wanglab/gogpt-training-data huggingface dataset:
Protein: Meiotic chromosome segregation protein P8B7.28c (O94276)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for meiotic chromosome segregation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Chromatin modification-related protein rik1
- Protein argonaute
- Rik1-associated factor 2
- Rik1-associated factor 1
- Chromo domain-containing protein 1
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Cullin-4
- RNA-induced transcriptional silencing complex protein tas3
- Protein Dicer
- Chromatin-associated protein swi6
Sequence:
MDFKSRKYKIKKHPKDCKLHAKKYRGTLNSKGKNDNDCLIMCMRCRKVKGIDSYSKTQWSKTFTFVRGRTVSVSDPKVICRTCQPKQHDSIWCTACQQTKGINEFSKAQRHVLDPRCQICVHSQRNDGDDNLESDKFVDPFIGDDSDLDDDIYIHDKQTINSEYADDVSDNTDEERTESKGQQESNSAEEYDDDDSDEDRMEEIFQQFKKEKQIV
Protein: DNA polymerase alpha catalytic subunit A (EC 2.7.7.7) (DNA polymerase I subunit A) (DNA polymerase alpha:primase complex p180 subunit) (DNA polymerase-primase complex p180 subunit) (Pol alpha-primase complex p180 subunit) (P13382)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13.
Subcellular location: Nucleus.
Interaction partners:
- DNA polymerase alpha-binding protein
- DNA primase large subunit
- Cell division control protein 13
- DNA primase small subunit
- DNA polymerase alpha subunit B
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- DNA polymerase delta small subunit
- Cell division control protein 45
- DNA replication licensing factor MCM4
Sequence:
MSSKSEKLEKLRKLQAARNGTSIDDYEGDESDGDRIYDEIDEKEYRARKRQELLHDDFVVDDDGVGYVDRGVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSIPIDNFDDILGEFESGEVEKPNILLPSKLRENLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSSTDKYLEIESSPLKLQSRKLRYANDVQDLLDDVENSPVVATKRQNVLQDTLLANPPSAQSLADEEDDEDSDEDIILKRRTMRSVTTTRRVNIDSRSNPSTSPFVTAPGTPIGIKGLTPSKSLQSNTDVATLAVNVKKEDVVDPETDTFQMFWLDYCEVNNTLILFGKVKLKDDNCVSAMVQINGLCRELFFLPREGKTPTDIHEEIIPLLMDKYGLDNIRAKPQKMKYSFELPDIPSESDYLKVLLPYQTPKSSRDTIPSDLSSDTFYHVFGGNSNIFESFVIQNRIMGPCWLDIKGADFNSIRNASHCAVEVSVDKPQNITPTTTKTMPNLRCLSLSIQTLMNPKENKQEIVSITLSAYRNISLDSPIPENIKPDDLCTLVRPPQSTSFPLGLAALAKQKLPGRVRLFNNEKAMLSCFCAMLKVEDPDVIIGHRLQNVYLDVLAHRMHDLNIPTFSSIGRRLRRTWPEKFGRGNSNMNHFFISDICSGRLICDIANEMGQSLTPKCQSWDLSEMYQVTCEKEHKPLDIDYQNPQYQNDVNSMTMALQENITNCMISAEVSYRIQLLTLTKQLTNLAGNAWAQTLGGTRAGRNEYILLHEFSRNGFIVPDKEGNRSRAQKQRQNEENADAPVNSKKAKYQGGLVFEPEKGLHKNYVLVMDFNSLYPSIIQEFNICFTTVDRNKEDIDELPSVPPSEVDQGVLPRLLANLVDRRREVKKVMKTETDPHKRVQCDIRQQALKLTANSMYGCLGYVNSRFYAKPLAMLVTNKGREILMNTRQLAESMNLLVVYGDTDSVMIDTGCDNYADAIKIGLGFKRLVNERYRLLEIDIDNVFKKLLLHAKKKYAALTVNLDKNGNGTTVLEVKGLDMKRREFCPLSRDVSIHVLNTILSDKDPEEALQEVYDYLEDIRIKVETNNIRIDKYKINMKLSKDPKAYPGGKNMPAVQVALRMRKAGRVVKAGSVITFVITKQDEIDNAADTPALSVAERAHALNEVMIKSNNLIPDPQYYLEKQIFAPVERLLERIDSFNVVRLSEALGLDSKKYFRREGGNNNGEDINNLQPLETTITDVERFKDTVTLELSCPSCDKRFPFGGIVSSNYYRVSYNGLQCKHCEQLFTPLQLTSQIEHSIRAHISLYYAGWLQCDDSTCGIVTRQVSVFGKRCLNDGCTGVMRYKYSDKQLYNQLLYFDSLFDCEKNKKQELKPIYLPDDLDYPKEQLTESSIKALTEQNRELMETGRSVVQKYLNDCGRRYVDMTSIFDFMLN
Protein: Putrescine export system permease protein SapC (P0AGH5)
Organism: Escherichia coli (strain K12)
Function: Part of a putrescine export transport system, does not play a role in resistance to antimicrobial peptides.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Putrescine export system permease protein SapB
- Putrescine export system ATP-binding protein SapD
- Putrescine export system ATP-binding protein SapF
- Probable ABC transporter periplasmic-binding protein SapA
- Dipeptide transport ATP-binding protein DppD
- Dipeptide transport ATP-binding protein DppF
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Nickel import ATP-binding protein NikD
- Probable D,D-dipeptide transport ATP-binding protein DdpF
- Oligopeptide transport ATP-binding protein OppD
Sequence:
MPYDSVYSEKRPPGTLRTAWRKFYSDASAMVGLYGCAGLAVLCIFGGWFAPYGIDQQFLGYQLLPPSWSRYGEVSFFLGTDDLGRDVLSRLLSGAAPTVGGAFVVTLAATICGLVLGTFAGATHGLRSAVLNHILDTLLAIPSLLLAIIVVAFAGPSLSHAMFAVWLALLPRMVRSIYSMVHDELEKEYVIAARLDGASTLNILWFAVMPNITAGLVTEITRALSMAILDIAALGFLDLGAQLPSPEWGAMLGDALELIYVAPWTVMLPGAAIMISVLLVNLLGDGVRRAIIAGVE
Protein: Rifin (Q8I494)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKFSYFNILLFSIPLNILINDHSKYSSCKHTSNSKTTKPHRSLYECGLYSPANNDNDPEMKRVMQQFEDRTSQRFHEYDERMQSKRMQCKEQCDKEIQKIILKDKLEKQMEQQLNTLETKIDTDDIPTCVCEKSLADKVEKGCLRCGYGLGTVAPTVGLIGAVAVHVWKPMALEAAIEAAIAKSAAEISAAANAAGIQAGKIAVIESLKKLYVDYFWPEMSNYILNMSHYNGVANLTAFIHEPKFNVCKDAGEVILDKCNAFDMGFGILKKDGVTNGLLPKDAVPRVLKGIVGQAEGPAKVAADAARQTVTAEITEKETAAINTIFMSKQTAIIASVVAIVVIVLIMIIIYLILRYRRKKKMKKKLQYIKLLKE
