wanglab/gogpt-training-data huggingface dataset:
Protein: Sensory rhodopsin-2 (Sensory rhodopsin II) (SR-II) (P42196)
Organism: Natronomonas pharaonis (Natronobacterium pharaonis)
Function: Photophobic photoreceptor responsible for the negative phototaxis. Activates the sensory rhodopsin II transducer (HTR-II) in response to blue light.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11937052, ECO:0000269|PubMed:1597180}; Multi-pass membrane protein {ECO:0000269|PubMed:11937052, ECO:0000269|PubMed:1597180}.
Interaction partners:
Sequence:
MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTTPLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLYVRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVAD
Protein: Not1, isoform E (EC 3.1.13.4) (A8DY82)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDTSWINLILEIGYEFTSSVEECKNHLCSRERERAELQSKDVAKIVGLMCRRHSSLLDCNVNLPTPANFWPGQGQGGGSNSSGSSQTQITPQQQNPGSSNNNDGSDGNSSSDKKDKKETTEATQTWKPDVFVQALKEVVPQLNWKDVCMELDHPEFVLKDRIGLELLLTILRLATGSNIFPHPECIYRHWANTEGQLSLIATMLKNPDLFSFADFVFSQPALDVLKTAPDADNKEISSWKSLHLVEVLLSIADKGYYTQVHELFKFPAQNCPDVLFLALLNTSPPMTPLRQDLFNQLIPTFLGNHPNSNVILASAWSSNNFQLRSNIMNAMSEWYLRGNEFDQVKLSRILDLAQDLKALSALLNARSFLFIIDLACLASRREYLKLEKWLTDKIREHGEPFMQAIIKVLHRRCPQVINAKVPEDQLPPKQAQLLPETVTTMINCLQTCINNCMQPEMVEVIMQMTANVAIMANKARAQQQQQPGLVPPPPPTILRGHRGMDLPGGIVPPPPQQPFSGNLNAQMFGPGMDPLTNMSNNLAGLNLSGPNGAFNFGNMLTSPSRLMTPGANPYPLNLMQMPQAPPPPNVGNLGRMLPGGPQQQTPTPTPTAPNPNNPVMADLQIPVSKEVEDEVNSYFQRIYNHQPNPTLSIDEVLDILQRFKESSNRREQEVFLCMLRNLFEEYRFFCQYPEKELQITAQLFGGIIDRNLVPTFVALGLSLRCVLDALRKPDGSKLYYFGVTALDRFRTRLHTYNKYCEHIRSIPHFSDFPPHLIQYVEYGMHGQEPPPQKLIGLSNTIPSAISSGPGTEPIYRNSSMLGNMPAATPGSGPKSNAAVSHATRMKSIANATNIDTLLVANQEEKVTVPPEPVQDKTAFIFNNLSQLNIPQKCDEIKEIMTKEYWPWLAQYLVLKRASMEFNFHTLYYNFLDALKNGEINRFVTKETLRNIKVLLRSDKGVINFSDRSLLKNLGHWLGMMTLGRNRPILQLDLDLKSLLAEAYHKGQQELLFVVPFVAKILESSAKSRIFRSPNPWTMGIMYVLAELHQEPDLKLNLKFEIEVLCKTLNLELAKLRQVIYLKDPNRTHRIEEQMSQPKPKQLEPVASAPALPREQQSPAQPPPPPQQQQPPQQQVPPPPSSADVDAQNAAAMMMAAGGANSTPGSVSSPNLPTDSSQVALPPPEPRYSYVDVNVSNFQLIGQQLVLPPNTPFLHANPGIKHMVVNAVERTITDWLQPIVDRSIRIACATTEQIIRKDFALDADENRMRTAAHQMVRNLAAGMAMITGKDEIARAISQNLHKALLSGLNGMPSMAEIQAAAMQLASENVELVCAFIQKTSAEKAAAEIDRRLSTDFETRKIAREEGNRFVDAQILTYQQERLPEAVRIKVGAAPATLYAVYSEFARSIPGFQQMSDRDIALFVPKPTDLSQPNVFANDDSMVYGELASKMEAFMNTAIGVPTLQIQASKMHMLLNALIATRRLRDQESAFNLLTRAVEGLTEGLVNMHENMEQMKMYQNIHLRILGLLNNSFGAPNTERAVTKCFFDIREEVRYNVEAARALITSHFVNLNQFDGMLRDCMDNGNNYVAISFGIALLERLIMDDRVINIVSDNEFMATVELLGRLTQHRHRYPECIVNAIDTLWSGNFNSSSDYSPFNGNDRYLSGASHYIHSGMHHVRSCDTDDPPGLQEKTEFLLKDWVALYTQQNQQSTRDARNFGAFVQKMNTYGILKTDDLITRFFRQATHICTDVVYRMFAEPSLPINQAKNKIFQWIDAFVHLIAMLVRHSGEAGNPTTKINLLNKVLGIVLGTLIKDHEMRGVSFQQVGYHRFFMMLFMELCTADVILESLMHSIVSAFAYTYHLLNPSVAPGFCFAWLELISHRVFLGRILVQIPGQKGWPLYAQLLQDLFKYLAPFLRNTELGKPVQLLYKGTLRVLLVLLHDFPEFLCDYHFGFCDTIPPNCVQMRNIILSAFPRNMRLPDPFTPNLKVDMLSDSSNAPKVLSSYIMNIQPANFKKDLDSYLKARAPVTFLSELRGHLQVTSEPGTRYNMALMNALVMYVGTQAIALIRNKNFVPNTSNIAHSAHMDIFQNLAVDLDTEGRYLFLNAIANQLRYPNSHTHYFSCAVLHLFAEANSEAIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPIYKFWDHDFVHCAPEITKLFESVARSCLAKSNVTQQLNMPVVDGEGQEVATIN
Protein: Plasminogen activator inhibitor 2 (PAI-2) (Monocyte Arg-serpin) (Placental plasminogen activator inhibitor) (Serpin B2) (Urokinase inhibitor) (P05120)
Organism: Homo sapiens (Human)
Function: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1.
Subcellular location: Cytoplasm. Secreted, extracellular space.
Interaction partners:
- Tissue-type plasminogen activator
- Urokinase-type plasminogen activator
- Plasminogen
- Plasminogen activator inhibitor 1
- Urokinase plasminogen activator surface receptor
- Vitamin K-dependent protein C
- Calcium-activated chloride channel regulator 1
- Periostin
- Signal transducer and activator of transcription 4
- Peptidyl-prolyl cis-trans isomerase FKBP5
Sequence:
MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGFMQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFGRFSSP
Protein: Cyclin-dependent kinase inhibitor 7 (Inhibitor/interactor of CDK protein 5) (KIP-related protein 7) (Q94CL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. May target specifically CDKA-1.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17253089, ECO:0000269|PubMed:18948957}. Note=Homogeneously distributed. Accumulates strongly in vegetative cell nuclei immediately after asymmetric division and disappears later.
