGSNNNTNMSSFIPFHLRFNTPTRQQQPRQQNVLPANQPTPPFPGSAPPPAPVASSSNNFSGQTPMFAAPLNHHPAPVMGMPVVLSIPPPPMPPASLPWNSPLFKITPLQQAPAKSNDGNQNDDVDNCPNFSIYSQESQAVANASAMPSGVPHGPADASDKFLKPNIMLLKPKQAI
Protein: Ankyrin-repeat, SH3-domain, and Proline-rich-region containing protein, isoform B (Q86BG1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GH01133p
- P53, isoform B
- LD40758p
Sequence:
MLTCVCRPVSGNLPKMPPASLMPAHRASASSASSSTSSTASLAFVSPTRGVVVTSEPKLNVPSRLTSAELRAMALRQQQQIDSQHQLLATKEQRLRFLKSQEVRSAVASAEGERLRRLRERVEAQESKLRRLRALRGQVDLQKTYNVTLSNDLDSIRALFSEKEKELSLAVAKVEALTRQLEELRRDRRCPVNILTAAGNGVGGQSLPPQASRELEKLRRELMYRNQLSLQQDARLHMQREALQQRQAELRSTDQRIYELQTRLQRKKQANTHHQQQQQQQQQHQQQQHQQQHQQTTVQQQQQQQQQLHVQSAQLLAAAAAATAQQQQQHQQHQQQQQQQQQQSASNLGKHGGVAALKQQLLQKQVNQLAAAAAAAAAGRARGNVAAVEPFIHTPQKSTITSTASYLSGGMKHAAATANTNQQNQLIQDLTHVKLGQNSGFFAGSVPVPVASSSCESDESKLAKKLLAAPAKTEAELRKQAQTEAMDSTTHIYAEVGPKKRDREAAAAAAAAAAAAAAAAQAAAEAANQAATAAAASAISPPATANASKIPKSTTSSSSSASALISKLNQQATAKESQDQQQSQAKKNEISVTSETLSERNTQQQLTVHSMPLGAISKSVALAVSNASKPLQVQVSNVAVPPRKPISSVAPNSVSSGSSIPKMITYSPKVNRVAPNVVMTDPRPALPPKPSKMSPTEQPSPVEANTSGSAGGAGSGAASASTANKTQTATFGLQSLNINDNLPIKAKPLTIRKQPLFEQPRLKSSQSSSNGQQKPPLLQLQNQRKSEPSARQPTENLPDTSPQHSPSSESSADETDRMVAPSITTSQQETSTSATSTTTTVTTSNIKERTGNGKPKLGRRVSFDPLALLLDASLEGELELVKKTAMQVANPSAANDEGITALHNAICAGHIDIVKFLVEFGCDVNAQDSDGWTPLHCAASCNNLSMVKFLVESGACLFASTLSDHETPAEKCEEDEEGFDGCSEYLYSIQEKLGILHNGDVYAVFSYEAQNGDELSFHVNEPLIVLRKGDDAENEWWWARNAAGEEGYVPRNLLGLYPRVPPHSPHFSD
Protein: Candida glabrata strain CBS138 chromosome B complete sequence (Q6FXR3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MKVAIITYSTYGHIDNLARAVKKGVESAGGQADLYRVEETLSKEILAQMNAPEKASDIPVATENILTEYDAFLFGVPTRFGTLPAQWSSFWDKTGGLWAQGALNGKVGGFFVSTSSYGGGQEATVKHCLSYLAHHGIIYVPLGYKNAFAELANIEEVHGGSPWGAGTLAGADGSRTASELELRIAQIQGKTFYETAIKFAPTSSAMMDDKMMKDDKMMKDDKMMKDDKMKSGKKAAMKDDKMMKDDKMKDDKMKDDKMKEKDSKFSCCTVM
Protein: ZIC family member 2 (Odd-paired homolog, Drosophila), A (Zinc finger cerebellum 2 protein) (Zinc finger protein ZIC 2a) (Q9IAT0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- EPH receptor B1.
- Homeobox protein TGIF1
- Sine oculis homeobox homolog 3a.
- Six3
- Sonic hedgehog protein
Sequence:
MLLDAGHQFPGLGVGTFARHHHSSSEMQDRDLSLAQNSFVDSAHMGAFKLNHDLSPGQSSAFTSQAPGYPAAALGAHAAHVTSYASSPFNSTRDFLFRSRGFGESSPAGGQHALFGPTAGSLHHSHTDSQGHILFPGIHEQHGSHGSPNVLNGQMRLGLPGEVFGRSDQYHQVSSPRTDPYSAAQLHNQYGSMNMNMGMNMAAHHHHPGAFFRYMRQQCIKQELICKWIDPEQLSNPKKSCNKTFSTMHELVTHVSVEHVGGPEQSNHICFWEECPRESKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFQCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSPPASDSSPAASSGYESSTPPGLVSPSTETQSNNNLSPSSAVHSSNNHSSLSSNFSEWYV
Protein: CD99 antigen-like protein 2 (MIC2-like protein 1) (Rhombencephalic expression protein 40 kDa) (Protein rhombex-40) (CD antigen CD99) (Q8R1R5)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:Q8TCZ2}.
Interaction partners:
- Cd99 protein
Sequence:
MVARLTTLLVCLVFSLATLVQRGYGDFDDFNLEDALKETSSVKQSHFSTTTRRTGTTRAPANPAERWDHMTTTTTKRPGTTRAPSNPLELDGFDLEDALDDRNDLDGPKKPSTGEGGGLSDKDLEDILGGGGYKPDKNKGGGGGYGSQDDPGSGAVTDPGTIAGLVSALAAALLGAVSGYLSYQHRKFCFSVQRGLDAAYVKGENLEAVVCEEPRVEAAMCEAPPVTDSTQHSQPTEPLAPERPRI