wanglab/gogpt-training-data huggingface dataset:
Protein: Protein-glutamine gamma-glutamyltransferase E (EC 2.3.2.13) (Transglutaminase E) (TG(E)) (TGE) (TGase E) (Transglutaminase-3) (TGase-3) [Cleaved into: Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain; Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain] (Q08188)
Organism: Homo sapiens (Human)
Function: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27866708}.
Interaction partners:
- Loricrin
- Cystatin-M
- Suprabasin
- Legumain
- Caspase-14
- Filaggrin-2
- Filaggrin
- Involucrin
- Cornulin
- Corneodesmosin
Sequence:
MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVSTGPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQGGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQFEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGTYTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSAHDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQERSQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIGRYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQEPSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSATMSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLEVLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFDILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE
Protein: Uncharacterized protein YHL026C (P38740)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative uncharacterized protein YML083C
- Putative cystathionine gamma-synthase YML082W
Sequence:
MKSSEPAPATPTGFRNSIWFIIFYLFVIQALGSAIISGGIEFAIAYAMYHSRVDLITLWAFPHTISGDCALSLFIQVGLTWASEEILVGFDDYKRPVFRLNKWITKPSPLKTESNEEIPPPKKRFIVDYFESKDNVVAKQNTLYHKHNWLFGYLEVNRGIIPKGKEATLKGFLTSQFIHDSTQSKFMNFIEWFVQKFIRSMILAIAMFIVIWPVTMGILAGIGHKVGSHDYYFNDYPLPQVMKLIYAVVIAFVCTPVAIIVIVLRNQFHEELYYEGLANGTLQQDQEVCSTGNRSSGSTDQDISTTKQQSQEAVA
Protein: A-type potassium channel modulatory protein DPP6 (DPPX) (Dipeptidyl aminopeptidase-like protein 6) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI) (P46101)
Organism: Rattus norvegicus (Rat)
Function: Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2. Has no dipeptidyl aminopeptidase activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12575952}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P42658}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- A-type potassium channel modulatory protein KCNIP1
- Potassium voltage-gated channel subfamily A member 4
- Voltage-gated potassium channel KCNC1
- A-type voltage-gated potassium channel KCND1
- IgLON family member 5
- A-type potassium channel modulatory protein KCNIP2
- Leucine-rich glioma-inactivated protein 1
- Major prion protein
- Calsenilin
Sequence:
MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDAGSKPLGPQAQAVAPRERGGAGGRPRFQYQARSDCDEEDELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDTSLSQKKKVTVEDLFSEDFKIHDPEAKWISDKEFIYRERKGSVILRNVETNNSTVLIEGKKIESLRAIRYEISPDKEYALFSYNVEPVYQHSHTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKSHIAHWWSPDGTRLAYATINDSRVPLMELPTYTGSVYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFVRAIPQGGRGKFYHITVSSSQPNSSNDNIQSITSGDWDVTEILTYDEKRNKLYFLSTEDLPRRRHLYSANTVDDFNRQCLSCDLVENCTYVSASFSHNMDFFLLKCEGPGVPTVTVHNTTDKRRMFDLEANEQVQKAIYDRQMPKIEYRKIEVEDYSLPMQILKPATFTDTAHYPLLLVVDGTPGSQSVSERFEVTWETVLVSSHGAVVVKCDGRGSGFQGTKLLHEVRRRLGFLEEKDQMEAVRTMLKEQYIDKTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKLAHRVSALEDQQFLIIHATADEKIHFQHTAELITQLIKGKANYSLQIYPDESHYFHSVALKQHLYRSIIGFFVECFRIQDKLPTATAKEDEEED
Protein: Beta-crystallin B1 (Beta-B1 crystallin) [Cleaved into: Beta-crystallin B1B] (P02523)
Organism: Rattus norvegicus (Rat)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Filensin
- Phakinin
- Alpha-crystallin B chain
- Gap junction alpha-3 protein
- Gap junction alpha-8 protein
- Beta-crystallin A3
- Gamma-crystallin A.