Interaction partners:
- F-box/LRR-repeat protein 17
- Cyclin-dependent kinase A-1
- Cyclin-D2-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B2-2
- E3 ubiquitin-protein ligase RHF1A
- Cyclin-D4-1
- Protein KINKY POLLEN
Sequence:
MSETKPKRDSEYEGSNIKRMRLDDDDDVLRSPTRTLSSSSSSSLAYSVSDSGGFCSVALSEEEDDHLSSSISSGCSSSETNEIATRLPFSDLEAHEISETEISTLLTNNFRKQGISSSENLGETAEMDSATTEMRDQRKTEKKKKMEKSPTQAELDDFFSAAERYEQKRFTEKYNYDIVNDTPLEGRYQWVSLKP
Protein: FYVE and coiled-coil domain-containing protein (Q8IKN0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MLNSKEKEVNGSPSDSLNGDAENENENERKCLWVPDEEVTNCYSCNVVFNVRVRKHHCRACGNVFCSNCSDNKIKISEYSYSEKVRVCDRCFMERSSPQTLLLQEDLGARKQINQDLKKALSEKMAIVERFKTFLIEFDNEILNNTDNTDGNTDVLSLLKRGEKGLKSLNEKIKNYDSIIEEQKNQLENLKMEKEQKMELNKMLNLRNHEIQQKNINIKNLMKEKNELALVKEESEGIIESYKKQVEKLIIRCNQLELEKKTYNKNDLNNFSMTNTSSSSYNQGSSFNLPSNGMSVSYTIADGPNEYMEDENCCNRCQRRMCNIM
Protein: Galectin-1 (Gal-1) (14 kDa laminin-binding protein) (HLBP14) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (HBL) (HPL) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (Putative MAPK-activating protein PM12) (S-Lac lectin 1) (P09382)
Organism: Homo sapiens (Human)
Function: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:14617626}. Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:32272059}. Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000269|PubMed:32272059}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase C
- Chorionic somatomammotropin hormone 1
- Chorionic somatomammotropin hormone 2
- Vimentin
- Fibronectin
- Galectin-3-binding protein
- Annexin A2
- GTPase HRas
- Epithelial membrane protein 3
- Chorionic somatomammotropin hormone 1
Sequence:
MACGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQPGSVAEVCITFDQANLTVKLPDGYEFKFPNRLNLEAINYMAADGDFKIKCVAFD
Protein: Transcription factor E2F5 (E2F-5) (Q15329)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor-initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis.
Subcellular location: Nucleus.
Interaction partners:
- Retinoblastoma-like protein 2
- Transcription factor Dp-1
- Retinoblastoma-like protein 1
- Mothers against decapentaplegic homolog 3
- Transcription factor Dp-2
- Transcription factor E2F4
- Retinoblastoma-associated protein
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 2
- Protein lin-37 homolog
Sequence:
MAAAEPASSGQQAPAGQGQGQRPPPQPPQAQAPQPPPPPQLGGAGGGSSRHEKSLGLLTTKFVSLLQEAKDGVLDLKAAADTLAVRQKRRIYDITNVLEGIDLIEKKSKNSIQWKGVGAGCNTKEVIDRLRYLKAEIEDLELKERELDQQKLWLQQSIKNVMDDSINNRFSYVTHEDICNCFNGDTLLAIQAPSGTQLEVPIPEMGQNGQKKYQINLKSHSGPIHVLLINKESSSSKPVVFPVPPPDDLTQPSSQSLTPVTPQKSSMATQNLPEQHVSERSQALQQTSATDISSAGSISGDIIDELMSSDVFPLLRLSPTPADDYNFNLDDNEGVCDLFDVQILNY
Protein: Sialic acid-binding Ig-like lectin 12 (Siglec-12) (Sialic acid-binding Ig-like lectin-like 1) (Siglec-L1) (Q96PQ1)
Organism: Homo sapiens (Human)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MLLLLLLLPPLLCGRVGAKEQKDYLLTMQKSVTVQEGLCVSVLCSFSYPQNGWTASDPVHGYWFRAGDHVSRNIPVATNNPARAVQEETRDRFHLLGDPQNKDCTLSIRDTRESDAGTYVFCVERGNMKWNYKYDQLSVNVTASQDLLSRYRLEVPESVTVQEGLCVSVPCSVLYPHYNWTASSPVYGSWFKEGADIPWDIPVATNTPSGKVQEDTHGRFLLLGDPQTNNCSLSIRDARKGDSGKYYFQVERGSRKWNYIYDKLSVHVTALTHMPTFSIPGTLESGHPRNLTCSVPWACEQGTPPTITWMGASVSSLDPTITRSSMLSLIPQPQDHGTSLTCQVTLPGAGVTMTRAVRLNISYPPQNLTMTVFQGDGTASTTLRNGSALSVLEGQSLHLVCAVDSNPPARLSWTWGSLTLSPSQSSNLGVLELPRVHVKDEGEFTCRAQNPLGSQHISLSLSLQNEYTGKMRPISGVTLGAFGGAGATALVFLYFCIIFVVVRSCRKKSARPAVGVGDTGMEDANAVRGSASQGPLIESPADDSPPHHAPPALATPSPEEGEIQYASLSFHKARPQYPQEQEAIGYEYSEINIPK
Protein: Dual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2) (O35491)
Organism: Mus musculus (Mouse)
Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9307018, ECO:0000269|PubMed:9852100}. Nucleus speckle {ECO:0000269|PubMed:9852100}. Note=Inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. {ECO:0000269|PubMed:9852100}.
