wanglab/gogpt-training-data huggingface dataset:
Protein: Myomesin 1 (A0A0G2K5P5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSLPFYQRSHQHYDLSYRNKDLHTTMSHYQQEKKRSAVYTHGSTAYSSRSSAAHRQESEALRQASAASYQQQASKAYSLGTSSSQHYQGSEVSRKTASSYDYGYSHGLTDSSLLLEDYSSRLSPQTKRAKRSLLSGEETGNLSGNYMVPIYSGRQVHISGIRDSEEERIKEAAAYIAQRTLLESEEAIMASKQSTASKQSTASKQSIASKQSTASKQSTASKQSTASKQATSTFQQEETFERKSRNISIREKAEELSLRKTLEETQAYHGKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSVAGWPEPRLTWYKNQVPINVHANPEKYIIESRYGMHTLEISKCDFEDTAQYRASAMNVQGEVSAYASVVVKRYKGELDDSLLRGGVSMPLSFAVTPYGYASKFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHVQPEVQWYRNGAPVSPSKWVQPHWSGDRATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVVSLDANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDTWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKTGIGLPSRVSEPVAALDPAEKARLKSRPSAPWTGQIIVTEEEPTEGVIPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCDVGTENWQRVNTELPVKSPRFALFDLVEGKSYRFRVRCSNSAGVGEPSESTEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESKDAKELVGYYIESSVVGSGQWEPCNNNPVKGSRFTCHGLTTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIGGGVSPDVWPQLSDTPGGLTDSGGAMSGASPPTSQKDALPSSKPNKPSPPSSPSNRGQKEVSKVNGSVQEELSPPSMEVASKEQSKSGPPEKKKDPVAVPSPPYDITCLESFRDSMVLGWKQPDKTGGAEITGYYVNYREVVGGVPGKWREANIKAVSDAAYKISELKENTVYQFQVSAMNIAGLGAPSAVSECFKCEEWTIAVPGPPHSLKLSEVRKNSLVLQWKPPVYSGRTPVTGYFVDLKEASAKDDQWRGLNEAAIPNKYLRVQGLKEGISYVFRVRAINQAGVGKPSDLAGPVVAETRPGTKEVVVNVDDDGVISLNFECDQMTPKSEFVWSKDYVPSEDSPRLEVESKGNKTKMVFKDLGPDDLGTYSCDVTDTDGIASSYLIDEEEMKRLLALSQEHKFPTVPTKSELAVEILEKGQVRFWMQAEKLSGNAKVNYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQIQDGKATGHSTLVLIGDVYKKLQKEAEFQRQEWIRKQGPHFAEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGFYEVILKDDRGKDKSRLKLVDEAFQDLMTEVCRKIALSATDLKIQSTAEGIRLYSFVCYYLDDLKVNWSHNGTGIKYTDRVKSGVTGEQIWLQINEPTQNDKGKYVMELFDGKTGHQKSVDLSGQAFDEAFAEFQRLNGFITFLPVTLSLQALNLTCNVWGDPTPEVSWLKNEKPLTSDDHCSLKFEAGKTAFFTISGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEEARKGASEPPKGNQKSK
Protein: Cytochrome c biogenesis B (Q2F954)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRRLFLEQFHKQIFPSTPITSFFLFLSYIVVTPLMIGFEKDFSCHSHLGSIRIPLLFPFPPEPFSRNDKESGTLELYYLSAYCLPKILLLQLVGHRVIQISRVFCAFPMLQLPYQFDRSGMDRLNILLGSPVLTLLCGIHSGSALGITSSSGWNSSQNPTTSPTLLPPTVSRTSIETEGFHVLSSIGYSSPFVSLYPISVSISSQD
Protein: Neprilysin (EC 3.4.24.11) (Atriopeptidase) (Enkephalinase) (Neutral endopeptidase 24.11) (NEP) (Neutral endopeptidase) (Skin fibroblast elastase) (SFE) (CD antigen CD10) (P08049)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (By similarity). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08473}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Angiotensin-converting enzyme
- Lysosomal Pro-X carboxypeptidase
- Insulin-degrading enzyme
- Meprin A subunit
- Xaa-Pro aminopeptidase 2
- Meprin A subunit
- CD19 molecule
- Angiotensinogen
- Amyloid-beta precursor protein
- BCL6 transcription repressor
Sequence:
MGRSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTVIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCVNETAIDSRGGQPLLKLLPDVYGWPVATQNWEQTYGTSWSAEKSIAQLNSNYGKKVLINFFVGTDDKNSMNHIIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMIAVAKLIRQEEGLPIDENQISVEMNKVMELEKEIANATTKSEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWSNFTNEIMSTVNINIPNEEDVVVYAPEYLIKLKPILTKYFPRDFQNLFSWRFIMDLVSSLSRTYKDSRNAFRKALYGTTSESATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWITGAAIVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGIDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGSLQNSVEFSEAFQCPKNSYMNPEKKCRVW
Protein: Ras-related protein Rab-28 (P51158)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23746546}. Note=Expressed in the basal body and ciliary rootlet of the photoreceptors.