Sequence:
MSQVAKAAATTAVNPGPDGKGKGTPSTGTAPAPGPTPVPASVPRPAAKVGELPPGSYRLVVFEQENFQGRRVEFSGECLNLGDRGFDRVRSLIVLSGPWVAFEQSAFRGEMFVLEKGEYPRWDTWTSSYRSDRLMSFRPIRMDSQEHKICLFEGANFKGNTMEIQEDDVPSLWVYGFCDRVGSITVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQAVRRLRDRQWHQEGCFPVLTAEPPK
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 3 (BLOC-1 subunit 3) (A8JNV4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- SNAPIN protein homolog
- Dysbindin protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- BLOC-2 complex member HPS5 homolog
- Hermansky-Pudlak syndrome 4, isoform A
- GH27401p
- Uncharacterized protein, isoform A
Sequence:
MADLVSGEASESDEELQEKNKIFAAEISGEASEEDDEDIYEQGRSSNQVNSTASIYRNNLLQRKLIENNIAIWRSLTAFTRSFVLSASKQLVTTDQMLIKSQHSLQSAHTSLQQAQKNAQDLQNRVADVITSNFLPHISIQKAT
Protein: Regulator of chromosome segregation (A0A0H2ZKY7)
Organism: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Function: Required for cell division and chromosome segregation. Binds to DNA and is involved in segregating the origin of replication (oriC) region to new daughter cells (By similarity). When the nucleoid is not properly segregated, involved in blocking the cell division to protect the nucleoid against premature truncation by the newly forming septum, a function which is dependent on CpsD and its autophosphorylation level.
Subcellular location: Cytoplasm, nucleoid {ECO:0000250|UniProtKB:Q8DQ15}. Cell membrane {ECO:0000250|UniProtKB:Q8DQ15}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8DQ15}. Note=Localizes at mid-cell at first and then at the future site of division as the cell elongates. Forms one or two bright foci per cell mostly around mid-cell of small cells. Localizes toward the center of the daughter cell as the cell elongates. The bright foci mostly co-localize with origin of replication (oriC). During the cell cycle, very faint, but highly dynamic foci are homogeneously distributed all around the cell periphery (By similarity). Co-localizes with CpsD at mid-cell only at the early stage of the cell cycle (PubMed:31182798). {ECO:0000250|UniProtKB:Q8DQ15, ECO:0000269|PubMed:31182798}.
Interaction partners:
Sequence:
MSIEMTVSEIAEVLGLSRQAINNRVKELPEEDTDKNDKGVTVVTRSGLIKLEEIYKKTIFEDEPVSEDVKQRELMEILVDEKNAEILRLYEQLKAKDRQLSEKDEQMRIKDRQIAEKDKQLDQQQQLTLQAMKDQENLKLELDQAKEEVQSTKKGFFARLFGG
Protein: AT17665p (Q8IHB1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTDAQDTVAPKTSSTKEVQCQHSGALDEPHVEELALPGPAPLAMPKSGRVGIFNAEDFLSRAQLNDKINNILRSPTKAPNGVRQRSVFTNNNPSPQATMRFVSSMNSPLAPRMSSLSLTGGVKRGLERGNSSSSMGNSASVGTSTSVLAKECSSQTNSCGRSYMNMGMHASSHSGFGVLPQSGAGYETMGWNMDAGNITRSGKSLTGRFNSGYGYEVDGAYCMPQAHHTQQFPSPMPPPPFAMDRVSSRTFEFENNTPPPCPGSGPIAMSNGTIQLRLREGVRIDMTLDKAVRVLNQRSMVAAALSRNCSNSALIHPNGRILQSGSKVEIVTYDGMKANNFVRYAKMWYKGVSFTSESCALIYLVDTAGTRTTTDTFTDLTKDYTLAVFYDDSRHGPSFVSDAHDVIANSTYNCAEDGTEVYDINGFRITQAADGLVKVSRQHSKCLIRTSPGNGSATLTTTGIHCTASLGKTSHLFVRRNEKRMHFDGSCFIVRNAGHSAGFNENNLLIVY
Protein: PC4 and SFRS1-interacting protein (Lens epithelium-derived growth factor) (Q812D1)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O75475}.