Protein: Uncharacterized protein, isoform D (Q86BG2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEMGGLKRKLVDQSLNLLDSLNTALRCDAIQFLLQTLKCKYPESCDQVVRNLFSHIAAANDNGESGGRAQQHELARTKQLQLLLTAKKEKKELGIGCEAEIKRENDEEEAGSTDLNQNFEKIPCKEEFLCLEEEEEDFLDDADTQNSSSLQFHTGNNVDALALGPGDPLELIQSGVSLLVKRKYAATFDDELIGDGDGDEANSNSSDGKMVKRKRTNNMHLTVSSVRRKEEHGQLGDGYVFHEDSQYTMRYHHSTGEFSERAFKAQFRALLRLALSQHHKPFLRQFYENFVVNGRLLGTTPSMRVLKELREQRLEEWRRQRERRQLVILMEQSETQRDEEFQQQQELVENQEEVQQEQEQQQQQLEDIQQQHLEEIQRQQQLPAISFGDSELESETESQLSSAAQEIMKFEEFIDEGVGAGRLIDGLEMEPEIDDMLAGAGSMNSASGHSSNSSSSGSGSAGNGNGISGVILENNSHHTHHLSSSSSANLVINGLTSSNSISNNNNNSNNVSLHRPQLTPQAQNQLAASMKPSDHIPISMPMENMDLKAGQAAHGTANAIMQGGSSSLASQLHQQQKPYNSSNNPLSMMGGMMQQQQQQHVAMPHHQRQMMMMPEDFPQHGASMMNSRQMPALAALSNLGDTPAMSGQLNSSLELDDNDLSADEDDDDLDHDLDELDAAKQQLIDGGSSSSTSLQAPPSQHGSGSGGSGGQTPGSKKDKPSYNCLLCPKSYRKRKSLLDHYKMHPGYCHDCGQRNGNTLEEIIHHNRTMHVKEFPFVCETCGESYSRKQQFHAHVESHNKKEIKTFPCGECGLKFPQKKLQQHFEETGHKADGAICEVCGEEFQSKNALYQHIIRVHKRDNFFECHICHNRFTLKANLERHVQLHTEIKRPYVCDLCGSSYFTYPALKEHYSNAHVDVSECKCTLCGKRFGSAKSLQRHLPSHSEERPHCCNYCDQTFKWKTHLVRHKQTMHGNEPPPPKKGKQRFPKTSEEDMGSLPDMPGPPPVKASKKAATSKAKAQAAAAAAAAASSQQQQQKGSAATPTPPPPVSTTPGCLQQDPFNAAMVSSNSSQSSTASTSQHSVSTSESQQNSIYNQSFNAEKQQPGQQQPQNTLHQQHPTPPPPQQQQQQQQQQQALPQSRVGPGELHLQRMNSFGQDGQFHFESNPAAGAYQQHQLISQYQQQQQQQQQQQQQQPQQQQQHHLAQQQQQHMRSHTPQSPHPPHPSQLQQQQPQQHFSSPHHMPPMHHQHQLMMQQQHRHNQRSPLHHHPAAQQLQQQHQQPSHSPQHQHARLQSPQPAPVQQQQQQQQQQQQQQQQFLQQQAADTWGNMNFGNPPNNQQVELKDNKFYIVESAEFLGLPMNVPPSPQQQQQQAVSKPQQQQQQQHPQPQQPDPTLAGDLMSFQHMWPAPGFSQTSQQQQPQQQQQQQAAQQQQQAQSQANSSDPHNYNNIGSILTNLIDTNPAPMEYNFDLMQQQQTPSAQQQQQQQQQQQAAQQQHHSAGAYGSGLMRSGGGVYGGAYEQHLSDQLVSEQQKQNSFQPYHPHGLQAQQQQPLHPHPHLLPPPAPHNNVYDRTGVGVGVGVGVGVGVGVGYPMLGDDTKSVLPPMMGGMMQQMPPHGQQPDLIYYPVKND
Protein: Tricalbin-3 (Q03640)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in membrane trafficking.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:35015055}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:35015055}; Multi-pass membrane protein {ECO:0000255}. Note=More enriched in the cortical endoplasmic reticulum (ER) that is closely apposed to the cell membrane than in the perinuclear ER or internal ER tubules that connect the nucleus to the cortical ER. {ECO:0000269|PubMed:22250200}.