Interaction partners:
Sequence:
MSDSEEESQDRQLKIVVLGDGTSGKTSLATCFAQETFGKQYKQTIGLDFFLRRITLPGNLNVTLQVWDIGGQTIGGKMLDKYIYGAQGILLVYDITNYQSFENLEDWYSVVKTVSEESETQPLVALVGNKIDLEHMRTVKPDKHLRFCQENGFSSHFVSAKTGDSVFLCFQKVAAEILGIKLNKAEIEQSQRVVKADIVNYNQEPMSRTVNPPRSSMCAVQ
Protein: Matrilin-3 (O15232)
Organism: Homo sapiens (Human)
Function: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O35701}.
Interaction partners:
- Secreted frizzled-related protein 3
- Asporin
- Collagen alpha-3
- Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
- Cartilage oligomeric matrix protein
- Collagen alpha-2
- Sulfate transporter
- Collagen alpha-1
- Growth/differentiation factor 5
- Aggrecan core protein
Sequence:
MPRPAPARRLPGLLLLLWPLLLLPSAAPDPVARPGFRRLETRGPGGSPGRRPSPAAPDGAPASGTSEPGRARGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEEHVFYVETYGVIEKLSSRFQETFCALDPCVLGTHQCQHVCISDGEGKHHCECSQGYTLNADKKTCSALDRCALNTHGCEHICVNDRSGSYHCECYEGYTLNEDRKTCSAQDKCALGTHGCQHICVNDRTGSHHCECYEGYTLNADKKTCSVRDKCALGSHGCQHICVSDGAASYHCDCYPGYTLNEDKKTCSATEEARRLVSTEDACGCEATLAFQDKVSSYLQRLNTKLDDILEKLKINEYGQIHR
Protein: Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1] (O08532)
Organism: Mus musculus (Mouse)
Function: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P54289}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent L-type calcium channel subunit beta-3
Sequence:
MAAGCLLALTLTLFQSGLIGPSSEEPFPSPVTIKSWVDKMQEDLVTLAKTASGVTQLADIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLAMEAEKVQAAHQWREDFASNEVVYYNAKDDLDPERNESEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSALDEVFKRNRDEDPTLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFAKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNVTGQSENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNVQNPKSQEPVTLDFLDAELENEIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYSFYYIKAKLEETITQARYSETLKPDNFEESGYTFIAPREYCNDLKPSDNNTEFLLNFNEFIDRKTPNNPSCNTDLINRILLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVELYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSMMRHLVNISLYAFNKSYDYQSVCDPGAAPKQGAGHRSAYVPSIADILQIGWWATAAAWSILQQLLLSLTFPRLLEAVEMEEDDFTASLSKQSCITEQTQYFFKNDTKSFSGLLDCGNCSRIFHVEKLMNTNLVFIMVESKGTCPCDTRLLMQAEQTSDGPDPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWSIFGLQFILLWLVSGSRHYLL
Protein: Interleukin-5 (IL-5) (B-cell growth factor II) (BCGF-II) (Cytotoxic T-lymphocyte inducer) (Eosinophil differentiation factor) (T-cell replacing factor) (TRF) (P04401)
Organism: Mus musculus (Mouse)
Function: Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils. Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation. Mechanistically, exerts its biological effects through a receptor composed of IL5RA subunit and the cytokine receptor common subunit beta/CSF2RB. Binding to the receptor leads to activation of various kinases including LYN, SYK and JAK2 and thereby propagates signals through the RAS-MAPK and JAK-STAT5 pathways respectively (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:32211550}.