Interaction partners:
- Menin
- Histone-lysine N-methyltransferase
- Retinoblastoma-binding protein 5
- Pogo transposable element with ZNF domain
- Serine/arginine-rich splicing factor 1
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Histone-lysine N-methyltransferase 2B
- Structural maintenance of chromosomes protein 3
Sequence:
MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQVSTKQSNASSDVEAEEKETSVSKEDTDQEEKASNEDVTKAADITTPKAARRGRKRKAEKQVDTEEAGVVTAATASNVKASPKRGRPAATEVKIPKPRGRPKVVKQPCPSESDMVIDEDKSKKKGPEEKPPKKQLKKEEEGQKEEEKPRKEPDKKEGKKEVESKRKNLAKPGVTSTSDSEEDDDQEGEKKRKGGRHFQAAHRRNMLKGQHEKEAADRKRKQEEQMETEQQTKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGTKSLNGGSDAQESNHPQHNGDSAEESKDSREAGSKTKTPGEEREAEVSLKESTLDN
Protein: Senescence-associated and QQS-related protein (Q9C7W0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Disease resistance protein RML1B
- Protein QUA-QUINE STARCH
- Dirigent protein 11
- Neurofilament heavy protein
- Disease resistance protein RML1A
- Cytochrome P450 86A7
Sequence:
MSFRKVEKKPTEMGRNMTHEKSDSDSDNEGAPMTVGGYTEFVARSDSDWDEPVYSGKARSNYNLTGTAKGTGPINSFSRKHFPNY
Protein: E3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) (ADP-ribosylation factor domain-containing protein 1) (GTP-binding protein ARD-1) (RING finger protein 46) (RING-type E3 ubiquitin transferase TRIM23) (Tripartite motif-containing protein 23) (P36406)
Organism: Homo sapiens (Human)
Function: Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28871090}. Endomembrane system {ECO:0000269|PubMed:9671726}. Golgi apparatus membrane {ECO:0000269|PubMed:9671726}. Lysosome membrane {ECO:0000269|PubMed:9671726}. Note=Membrane-associated with the Golgi complex and lysosomal structures.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Cytohesin-2
- E2 ubiquitin-conjugating enzyme
- Cytohesin-1
- Ubiquitin-conjugating enzyme E2 E1
- POTE ankyrin domain family member B2
Sequence:
MATLVVNKLGAGVDSGRQGSRGTAVVKVLECGVCEDVFSLQGDKVPRLLLCGHTVCHDCLTRLPLHGRAIRCPFDRQVTDLGDSGVWGLKKNFALLELLERLQNGPIGQYGAAEESIGISGESIIRCDEDEAHLASVYCTVCATHLCSECSQVTHSTKTLAKHRRVPLADKPHEKTMCSQHQVHAIEFVCLEEGCQTSPLMCCVCKEYGKHQGHKHSVLEPEANQIRASILDMAHCIRTFTEEISDYSRKLVGIVQHIEGGEQIVEDGIGMAHTEHVPGTAENARSCIRAYFYDLHETLCRQEEMALSVVDAHVREKLIWLRQQQEDMTILLSEVSAACLHCEKTLQQDDCRVVLAKQEITRLLETLQKQQQQFTEVADHIQLDASIPVTFTKDNRVHIGPKMEIRVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVVDSSHRDRISEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEITELLSLHKLCCGRSWYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA
Protein: GH15647p (Q961M6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLDIQVPRIAACYSLNTASVDVLAPDMAKEATTSAAATGSTHGSTDTNSANVCTFYNDVVKNMNTLVSKKMQDIDLALQRESKIIPSPNEEILCIIKWTNFLAAFESGFVFIWDVQMKTHNFLAATTTNLMPSVCGAIAVVNTKFAPDPQALPLMARMLMNSMRNEKTNRLAVVMQGRQSFWLVKGFLRHMQGNACTKPTPMTHPLLTKKINVLCSLLVKQRVRENEKKTLGDGSGAPYEVLAGDVSPQTSLLMKNRSRDLKRKSQADERLLPSGPSMTKSSKPSAGGYPIAASVATSTTSAFASSSGKSTPVCTAKTNSASTKNKSSATGIRSNIEFRKVNHNDVDELQIPELHQTDHRWVVLDIFDDFSHIFVPSFSDMISLTRIHSVMQVAEERQKVVKLQFFPNAPYDAFVTPSSKKKIYFGPLSLDMPPPVLVLLQSVDRKMMLREVYQREHSIPVQRHRRSMAFWVLQINGQVHFEIDTESTAKLAAQQKNAIGTPPGLNVLKIPSQLSVEIEKNQDEVPPVVVIDSDEEDDDGERQLVIDEQDDEQAETDVKQEVERTGFTIQTLPSSGALQITISDSAETSSHPAKDVNTCHFSGGFMPFIANVPAKFGETAPTTQFLTPQVQVTTSQSGPETLTSSSSSHLPASKSAYPKINESLQELFSSGVPPGGITITKVDSQEKTLPNETVQVVKNKKSIAITGIHKQVTKAASSTATVTAARAPVVKPQSTSVSKVAPPIRPGATTQPKTLVRLYPKPALAAGRKSLPANAKTPVATPRQSQPVACDKPPLVSGSTLPALVEPSARKSLPSKPLAAGEHLRPRQSLPAKVTANPPAAARPDAASTSAQNLTNVSKAQLAKEEICYGIMVAKDLPRFRAKVEGSDFMIKIPEHGVFRFKTFGLAASFLSRHVAKDPKLKQFLPAEWKFHPLEQFNKQVPSRSQQSPAAIVIED