Interaction partners:
- PHD finger protein 12
Sequence:
MPHPRRYHSSERGSRGSYHEHYQSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDHSSDRRLYDRRYCGSYRRNDYSRDRGEAYYDTDFRQSYEYHRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGTQVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPVPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEDHHQLFDLIENMLEYEPAKRLTLGEALQHPFFACLRTEPPNTKLWDSSRDISR
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (B6CAM1)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
Interaction partners:
Sequence:
MEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDFCSLNEFSITGSTYAPEGEVLKNDKPIRSGQFDGLVELATICALCNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRNLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPMTGPVKEKILSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSSRFMEYETDLTFVGVVGMLDPPRKEVMGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVGAAAWWFMYAEDGPGVTYHQLTHFMQCTEDHPHFEGLDCEIFEAPEPMTMALSVLVTIEMCNALNSLSENQSLMRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLKALDLTQWLMVLKISLPVIGLDEILKFIARNYLEG
Protein: Leucine-rich repeat protein 1 (AtLRR1) (Q9FPJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plant defense response.
Interaction partners:
- U-box domain-containing protein 11
- At1g50440
- Bromo-adjacent homology
- Glucan endo-1,3-beta-glucosidase 14
- Protein kinase superfamily protein
- Kinase superfamily with octicosapeptide/Phox/Bem1p domain-containing protein
Sequence:
MASRNYRWELFAASLTLTLALIHLVEANSEGDALYALRRSLTDPDHVLQSWDPTLVNPCTWFHVTCNQDNRVTRVDLGNSNLSGHLAPELGKLEHLQYLELYKNNIQGTIPSELGNLKNLISLDLYNNNLTGIVPTSLGKLKSLVFLRLNDNRLTGPIPRALTAIPSLKVVDVSSNDLCGTIPTNGPFAHIPLQNFENNPRLEGPELLGLASYDTNCT
Protein: Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked nuclear protein) (A0A096LNL9)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQSETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTTIMELRDRLPKKQQASASTDGVDKLSGKEESFTSLEVRKVAETKEKSKHLKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLPEREEICHFPKGIKQIKNGTTDGEKKSKKIRDKTSKKKDELSDYAEKSTGKGDSCDSSEDKKSKNGAYGREKKRCKLLGKSSRKRQDCSSSDTEKYSMKEDGCNSSDKRLKRIELRERRNLSSKRNTKEIQSGSSSSDAEESSEDNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADITSSSSSDIEDDDQNSIGEGSSDEQKIKPVTENLVLSSHTGFCQSSGDEALSKSVPVTVDDDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRTGKQNEENPGDEEAKNQVNSESDSDSEESKKPRYRHRLLRHKLTVSDGESGEEKKTKPKEHKEVKGRNRRKVSSEDSEDSDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSY
Protein: Large ribosomal subunit protein mL42 (28S ribosomal protein S32, mitochondrial) (MRP-S32) (S32mt) (39S ribosomal protein L31, mitochondrial) (L31mt) (MRP-L31) (39S ribosomal protein L42, mitochondrial) (L42mt) (MRP-L42) (Q9CPV3)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y6G3}.