Interaction partners:
- Cytokine receptor common subunit beta
- Interleukin-5 receptor subunit alpha
- Interleukin-2
- Interleukin-3
- Interleukin-1 beta
- Interleukin-7
- Interleukin-9
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-13
- Interleukin-4
Sequence:
MRRMLLHLSVLTLSCVWATAMEIPMSTVVKETLTQLSAHRALLTSNETMRLPVPTHKNHQLCIGEIFQGLDILKNQTVRGGTVEMLFQNLSLIKKYIDRQKEKCGEERRRTRQFLDYLQEFLGVMSTEWAMEG
Protein: Probable cysteine--tRNA ligase (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) (Q09860)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Putative glycine--tRNA ligase
- Putative leucine--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase C19C7.06
- Serine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Tryptophan--tRNA ligase, cytoplasmic
Sequence:
MSTRNPAQSHWGVPKGQRTELYVYNTLTHSKVPFVSNGSNLTWYCCGPTVYDASHMGHARNYVTTDILRRILQSYFGYNITFVQNVTDIDDKIILRARQQYLFEEYKKQQGTNKSHSEAREKVTEAWFAYAKKNLPEPPSSMSEWPQWLASHDIPTLAINNPKLPMHVDALKSALDALQVSEASEIISLDGFWPKVQDVLVPLLDAELGSTVTDPAIFRKLAAYWEDDFNKDMANLNVLPPTAVTRVSEYVPEIVDFVQRIIDRGYAYPVTDGSVYFDTEAFEKGGHFYAKLEPWNKGNRELIAEGEGSLAALTGKKRPGDFALWKASKPGEPSWDSPWSKGRPGWHIECSVMASALLGSNIDIHSGGIDLAFPHHDNELAQSEAYFDCPQWVNYFFHAGHLHIEGQKMSKSLKNFITIKEILKKFTPRQLRLAFLLQQWNTQLDFKETLLAYVLNIEQALENFFRTVRALMNETEGVSANGGHVPEKFDKLEIELLEKFQQTQQNTHLALCDSFNTPLVMQHIDNLVTQANIYIREVGQQPCSRLLGQIASWITSMLQIFGLDENGHPNAVGWSSSKGSSSENTDAMPYIRAVSSFRDRVRELCIAKASSQEILKACDIFRDYDMAALGVSFNDRPQGSALVKLVDAEELIAAREQKLEEERAKQAKKAQAKAEQEKKQVERVMKGKTSPSEMFKMFKEYLSFDEAGLPTKMRGEDGSEIDVPKSRKKKLQKEYAQQEKLHKEYLSYIESNKS
Protein: Uncharacterized protein At5g43822 (Q6NPG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEAVIRKWQQKFRKGKEEMEKWEALQVRWVSLFRNASSIIQRLQEMQNHGSYGALRCLKGIEDAVVQQQMGQLESLLRSMKNVMEEFWGCVLTFEKLHRDGLQLREIESSKRRVEERIGVKPCITDCLEGLSILYDMHQSEYHLKSSILSVLSCLILKPSPGDLNALQYLVVDQPNIPKDEVQHIFDVIFAEEIK
Protein: V-type proton ATPase subunit c4 (V-ATPase subunit c4) (V-type proton ATPase 16 kDa proteolipid subunit c4) (V-ATPase 16 kDa proteolipid subunit c4) (Vacuolar H(+)-ATPase subunit c isoform 4) (Vacuolar proton pump 16 kDa proteolipid subunit c4) (Vacuolar proton pump subunit c4) (P59229)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast.