Interaction partners:
- Increased sodium tolerance protein 2
- Vesicle-associated membrane protein-associated protein SCS2
- Vesicle-associated membrane protein-associated protein SCS22
- Tricalbin-1
- Phosphatidylinositol-3-phosphatase SAC1
- Oxysterol-binding protein homolog 6
Sequence:
MTGIKAQVHPPPDSTLFHEEEKKKVGGNLPQKVINQQERGSDHAPSGHHQYHQLINHDANDTKTSNSVSDVSKGQKTADSNPEGKKQSSKDIFVASSAQKTNQLPGPNPQGSIGAVPLEGLRPKEFRSAPSRKPNKFDTSITKPGVLDDLGKLDEKDIKEKFHLDSDDKLFPWQNVGEFHASGKGSPNTKMSRVIKAYILENFYNDWYCNIATVLGTCFFSWLFAYIGFSWWSMIFIFLGTATVYNAEYTRFNRNIRDDLKRVTVEETLSDRVESTTWLNSFLSKFWVIYMPVLSQQVKDNVNPQLAGVAPGYGIDALAIDEFTLGSKAPTIKGIKSYTKTGKNTVEMDWSFAFTPSDVSDMTATEAREKINPKISLGVTLGKSFVSKTMPILVEDINVAGKMRIKVEFGKAFPNIKIVSLQLLEPPLIDFALKPIGGDTLGLDVMSFLPGLKSFVKNIINSNIGPMLFPPNHLDINVEDIMAAQSKEAIGVLAVTIASADSLKGSDFITNTVDPYIVMTTEDAVPGTDEEVRTSIKSNVKNPRWNETKYLLLNTLEQKLNLKCFDFNDVRKDTVIGDLQLDLADLLQNPVLDNQTAELRSGTKSKGILHYSLHWFPVKEDKSEEKAVERAEAKAKGKKEDENEDTTEKEEDENEESSQTDVGIAKITLQKVKYLDTTSSMTGSLSPCAELFIDGQKVKSYRTLRRINEPSWNETIEVLVPSKSNSKFVLKIFDDRMNGKALICEYSSSLDDIMTTLDTAQEFVKGSPQGDIYLDVSWKSIEMTGAFAAANSVSEPIGCIKLDVKDAIIKGDLSGVGDVDPYYTVSLNRRVLYKSIYHSDTDHPIFDNSTYVPIFSPNQILTLEFHDYQKIGKDRFIGSVQIPTSNVFKKDPKSGKYVGNNGKEEISKLKLKDHEHKVTESIVNVSTTFIPINLVYSPEELVNVEKLEKELKEKKKKFEATQEENEQEMEKNPKEWEVAEIEDPFDSDEKKINRKAKLSLNELIKQKSGILSMQILEGTLSPSSAYLEILADDISYPVFICMKPSQGKLNSEMANIFIRDLNYSKLHFRVSKKHIAKDSDDVISETSYSTLKLLKQAYEEPMWLNFNGSKMKVRFLYTPTSVKLPSSESVEDTGYLNIKLISGHGLKSADRNGYSDPFVHIFVNDKKVFKSNIKKKTLDPVWNEDAKIPILSRSKNQVIFNVLDWDRAGDNDDLGQASLDVSSLEVGKTYNWNLNLNTQGSIKLQGSFNPEYIKPSFDIVKGGITDKPMKIASGAAHATVGIAGTGIGAATGVATGGLKKGGHLLKSLGGNPMKRSKSSNGNESNGAKKSSEKKSFDRRSPSNLNSTSVTPRASLDYDPSVPNTSYAPVQSASPVVKPTDNTSSSSNKKDTPSSNSRGHSRASSFARTLAPHGTYNGFITVVAAENVAKHVQIKISLTQGGRLKHIYKTKSQKANNDGVAVFDEECSFKASPEANLVLGAISHQRLSRDKDLGIAQINLGDPQIQQDGQISVKLGDGHLIVKINYGKDKNGQVPPVPEVPQEYTQ
Protein: Cytochrome c oxidase subunit 7C, mitochondrial (Cytochrome c oxidase polypeptide VIIc) (P17665)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 6C
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome b-c1 complex subunit 7
Sequence:
MLGQSIRRFTTSVVRRSHYEEGPGKNLPFSVENKWRLLAMMTVYFGSGFAAPFFIVRHQLLKK
Protein: Fructose-bisphosphate aldolase, cytoplasmic isozyme (EC 4.1.2.13) (P29356)
Organism: Spinacia oleracea (Spinach)
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MTAYRGKYADELIANASYIATPGKVILAADESTGTIGKRFPSINVENVESNRRALRELLFTTPGALPYLSGVILFEETLYQKTADGKPFVDAMKDGGVLPGIKVDKGTVELAGTNGETTTQGLDGLAQRCAQYYTAGARFAKWRAVLKIGPTEPSPLAILENANGLARYGIICQENGLVPIVEPEILVDGTHDIDRCAEVSERVLAACYKALNDHHVLLEGTSLKPNIVTPGSESKKVTPEVIAEYTVRTLQRTVPQAVPGVMFLSGGQSEEEATLNLNAMNKLETKKPWTLSFSYGRALQQSTLKAWQGKEENVAKAQEVFLARAKGNSEATLGKYQGGAGGADASESLHVKDYKY
Protein: Insecticidal protein LA-a (EC 3.2.1.132) (EC 3.2.1.14) (Latex abundant protein a) (P86799)
Organism: Morus alba (White mulberry)
Function: Has insecticidal activity when consumed by D.melanogaster larvae. Has low chitinase and chitosanase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:20109180}.