Interaction partners:
- Small ribosomal subunit protein bS18m
- Large ribosomal subunit protein mL66
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein uS12m
Sequence:
MAAAVKWAISNRTIWKHLLPIQNGALSSACHKSTYSSLPDDYNCQVDLALTADGRTIVCYHPSVDIPYEHTKPIPQPDLLHNNEETHEQILKAKLEVRKSKQLEQGPMIEQLSKVFYTTKHRWYPHGQYHNRRKKLNPPRDR
Protein: Sialic acid-binding Ig-like lectin 5 (Siglec-5) (CD33 antigen-like 2) (Obesity-binding protein 2) (OB-BP2) (OB-binding protein 2) (CD antigen CD170) (O15389)
Organism: Homo sapiens (Human)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Sialic acid-binding Ig-like lectin 14
- Toll-like receptor 2
- Signal transducer CD24
Sequence:
MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMKRQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALRLLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRAQHPLGFLQIFLNLSVYSLPQLLGPSCSWEAEGLHCRCSFRARPAPSLCWRLEEKPLEGNSSQGSFKVNSSSAGPWANSSLILHGGLSSDLKVSCKAWNIYGSQSGSVLLLQGRSNLGTGVVPAALGGAGVMALLCICLCLIFFLIVKARRKQAAGRPEKMDDEDPIMGTITSGSRKKPWPDSPGDQASPPGDAPPLEEQKELHYASLSFSEMKSREPKDQEAPSTTEYSEIKTSK
Protein: Tumor necrosis factor ligand superfamily member 18 (Activation-inducible TNF-related ligand) (AITRL) (Glucocorticoid-induced TNF-related ligand) (hGITRL) (Q9UNG2)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B. Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1. Promotes leukocyte adhesion to endothelial cells. Regulates migration of monocytes from the splenic reservoir to sites of inflammation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17449724}; Single-pass type II membrane protein {ECO:0000269|PubMed:17449724}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 18
- Tumor necrosis factor ligand superfamily member 4
- Tumor necrosis factor receptor superfamily member 4
- Tumor necrosis factor ligand superfamily member 9
- Tumor necrosis factor receptor superfamily member 9
- Indoleamine 2,3-dioxygenase 1
- Tumor necrosis factor receptor superfamily member 14
- Indoleamine 2,3-dioxygenase 2
- Ig-like domain-containing protein
- CD70 antigen
Sequence:
MCLSHLENMPLSHSRTQGAQRSSWKLWLFCSIVMLLFLCSFSWLIFIFLQLETAKEPCMAKFGPLPSKWQMASSEPPCVNKVSDWKLEILQNGLYLIYGQVAPNANYNDVAPFEVRLYKNKDMIQTLTNKSKIQNVGGTYELHVGDTIDLIFNSEHQVLKNNTYWGIILLANPQFIS
Protein: Antigen presenting cell lectin-like receptor A1 (C-type lectin domain family 4, member b2) (Q67DU8)
Organism: Mus musculus (Mouse)
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- Antigen presenting cell lectin-like receptor A2
- C-type lectin domain family 6 member A
- E3 ubiquitin-protein ligase CBL-B
Sequence:
MMQERPAQGQVVCWSLRLWMAALISILLLSTCFIASCVVTYQLMMNKPNRRLSELHTYHSNLICFSEGTTVSEKVWSCCPKDWKPFGSYCYFTSTDSRASQNKSEEKCSLRGAHLVVIHSQEEQDFITRMLDTAAGYFIGLSDVGNSQWRWIDQTPYNDRATFWHKGEPNNDYEKCVILNYRKTMWGWNDIDCSDEENSVCQMKKIYL
Protein: Ubiquitin carboxyl-terminal hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme 1) (hUBP) (Ubiquitin thioesterase 1) (Ubiquitin-specific-processing protease 1) [Cleaved into: Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment] (O94782)
Organism: Homo sapiens (Human)
Function: Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:15694335}.