Interaction partners:
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- ATP synthase subunit b, chloroplastic
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit e2
- V-type proton ATPase subunit e1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B1
Sequence:
MASSGFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE
Protein: 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) (5,10-methenyl-tetrahydrofolate synthetase) (MTHFS) (Methenyl-THF synthetase) (Q9D110)
Organism: Mus musculus (Mouse)
Function: Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10-methenyltetrahydrofolate (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- C-1-tetrahydrofolate synthase, cytoplasmic
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Formimidoyltransferase-cyclodeaminase
- 5-formyltetrahydrofolate cyclo-ligase
- Serine hydroxymethyltransferase, cytosolic
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
Sequence:
MAAVTVNSAKRGLRAELKQRLRALSAEERLRQSLLLTQKVIAHNQYQNSKRISIFLSMQDEVETEVIIKDIFKQGKICFIPRYQFQSNHMDMVRLTSSEEIALLPKTSWNIHQPGEGDVREEALSTGGLDLIFLPGLGFDKDGNRLGRGKGYYDTYLKRCVQHQEVKPYTMALAFKEQICPQIPVDEHDMKVDEVLYEDSPAS
Protein: Nif-specific regulatory protein (P03027)
Organism: Klebsiella pneumoniae
Function: Required for activation of most nif operons, which are directly involved in nitrogen fixation.
Interaction partners:
Sequence:
MIHKSDSDTTVRRFDLSQQFTAMQRISVVLSRATEASKTLQEVLSVLHNDAFMQHGMICLYDSQQEILSIEALQQTEDQTLPGSTQIRYRPGEGLVGTVLAQGQSLVLPRVADDQRFLDRLSLYDYDLPFIAVPLMGPHSRPIGVLAAHAMARQEERLPACTRFLETVANLIAQTIRLMILPTSAAQAPQQSPRIERPRACTPSRGFGLENMVGKSPAMRQIMDIIRQVSRWDTTVLVRGESGTGKELIANAIHHNSPRAAAAFVKFNCAALPDNLLESELFGHEKGAFTGAVRQRKGRFELADGGTLFLDEIGESSASFQAKLLRILQEGEMERVGGDETLRVNVRIIAATNRHLEEEVRLGHFREDLYYRLNVMPIALPPLRERQEDIAELAHFLVRKIAHSQGRTLRISDGAIRLLMEYSWPGNVRELENCLERSAVLSESGLIDRDVILFNHRDNPPKALASSGPAEDGWLDNSLDERQRLIAALEKAGWVQAKAARLLGMTPRQVAYRIQIMDITMPRL
Protein: CTD kinase subunit alpha (CTDK-I subunit alpha) (EC 2.7.11.23) (CTD kinase subunit 1) (Latrunculin sensitive kinase 1) (O14098)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity). Together with ctk2/lsc1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD. Required for nuclear localization of ctk2/lsc1. Positively regulates the septation initiation network (SIN) and promotes successful completion of cytokinesis in response to perturbation of the actomyosin ring. Acts in parallel to clp1 to promote actomyosin ring stability upon cytokinesis checkpoint activation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17502918}. Note=Localized to nucleus during all cell cycle phases. {ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:16823372}.