Interaction partners:
Sequence:
SEPQXGRDAGGAL
Protein: AT4g12340/T4C9_180 (Copper ion binding protein) (Q9STH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGDFSIQISSKLINQLAEGNDQPKRRAKKTKPKVSPQSKQKTNQDEEKKPNPVAELPMQPPFFFPIPPQGAASTELESIKSVVKESEKVLEKLELQEKNIVREVTERAKDLREKEFKIPEPKPMPCSSDHEAWMKCYKENIGSPLKCSGFVKSFQDCARRSRQQVNPEEK
Protein: Probable Rho-GTPase-activating protein 7 (O94466)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Cell division control protein 15
- LIM domain-containing protein C4F6.12
- Uncharacterized protein C688.07c
- GTP-binding protein rho2
- Septation protein imp2
- Ingression protein fic1
- Probable Rho-type GTPase-activating protein 4
- GTP-binding protein rho1
- Rho-GTPase-activating protein 8
- Uncharacterized protein P22H7.03
Sequence:
MLSAPSSSTTPASPPTSPPNTTSSDDFAVLKEPKVEAILNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANHSLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYNRALDNKNTGDSQKKVGFFKPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTLLNGLTIRPQKPTPTNCGLQHALDNINANTDFVQYVLHASIKHEDNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFPNPSVASPAFPNSSTSNPSTAPASASPLASTLKPSTANDTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPPSSINSNRAASPFRPTSVSPQPSSPTKSLLFGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEDYENDVHAVADLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIKQATIPEISSFSRTIEILIDYCFTIFDYD
Protein: Ubiquitin-like modifier-activating enzyme 5 (Q38EW4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ubiquitin-protein ligase, putative
- Ubiquitin-protein ligase, putative
- E3 ubiquitin-protein ligase TRIP12
- HECT-type E3 ubiquitin transferase
- Ubiquitin-conjugating enzyme E2, putative
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-conjugating enzyme E2, putative
- E2 ubiquitin-conjugating enzyme
Sequence:
MSQDRGKRQVLDATVRDDNPYSRLMALQRMGVVENYEAIRQKSVAIIGAGGVGSVVAEMLTRCGIAKILLFDYDKVELANMNRLFYRPEQQGMSKVAAAKQTLEGINPDTEIVPFDFSITAAEHWQDFADALTKNGGVKPSTPVDLLLCCVDNFQARLTVNYACLLFNIPWMESGVAENAVSGHIQLLLPGVTPCYECCPPLVVATGMPEAKREGVCAASLPTTMGIVAGFLAQNALKYLLNFGTVSEYIGYDAVRDYFPSVTIKANPDCRNATCVEKQREYAERKARLGDAAHPLHNAAKHRTEREAKEREAAKARAAASAKEWGIVVEEHGKDDLSVNTKGDTGGVEYAYGAGGKAEGNAPREDEFVAADSGESLEALMAKMRAM
Protein: Probable cytosolic iron-sulfur protein assembly protein CIAO1 (WD repeat-containing protein 39) (O76071)
Organism: Homo sapiens (Human)
Function: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2. Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23585563}.
