wanglab/gogpt-training-data huggingface dataset:
Protein: Coiled-coil domain-containing protein 39 (Flagellar-associated protein 59) (A8IQE0)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, by acting as a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Together with CCDC40/FAP172 forms a 96-nm-long complex in flagella. This complex does not act as a physical ruler, but rather act as a negative regulator for radial spokes: the complex lays along specific protofilaments, masking radial spoke binding sites and allowing recruitment of inner dynein arm (IDA) and nexin-dynein regulatory complexes (N-DRC).
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:25395538}.
Interaction partners:
Sequence:
MANIDPYRTEEELVEDDEEVDMSFLPPFAKGTENEVLYVENARMERRLERTERALETNMDRLHIMDEHLKNVQQELKYTQTRVEAKNKEIESEKHLNAMAEREMGRLKKDIGKMEAERQELADKINGLQNQIYKNNEKLDQFKMLMNWNQEELEQWALAERQKAEDNAALEKYRHADDGKVKELTLALERVSKQVVGRKEELEAEVVETQAAQIQLDKAAEDFRKLHVERQDLIRQWEEAVEAMRHRDAAIAAASEQFAMQKDVLRERKRELDAQARFLENETLNTKEADARVAYYEREVGKQRDVLAREQARTEELNNQVELVKATLSKAATELAQRTVENKQAREDLDAKRQKLDAARKRFVVLKRKLENEFGNLDSMEAKASELEAMRRGEEARLKAILKEHELLKKEQYKRSQVLFDLRQKERELISEISGGQGQNKNLAARIHALDEQVVARAGGVRSEEETRALNARIEKLTAILEGVKRAEDDLLAARRANTSLRADRAKLDETISTLKLENDMVSRQVKGSVEAREKALVDHDVLALEVKRLRDILAAHADEVFSLENRKQQLALSMEERKQEVEVHRDGLRAELRLLREDVHRITLELKERLLRCEKLQAKFEIISAKHRGSGEDDGEERTQAYYVIKAAQEREALQREGDDLDGRIRVAEKEVAALEATLAQLMAVNTNFAASYKKVGSKEAFEERAALRDKLDKAYDKLKARRADEAAIAGDIQVSEARLSNLGQEQRSLQALVDDMTRRKAEAQRQLDEQREKLGRALGRTDKLRQKLGLANSPQGADVELAEVRDVTRAMLLELKALALANPGAMIAEACEAAGIRLPSGGSNPPSLGGSRPGSARSQTSLGSVRSARSVASQQRGGMGGSPAVRTIQLGA
Protein: RecQ-mediated genome instability protein 1 (Q02685)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Structure-specific DNA-binding protein with a preference for cruciform structures. Also binds single-stranded DNA (ssDNA). Functions together with SGS1 and TOP3 to maintain genome integrity. Essential for proper meiotic cell division. Required for normal S-phase progression and DNA damage response. Required for resistance to the DNA-damaging agent methyl methanesulfonate (MMS).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA topoisomerase 3
- ATP-dependent helicase SGS1
- Crossover junction endonuclease MUS81
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA repair protein RAD51
- ATP-dependent DNA helicase SRS2
- Crossover junction endonuclease MMS4
- Exodeoxyribonuclease 1
- DNA repair and recombination protein RAD52
- Structure-specific endonuclease subunit SLX1
Sequence:
MSFSSILSQDITDDITPPAYSATLGSREQIVFRAYQNEPWLAGTASNLILDKKLVIVDRELLFQVLMVENITKSKLTQIDDIKTKLDPKKQKVDRLRSGAQGNGAKKYEVITQVDMEDDGNVADNNCAKENNSNNNSSAAKNKAVFKLTLQSKSGDVFFAINSTPISWSSCMLGSKIVILPGTVFNRGVFILKDSQVIFLGGINRVWNENRDQKFCDYLESKLQRDKQLVNGGSKKRKAND
Protein: Synaptophysin (A0A0G2KAD8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004644}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004644}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
ACPLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYTGELRLSVECANKTESALNIEVEFEYPFRLHQVYFDAPSCVKGGTTKIFLVGDYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMMDFLATAVFAFMWLVSSSAWAKGLSDVKMATDPENIIKEMPMCRQTGNTCKELRDPVTSGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFMRAPPGAPEKQPAPGDAYGDAGYGQGPGGYGPQDSYGPQGGYQPDYGQPASGGGGYGPQGDYGQQGYGQQGAPTSFSNQM