Interaction partners:
- CTD kinase subunit gamma
- CTD kinase subunit beta
- DNA-directed RNA polymerase II subunit rpb1
- Cyclin pch1
- Transcription elongation factor spt5
- Transcription elongation factor spt4
- RNA polymerase II subunit A C-terminal domain phosphatase
- Probable cyclin-dependent kinase 9
- Cell division control protein 73
- Cyclin mcs2
Sequence:
MSYSKSTIYRRQGTEPNSHFRRTVEEKSQLSGTNEESLGGHTLSSNAFKNNSSSISPSSSAKDPREQRKRTFPLNDTHSSRARQHERPFRSRKSRRRKGKKAFSPRPGSPPSPSFYRSGSQKRARNLTTKDYFAKRSESSSSASVSPISPSANRNDSKRQASSFRRSPPSSVHMKPSAFNGRKVSRRPSSSPPPIPSIPHETTSSDTQKKSSVSSGFPENKHGKFHFHIPNERRSRFDQPPSKRMALTSTARESVPAPLPSPPSGPIYTYTYPKPAYEKIDQIGEGTYGKVYKAINTVTGDLVALKRIRLEQEKDGFPITTVREVKILQRLRHKNIVRLLEIMVEKSSVYMVFEYMDHDLTGVLLNSQLHFTPGNIKHLSKQIFEALAYLHHRGVLHRDIKGSNILLNNNGDLKFADFGLARFNTSSKSANYTNRVITLWFRPPELLLGETAYDTAVDIWSAGCIVMELFTGKPFFQGRDEISQLEVIYDMMGTPDVHSWPEVKNLPWYELLKPVEEKKSRFVETFKEILSPAAIDLCQKLLALNPFCRPSAHETLMHEYFTSESPPPEPAVILKNMQGSWHEWESKKRKSKR
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-B, mitochondrial (EC 7.1.1.2) (Q9FX83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase 1 beta subcomplex subunit 10-A
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase flavoprotein 1, mitochondrial
Sequence:
MASLLARRSFSALRARHLAFSGQGLQGSHLCGLQSRAISYGSNKDDEEAEQLAKEISKDWSTVFERSMNTLFLTEMVRGLSLTLKYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLRSESLYR
Protein: Ras-related protein Rab-15 (EC 3.6.5.2) (P35289)
Organism: Rattus norvegicus (Rat)
Function: May act in concert with RAB3A in regulating aspects of synaptic vesicle membrane flow within the nerve terminal.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MAKQYDVLFRLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFKMKTIEVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLVYDISSERSYQHIMKWVSDVDEYAPEGVQKILIGNKADEEQKRQVGREQGQQLAKEYGMDFYETSACTNLNIKESFTRLTELVLQAHRKELDGLRTCASNELALAELEEDEGKTEGPANSSKTCWC
Protein: Non-structural maintenance of chromosomes element 3 homolog (Non-SMC element 3 homolog) (Hepatocellular carcinoma-associated protein 4) (MAGE-G1 antigen) (Melanoma-associated antigen G1) (Necdin-like protein 2) (Q96MG7)
Organism: Homo sapiens (Human)
Function: Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:18086888}. Chromosome, telomere {ECO:0000305|PubMed:18086888}.
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Structural maintenance of chromosomes protein 6
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase NSE2
- Non-structural maintenance of chromosomes element 4 homolog A
- EP300-interacting inhibitor of differentiation 3
- Small ubiquitin-related modifier 4
- SMC5-SMC6 complex localization factor protein 2
- E3 ubiquitin-protein ligase Praja-1
- Double-strand-break repair protein rad21 homolog
Sequence:
MLQKPRNRGRSGGQAERDRDWSHSGNPGASRAGEDARVLRDGFAEEAPSTSRGPGGSQGSQGPSPQGARRAQAAPAVGPRSQKQLELKVSELVQFLLIKDQKKIPIKRADILKHVIGDYKDIFPDLFKRAAERLQYVFGYKLVELEPKSNTYILINTLEPVEEDAEMRGDQGTPTTGLLMIVLGLIFMKGNTIKETEAWDFLRRLGVYPTKKHLIFGDPKKLITEDFVRQRYLEYRRIPHTDPVDYEFQWGPRTNLETSKMKVLKFVAKVHNQDPKDWPAQYCEALADEENRARPQPSGPAPSS
Protein: High affinity copper uptake protein 1 (Copper transporter 1) (rCTR1) (Liver regeneration-related protein LRRGT00200) (Solute carrier family 31 member 1) [Cleaved into: Truncated CTR1 form] (Q9JK41)
Organism: Rattus norvegicus (Rat)
Function: High-affinity, saturable copper transporter involved in dietary copper uptake.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23123662}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O15431}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:O15431}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:20699218}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q8K211}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8K211}; Multi-pass membrane protein {ECO:0000255}. Note=The localization is controlled by the intra and extra-cellular copper concentration. Under conditions of elevated extracellular copper concentrations, it is rapidly internalized by endocytosis from the plasma membrane by a clathrin- and dynamin-mediated process and degradated in order to prevent intracellular copper accumulation and to reduce the transport of the copper across the membrane. The internalized SLC31A1 is then localized in early endosomes, and, upon a low extracellular copper concentrations, it is transported back to the plasma membrane in a RAB11A-dependent recycling pathway (By similarity). Localizes to the apical membrane in intestinal epithelial cells (PubMed:20699218). Localizes to the neuronal cell body plasma membranes (PubMed:23123662). Mainly localized on the basolateral side of renal tubular cells (By similarity). {ECO:0000250|UniProtKB:O15431, ECO:0000250|UniProtKB:Q8K211, ECO:0000269|PubMed:20699218, ECO:0000269|PubMed:23123662}.