Interaction partners:
- Cytosolic iron-sulfur assembly component 2B
- Cytosolic iron-sulfur assembly component 2A
- MMS19 nucleotide excision repair protein homolog
- Cytosolic iron-sulfur assembly component 3
- ADP/ATP translocase 2
- General transcription and DNA repair factor IIH helicase subunit XPD
- Cytosolic Fe-S cluster assembly factor NUBP1
- ADP/ATP translocase 3
- Cytosolic Fe-S cluster assembly factor NUBP2
- DNA polymerase delta catalytic subunit
Sequence:
MKDSLVLLGRVPAHPDSRCWFLAWNPAGTLLASCGGDRRIRIWGTEGDSWICKSVLSEGHQRTVRKVAWSPCGNYLASASFDATTCIWKKNQDDFECVTTLEGHENEVKSVAWAPSGNLLATCSRDKSVWVWEVDEEDEYECVSVLNSHTQDVKHVVWHPSQELLASASYDDTVKLYREEEDDWVCCATLEGHESTVWSLAFDPSGQRLASCSDDRTVRIWRQYLPGNEQGVACSGSDPSWKCICTLSGFHSRTIYDIAWCQLTGALATACGDDAIRVFQEDPNSDPQQPTFSLTAHLHQAHSQDVNCVAWNPKEPGLLASCSDDGEVAFWKYQRPEGL
Protein: Zeta-crystallin (O97764)
Organism: Bos taurus (Bovine)
Function: Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species and enhances their stability. NADPH binding interferes with mRNA binding (By similarity). Has minimal or no quinone reductase activity. Binds strongly to single-stranded DNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- TRPM8 channel-associated factor 1
Sequence:
MATGQKLMRAIRVFEFGGPEVLKLQSDVAVPIPKDHQVLIKVQACGVNPVDTYIRSGTHNIKPLLPYTPGFDVAGIIEAVGESVSAFKKGDRVFTTRTISGGYAEYALAADHTVYTLPEKLDFKQGAAIGIPYFTAYRALLHSACVKPGESVLVHGASGGVGIAACQIARAYGLKVLGTASTEEGQKIVLENGAHKVFNHKEADYIDKIKKSVGEKGVDVIIEMLANVNLSNDLNLLSHGGRVIVVGSRGTIEINPRDTMTKESSIKGVTLFSSTKEEFQQFAAALQAGMEIGWLRPVIGPQYLLEKATQAHENIIHSSGATGKMILLLN
Protein: Insulin-like growth factor-binding protein complex acid labile subunit (ALS) (P35858)
Organism: Homo sapiens (Human)
Function: Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor-binding protein 5
- Insulin-like growth factor-binding protein 6
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein 2
Sequence:
MALRKGGLALALLLLSWVALGPRSLEGADPGTPGEAEGPACPAACVCSYDDDADELSVFCSSRNLTRLPDGVPGGTQALWLDGNNLSSVPPAAFQNLSSLGFLNLQGGQLGSLEPQALLGLENLCHLHLERNQLRSLALGTFAHTPALASLGLSNNRLSRLEDGLFEGLGSLWDLNLGWNSLAVLPDAAFRGLGSLRELVLAGNRLAYLQPALFSGLAELRELDLSRNALRAIKANVFVQLPRLQKLYLDRNLIAAVAPGAFLGLKALRWLDLSHNRVAGLLEDTFPGLLGLRVLRLSHNAIASLRPRTFKDLHFLEELQLGHNRIRQLAERSFEGLGQLEVLTLDHNQLQEVKAGAFLGLTNVAVMNLSGNCLRNLPEQVFRGLGKLHSLHLEGSCLGRIRPHTFTGLSGLRRLFLKDNGLVGIEEQSLWGLAELLELDLTSNQLTHLPHRLFQGLGKLEYLLLSRNRLAELPADALGPLQRAFWLDVSHNRLEALPNSLLAPLGRLRYLSLRNNSLRTFTPQPPGLERLWLEGNPWDCGCPLKALRDFALQNPSAVPRFVQAICEGDDCQPPAYTYNNITCASPPEVVGLDLRDLSEAHFAPC