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin a2 (Q6DUH4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATPTDPAAMPHPGPSPGPGPSPGPILGPSPGPGPSPGSVHSMMGPSPGPPSVSHPMSTMGSADFPQEGLHQLHKPMDGIHDKGIVEGVHCGSMKGTSMRPPHPGVGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPISGGGPTPPQMPPSQPGTLIPGDLQAMNQPDRGPSPFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQGKRTLPGIQQQQQQQQQQQQQQQQQQPQQPQQPQQQTQAQPQQQQQQQQQPPTLVSYNRPSGPGQELLMTAQNTQRKLSAPAPSGRPSPAPPAATQPTATAVPGPSVQEPAPGQPSPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRIQELESLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTTLETALNSKAYKRSKRQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAYLLQQTDEYVANLTNLVWEHKQAQAAKEKKKRRRRRKKAEENAEGGEPALGPDGEPIDESSQMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPRSDSEESESDYEEEDEEEESSRQETEEKILLDPNSKEVSEKDARQIIETAKQDVDDEYSMQYSARGSQSYYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGPGKTIQTIALITYLMEHKGLNGPYLIIVPLSTLSNWTYEFDKWAPSAVKISYKGTPAMRRSLVPQLRSGKFNALLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLKKEVESQLPEKVEYVIKCDMSALQKILYRHMQAKGILLTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHLGYSNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEENEEEDEVPDDETLNQMIARREEEFDLFMRMDMDRRREDARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWLRAIEDGNLEEMEEEVRLKKRKRRRNVDKDPVKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDRCNVEKVPCNSQLEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKIAKEEESEEESNEEEEEEDEEESEAEAKSVKVKIKLNKKEEKGRDTGKGKKRPNRGKAKPVVSDFDSDEEQDENEQSEASGTDDE
Protein: Putative DNA repair helicase RadD (EC 3.6.4.12) (P33919)
Organism: Escherichia coli (strain K12)
Function: RadD contains helicase motifs, suggesting it may be a helicase, although that activity has not been observed (Probable). In combination with RadA is important in repair of double-strand DNA breaks (DSB). Has DNA-independent ATPase activity that is stimulated by single-stranded DNA-binding protein SSB. ATPase is stimulated by a peptide with the last 10 residues of SSB, but not when the peptide's last Phe residue is missing. Binds ssDNA; binding is slightly better in the presence of nucleotides. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds to DNA structures with 3 branches that resemble replication forks.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- ATP-dependent DNA helicase DinG
- ATP-dependent DNA helicase YoaA
- 3-ketoacyl-CoA thiolase FadA
- RNA polymerase-associated protein RapA
- DNA polymerase I
- Single-stranded DNA-binding protein
- DNA-directed RNA polymerase subunit beta'
Sequence:
MIFTLRPYQQEAVDATLNHFRRHKTPAVIVLPTGAGKSLVIAELARLARGRVLVLAHVKELVAQNHAKYQALGLEADIFAAGLKRKESHGKVVFGSVQSVARNLDAFQGEFSLLIVDECHRIGDDEESQYQQILTHLTKVNPHLRLLGLTATPFRLGKGWIYQFHYHGMVRGDEKALFRDCIYELPLRYMIKHGYLTPPERLDMPVVQYDFSRLQAQSNGLFSEADLNRELKKQQRITPHIISQIMEFAATRKGVMIFAATVEHAKEIVGLLPAEDAALITGDTPGAERDVLIENFKAQRFRYLVNVAVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGKTDCLILDYAGNPHDLYAPEVGTPKGKSDNVPVQVFCPACGFANTFWGKTTADGTLIEHFGRRCQGWFEDDDGHREQCDFRFRFKNCPQCNAENDIAARRCRECDTVLVDPDDMLKAALRLKDALVLRCSGMSLQHGHDEKGEWLKITYYDEDGADVSERFRLQTPAQRTAFEQLFIRPHTRTPGIPLRWITAADILAQQALLRHPDFVVARMKGQYWQVREKVFDYEGRFRLAHELRG
Protein: Cytochrome c1, heme protein, mitochondrial (EC 7.1.1.8) (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome c oxidoreductase cytochrome c1 subunit) (Cytochrome c-1) (P07143)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c isoform 1
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 1
Sequence:
MFSNLSKRWAQRTLSKSFYSTATGAASKSGKLTQKLVTAGVAAAGITASTLLYADSLTAEAMTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFVFNPPKPRK
Protein: Sensor histidine kinase CusS (EC 2.7.13.3) (P77485)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Acts as a copper/silver ion sensor. Activates CusR by phosphorylation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcriptional regulatory protein CusR
- Cation efflux system protein CusB
- Cation efflux system protein CusF
- Cation efflux system protein CusC
- Cation efflux system protein CusA
- Transcriptional regulatory protein HprR
- DNA-binding dual transcriptional regulator OmpR
- Transcriptional regulatory protein CpxR
- Transcriptional regulatory protein BaeR
- Multicopper oxidase CueO
Sequence:
MVSKPFQRPFSLATRLTFFISLATIAAFFAFAWIMIHSVKVHFAEQDINDLKEISATLERVLNHPDETQARRLMTLEDIVSGYSNVLISLADSQGKTVYHSPGAPDIREFTRDAIPDKDAQGGEVYLLSGPTMMMPGHGHGHMEHSNWRMINLPVGPLVDGKPIYTLYIALSIDFHLHYINDLMNKLIMTASVISILIVFIVLLAVHKGHAPIRSVSRQIQNITSKDLDVRLDPQTVPIELEQLVLSFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLNLADEVGKVFDFFEALAEDRGVELRFVGDKCQVAGDPLMLRRALSNLLSNALRYTPTGETIVVRCQTVDHLVQVIVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDARGTRFVITLPA
Protein: Dynamin-like protein ARC5 (EC 3.6.5.5) (Dynamin-related protein 5B) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 5) (AtARC5) (Q84N64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mechanochemical GTPase component of both plastid and peroxisome division machinery. Required for the last steps of plastid division specifically in mesophyll-cell, when the narrow isthmus breaks, facilitating the separation of the daughter plastids. Necessary for peroxisome activities. Seems to influence stromule (stroma-filled tubular extensions of the plastid envelope membrane) length and frequency.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32005784}. Plastid, chloroplast outer membrane {ECO:0000269|PubMed:25736058, ECO:0000269|PubMed:32005784}; Peripheral membrane protein {ECO:0000269|PubMed:32005784}. Peroxisome {ECO:0000269|PubMed:20179140}. Cytoplasm, cytosol {ECO:0000269|PubMed:32005784}. Note=Plastid equatorial positioning (in a discontinuous ring shape) mediated by PDV2 in complex with ARC6 and dissociation from the outer envelope membranes (OEMs) is triggered by PDV1; this localization with OEMs is repressed by phosphatidylinositol 4-phosphate (PI4P) (PubMed:25736058, PubMed:32005784). Dynamic subunit exchange within chloroplastic DRP5B rings with a cytosolic pool during chloroplast membrane constriction in a GTPase activity-dependent manner (PubMed:32005784). {ECO:0000269|PubMed:25736058, ECO:0000269|PubMed:32005784}.
Interaction partners:
- Plastid division protein PDV1
- Plastid division protein PDV2
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 3
- Mitochondrial fission 1 protein A
- Cell division protein FtsZ homolog 1, chloroplastic
- Dynamin
- Plastid division protein CDP1, chloroplastic
- Cell division topological specificity factor homolog, chloroplastic
- Mitochondrial fission 1 protein B
Sequence:
MAEVSAKSVTVEEMAEEDDAAIEERWSLYEAYNELHALAQELETPFEAPAVLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQFPLCHLGSDDDPSVSLPKSLSQIQAYIEAENMRLEQEPCSPFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNRALQVQARAVEALVRAKMQHKEFIILCLEDSSDWSIATTRRIVMQVDPELSRTIVVSTKLDTKIPQFSCSSDVEVFLSPPASALDSSLLGDSPFFTSVPSGRVGYGQDSVYKSNDEFKQAVSLREMEDIASLEKKLGRLLTKQEKSRIGISKLRLFLEELLWKRYKESVPLIIPLLGKEYRSTVRKLDTVSKELSSLDEAKLKERGRTFHDLFLTKLSLLLKGTVVAPPDKFGETLQDERTQGGAFVGTDGLQFSHKLIPNAGMRLYGGAQYHRAMAEFRFLVGAIKCPPITREEIVNACGVEDIHDGTNYSRTACVIAVAKARETFEPFLHQLGARLLHILKRLLPISVYLLQKEGEYLSGHEVFLKRVASAFNSFVESTEKSCRDKCMEDLASTTRYVTWSLHNKNRAGLRQFLDSFGGTEHNTTSGNAIGFSLPQDALGGTTDTKSRSDVKLSHLASNIDSGSSIQTTEMRLADLLDSTLWNRKLAPSSERIVYALVQQIFQGIREYFLASAELKFNCFLLMPIVDKLPALLREELENAFEDDLDSIFDITNLRQSLDQKKRSTEIELRRIKRIKEKFRVMNEKLNSHEFAQNLKAPSVQH