Interaction partners:
- WD repeat-containing protein 48
- Fanconi anemia group D2 protein
- Fanconi anemia group I protein
- Polyubiquitin-C
- E3 ubiquitin-protein ligase FANCL
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- RAD51-associated protein 1
- Proliferating cell nuclear antigen
Sequence:
MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQENEEKASEYRASEIDQVVPAAQSSPINCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIISRKKEALKDEANQKDKGNCKEDSLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEVKNVAELPTKVEEIPHPKEEMNGINSIEMDSMRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSKEHQSLEENQRQTRSKRKATSDTLESPPKIIPKYISENESPRPSQKKSRVKINWLKSATKQPSILSKFCSLGKITTNQGVKGQSKENECDPEEDLGKCESDNTTNGCGLESPGNTVTPVNVNEVKPINKGEEQIGFELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKVTDLNSLELDKGNFVVDQMCEIGKPEPLNEEEARGVVENYNDEEVSIRVGGNTQPSKVLNKKNVEAIGLLGGQKSKADYELYNKASNPDKVASTAFAENRNSETSDTTGTHESDRNKESSDQTGINISGFENKISYVVQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPSTSPTSTPYLLFYKKL
Protein: Dr1-associated corepressor (Dr1-associated protein 1) (Negative cofactor 2-alpha) (NC2-alpha) (Q14919)
Organism: Homo sapiens (Human)
Function: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein Dr1
- Forkhead box protein H1
- TATA-box-binding protein
- TATA-binding protein-associated factor 172
- TATA box-binding protein-like 2
- Transcription initiation factor IIB
- Cilia- and flagella-associated protein 20
- TATA box-binding protein-like 1
- Cilia- and flagella-associated protein HOATZ
- Nuclear transcription factor Y subunit beta
Sequence:
MPSKKKKYNARFPPARIKKIMQTDEEIGKVAAAVPVIISRALELFLESLLKKACQVTQSRNAKTMTTSHLKQCIELEQQFDFLKDLVASVPDMQGDGEDNHMDGDKGARRGRKPGSGGRKNGGMGTKSKDKKLSGTDSEQEDESEDTDTDGEEETSQPPPQASHPSAHFQSPPTPFLPFASTLPLPPAPPGPSAPDEEDEEDYDS
Protein: cAMP-specific phosphodiesterase, putative (Q38EQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGKNERDQYQDLALHLSFSSGTELSDSYVMSYRGSDGCFGDAVFNGAAPARNVLFGNIPCKQRVEKFSIQDSSLANRCNMQVNLKRDTPVLQDPSDTFARMNQVMHQTLKYVKEVESIDFSSSNIIDFNGEIMEDPRRVFLSVCTSVFANFSFCSQLDVEKLLSFLSDIFENYSEDNAYHNAVHAADSVQMLYLILREKPAILLFTNEEILVCFLATLCLSFIHPGVTDAFLARIDHPLTLVYGDVTTQRSASLTAFLYFLNREENRFIDLSSSAGTRPISQYLRELLVETVLATAPRSRRTLLSDLQDVAASNVVSVDDLRFLLSAIVTLSDSALALRPRAQFISWSRLLCAEWLSEATQEERRRMDPLVPNLQKRVGEGGLTMVSDYCRVWLRPVAAATRALVPQDLYDNLERNSDVPTFGEVAAFSVPDVSADKPWSDGSLSVFEILRKVTMHAKSLDRKASKRAILNATCGRLVSAPASQLSSPFHAPSEPSISCSPVEKLVSHPSRCEHYFSFLRLYDTYDREGRPATEFAEQLVFLAMQLNPDYVGRYAREGIDASSKEDCSKIASLIIQSEEAPSTAEVIASPLRGAEQTDGFILRLMEMYTERDRNRNNCSVQNSHTNLQSTSRCLLPCSNPVYGGMDRGRK
Protein: HERC1 (Q9CS23)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GVDAGLRVGGRCVHKQTGRHATLLGVVKEGSTSAKVQWDEAEITISDTPLYNLEPCEPLLFDVARFRGLTASVLLDLTYLTGIHEDVGKQSIKRHEKKHRHESEEKGDIEQKPESESILDVRTGLMSDDVKSQGTTSSKSENEIASFSLEPTLPGVESQH