Protein: PWWP domain-containing protein 1 (Set9-associated factor pdp1) (O59676)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Necessary for DNA damage checkpoint activation. Required for the association of set9 with chromatin and subsequent methylation of H4K20. Associates with H4K20me1 to increase the concentration of set9 on chromatin to perform H4K20me3. H4K20me3 is mainly enriched at heterochromatin and is required for proper heterochromatin assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone-lysine N-methyltransferase set9
- Ribosomal lysine N-methyltransferase 4
- PWWP domain-containing protein 3
- PWWP domain-containing protein2
- Histone acetyltransferase mst2
- Mst2 complex subunit nto1
- Chromatin modification-related protein eaf6
- Protein arginine N-methyltransferase 1
- Protein arginine N-methyltransferase 2
- Ribosomal protein arginine N-methyltransferase rmt3
Sequence:
MNNARTNAKRRRLSSKQGGLSISEGKESNIPSVVEESKDNLEQASADDRLNFGDRILVKAPGYPWWPALLLRRKETKDSLNTNSSFNVLYKVLFFPDFNFAWVKRNSVKPLLDSEIAKFLGSSKRKSKELIEAYEASKTPPDLKEESSTDEEMDSLSAAEEKPNFLQKRKYHWETSLDESDAESISSGSLMSITSISEMYGPTVASTSRSSTQLSDQRYPLSSNFDHRGEAKGKGKQPLKNPQERGRISPSSPLNDQTKALMQRLLFFRHKLQKAFLSPDHLIVEEDFYNASKYLNAISDIPFLNYELITSTKLAKVLKRIAFLEHLENDELYDIRQKCKNLLYSWAMFLPNEPSIKGM
Protein: Heparin cofactor 2 (Heparin cofactor II) (HC-II) (Protease inhibitor leuserpin-2) (Serpin D1) (Q64268)
Organism: Rattus norvegicus (Rat)
Function: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT) (By similarity).
Interaction partners:
- Prothrombin
- Plasminogen
- Fibrinogen gamma chain
- Fibrinogen alpha chain
- Fibrinogen beta chain
- Coagulation factor XIII B chain
- Carboxypeptidase B2
- Tissue factor pathway inhibitor
- Antithrombin-III
- Tissue factor pathway inhibitor
Sequence:
MKHPAYTLLLSLIMSMCAGSKGLAEQLTKENLTVSLLPPNFHKENTVTNDWIPEGEEDDDYLDLEKLLSEDDDYIYVVDAVSPTDSESSAGNILQLFQGKSRIQRLNILNAKFAFNLYRVLKDQATSSDNIFIAPVGISTAMGMISLGLRGETHEEVHSVLHFKDFVNASSKYEVTTIHNLFRKLTHRLFRRNFGYTLQSVNDLYIQKQFPIREDFKAAMREFYFAEAQEADFSDPAFISKANSHILKLTKGLIKEALENTDSATQMMILNCIYFKGAWMNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVIPRKLSGMKTLEAQLTPQVVERWQKSMTNRTREVLLPKFKLEKNYNLVEVLKSMGITKLFNKNGNMSGISDQRIIIDLFKHQSTITVNEEGTQAAAVTTVGFMPLSTQVRFTVDRPFLFLVYEHRTSCLLFMGRVANPAKS
Protein: General amino acid permease AGP1 (Asparagine/glutamine permease) (P25376)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- High-affinity glutamine permease
- Valine/tyrosine/tryptophan amino-acid permease 1
- General amino-acid permease GAP1
- SPS-sensor serine protease component SSY5