Interaction partners:
- Copper transport protein ATOX1
- Copper-transporting ATPase 1
- Copper-transporting ATPase 2
- Cytochrome c oxidase copper chaperone
- Copper chaperone for superoxide dismutase
- Solute carrier family 22 member 2
- Proton-coupled zinc antiporter SLC30A1
- Natural resistance-associated macrophage protein 2
- Ceruloplasmin
Sequence:
MRMNHMEMHHMGMNHTDDNITMPPHQHPTTSASHSHEMMMPMTFYFGFKNVDLLFSSLVINTPGEMAGAFVAVFLLAMFYEGLKIAREGLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH
Protein: Larval serum protein 1 gamma chain (Hexamerin-1-gamma) (P11997)
Organism: Drosophila melanogaster (Fruit fly)
Function: Larval storage protein (LSP) which may serve as a store of amino acids for synthesis of adult proteins.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:3097321}.
Interaction partners:
- Larval serum protein 1 beta chain
- Larval serum protein 1 alpha chain
- Larval serum protein 2
- Fat body protein 2
- Fat-body protein 1
Sequence:
MKLTLVILALVACVTAFSVPTQKVKIADKNFLEKQKFLFEIVHRIDEPLMFEEWIKMGQKLITDKAQYETFDFYMEKLWESYKLGALLPKGEFFGALVKTHHKQAYGLFNFFYYAKDWETFVRNVAWARIHVNEGMFVYALTLAVIHKPEFEGLILPQIYEIFPQYFFNSKFVYAAEKFDYEVFSKLTMYEKEYKDILYKDYSEFTGNFYFYTKDWKTWQWYKMMGLDQEWYVEDKYFLRENLSQFVNDPKYVDVVKGLKKFYMPVDYTRDIDFFNDETKMTYFTEDLGWNAYWYYLNMDYAFFLNGKQFGLDKDRRGEYWIYNVQQILARYYQERLANGFGEIPEFFWYKQIEYGYDPQLIYYNGIGYSYRKNYYDFYTYGKFEMYSQIQNFFSRVYKVLETGFYKTADGQVFDLHKPEAIKIVGNYLQGNADTFDKYFFNYYYLLAHMYFADVDYNDMEVFPNVFLNFETMLRDPFFYTFYKKFTDVFYTFKYYLKPYTQKDLFYEGITIKDVSVSKLVTYYDIVDFDVTNLLNDKMTFVDGQYIWDKALLARQARLNHKPFNFEFTIDSDKVQKGVVRVFLGPKFDEYGRVIPLDYNRKNFVQIDSFVYPFIAGTNTIKRSSKEFSWTAEDRITYTELYKYVMLASEGKYDFPLDISEPHNAFPDRLVLPKGWEQGMPMQFYFFVSPFAETYEQFSNFDYTYSSGVGSGTRFVDTKPFGYPFDRQIDESDFFVPNGFFKDVKVYYVDTFAKYFEKKYTQFGTFDYSIEY