- SPS-sensor component PTR3
- Peptide transporter PTR2
- Ammonium transporter MEP2
- Transcription factor STP1
Sequence:
MSSSKSLYELKDLKNSSTEIHATGQDNEIEYFETGSNDRPSSQPHLGYEQHNTSAVRRFFDSFKRADQGPQDEVEATQMNDLTSAISPSSRQAQELEKNESSDNIGANTGHKSDSLKKTIQPRHVLMIALGTGIGTGLLVGNGTALVHAGPAGLLIGYAIMGSILYCIIQACGEMALVYSNLTGGYNAYPSFLVDDGFGFAVAWVYCLQWLCVCPLELVTASMTIKYWTTSVNPDVFVIIFYVLVITINIFGARGYAEAEFFFNCCKILMMTGFFILGIIIDVGGAGNDGFIGGKYWHDPGAFNGKHAIDRFKGVAATLVTAAFAFGGSEFIAITTAEQSNPRKAIPGAAKQMIYRILFLFLATIILLGFLVPYNSDQLLGSTGGGTKASPYVIAVASHGVRVVPHFINAVILLSVLSMANSSFYSSARLFLTLSEQGYAPKVFSYIDRAGRPLIAMGVSALFAVIAFCAASPKEEQVFTWLLAISGLSQLFTWTAICLSHLRFRRAMKVQGRSLGELGFKSQTGVWGSAYACIMMILILIAQFWVAIAPIGEGKLDAQAFFENYLAMPILIALYVGYKVWHKDWKLFIRADKIDLDSHRQIFDEELIKQEDEEYRERLRNGPYWKRVVAFWC
Protein: Calcium-dependent protein kinase 30 (EC 2.7.11.1) (Calcium-dependent protein kinase isoform CDPK1a) (AtCDPK1a) (Q9SSF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger. May be a positive regulator controlling stress signal transduction. Acts as a calcium sensor involved in the hormone-signaling pathways.
Subcellular location: Membrane; Lipid-anchor.
Interaction partners:
- Protein NLP7
- Protein NLP6
- Respiratory burst oxidase homolog protein F
- Probable respiratory burst oxidase homolog protein I
- Respiratory burst oxidase homolog protein E
- Respiratory burst oxidase homolog protein D
- Respiratory burst oxidase homolog protein B
Sequence:
MGNCIACVKFDPDNSKPNQKKKPPRGRQRNPYDDPDGLRTHAPLRVIPMSHQSQISDKYILGRELGRGEFGITYLCTDRETREALACKSISKRKLRTAVDVEDVRREVTIMSTLPEHPNVVKLKATYEDNENVHLVMELCEGGELFDRIVARGHYTERAAATVARTIAEVVRMCHVNGVMHRDLKPENFLFANKKENSALKAIDFGLSVLFKPGERFTEIVGSPYYMAPEVLKRNYGPEVDVWSAGVILYILLCGVPPFWAETEQGVALAILRGVLDFKRDPWSQISESAKSLVKQMLEPDSTKRLTAQQVLDHPWIQNAKKAPNVPLGDIVRSRLKQFSMMNRLKKKALRVIAEHLSIQEVEVIRNMFTLMDDDNDGKISYLELRAGLRKVGSQLGEPEIKLLMEVADVNGNGCLDYGEFVAVIIHLQKMENDEHFRQAFMFFDKDGSGYIESEELREALTDELGEPDNSVIIDIMREVDTDKDGKINYDEFVVMMKAGTDWRKASRQYSRERFKSLSLNLMKDGSMHLHDALTGQSIAV
Protein: RING finger protein 44 (Q7L0R7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRPWALAVTRWPPSAPVGQRRFSAGPGSTPGQLWGSPGLEGPLASPPARDERLPSQQPPSRPPHLPVEERRASAPAGGSPRMLHPATQQSPFMVDLHEQVHQGPVPLSYTVTTVTTQGFPLPTGQHIPGCSAQQLPACSVMFSGQHYPLCCLPPPLIQACTMQQLPVPYQAYPHLISSDHYILHPPPPAPPPQPTHMAPLGQFVSLQTQHPRMPLQRLDNDVDLRGDQPSLGSFTYSTSAPGPALSPSVPLHYLPHDPLHQELSFGVPYSHMMPRRLSTQRYRLQQPLPPPPPPPPPPPYYPSFLPYFLSMLPMSPTAMGPTISLDLDVDDVEMENYEALLNLAERLGDAKPRGLTKADIEQLPSYRFNPDSHQSEQTLCVVCFSDFEARQLLRVLPCNHEFHTKCVDKWLKANRTCPICRADASEVPREAE