Protein: Nitrate/nitrite transporter (P95224)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU366033}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU366033}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Nitrate reductase alpha subunit
- Nitrate reductase-like protein NarX
- Nitrate reductase-like protein NarX
- Probable respiratory nitrate reductase
- assimilatory sulfite reductase
- Nitrite reductase small subunit
- Probable nitrate/nitrite transporter NarK2
- Probable respiratory nitrate reductase
- Probable nitronate monooxygenase
- Nitronate monooxygenase
Sequence:
MALTTAPAIDYALPRQQDEGDHWIDDWRPEDPVFWETIGRPIARRNLIFSIFAEHVGFSVWMLWSIVVVQMTAAAPGHPAASGWALSASQALCLVAVPSGVGAFLRLPYTFAIPIFGGRNWTTVSAALLVIPCLLLAWAVSHPSLPFAVLVVIAATAGFGGGNFASSMANISFFYPEKDKGWALGLNAAGGNIGVAVVQKIIPPIVVAGSGVALSRAGLFFVPLAVAAAVCAFLFMNNLTEAKADVKPVWQSLRHADTWIMSLLYIGTFGSFIGYSAAFPTLLKTVFGRGDIALGWAFLGAGIGSLVRPLGGKLADRIGGARITAASFVMLAAGAAAALWSVQSVNLPVFFVSFMFLFVATGIGNGSSYRMISRIFQVKGEVAGGDPETMVNMRRQAAGALGIISSIGAFGGFVVPLAYAWSKVHFGNIEPALHFYVAFFLALLVVTWYCYLRRTTPMGQVGV
Protein: Proteasome subunit alpha type-2 (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3) (Proteasome subunit alpha-2) (alpha-2) (P49722)
Organism: Mus musculus (Mouse)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus {ECO:0000269|PubMed:22078707}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (By similarity). Colocalizes with TRIM5 in cytoplasmic bodies (PubMed:22078707). {ECO:0000250|UniProtKB:P25787, ECO:0000269|PubMed:22078707}.
Interaction partners:
- Proteasome subunit alpha type-1
- 26S proteasome non-ATPase regulatory subunit 2
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 6
- Proteasome subunit beta type-5
- Proteasome subunit beta type-3
- 26S proteasome regulatory subunit 6A
Sequence:
MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVRDYLAAIA
Protein: C-C motif chemokine 21b (6Ckine) (Beta-chemokine exodus-2) (Small-inducible cytokine A21b) (Thymus-derived chemotactic agent 4) (TCA4) (P86792)
Organism: Mus musculus (Mouse)
Function: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Potent mesangial cell chemoattractant. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 7
- Atypical chemokine receptor 4
- C-C motif chemokine 19
- C-C motif chemokine 21a
- Fractalkine
- C-X-C chemokine receptor type 4
- C-X-C chemokine receptor type 5
- C-X-C chemokine receptor type 3
- Stromal cell-derived factor 1
- Eotaxin
Sequence:
MAQMMTLSLLSLVLALCIPWTQGSDGGGQDCCLKYSQKKIPYSIVRGYRKQEPSLGCPIPAILFLPRKHSKPELCANPEEGWVQNLMRRLDQPPAPGKQSPGCRKNRGTSKSGKKGKGSKGCKRTEQTQPSRG
Protein: SAM-motif ubiquitously expressed punctatedly localized protein, isoform A (SAM-motif ubiquitously expressed punctatedly localized protein, isoform B) (Q9VKL0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKEIDTETTVVWPAWCYSGNAPTDILQQKPAKATTAIVGGRSAAQPATHDDQEAATTASTATKRKHLERLASDLRQLGKKGRRSRSVSPCSRYPAVAETARMLSERSLLLSGYGAIESSAKKLSEAATGGAGGGGGGAAGQAATPTTSQLSAPASSASSSSMSSSSAGSTCTTNANTASVAAAYAAFYLEKVKHEKMDNHKDAPMVTIHNNNNNNTINNNNSSSSSSSSIINNHQSSQPSLGHSVKRERLSPGSNSSSHNGELTVSSFARSRSATPSSSSYRGAGGGAGGGVSPSHQQQQQQQQQSLQQQQRLSPPSGPSMATATTTSSLSSSSSASASASASASAATHMPLHNLSTNLLNSIQQAAASQQQLRSSNSNSSSNISGSSNNTKSDGGAASNATDFSTRNYSDIMRCLAAKYNNANPNDNNATRRNSYYDGSTSATTATGGAGGGGGGAGGSNSAPSSALKTASSSTGSTTTTAKKLSPSAASAANSAAVSLSKESKVSAVGGAGVGGAVASSGGGGSSMSQLAPPPTAPSPTEQAKSQMAAVVAAASVSPFMTNFLPFSSGIFPPLIDMSSTQALLTLARAVKDAEIQEILRSKQQRSGSNASSPSASAAGTPRSSSTLNAALHQAAQFVTPALIYSAQLQQQQQQQQQQHQRQQQQQSQHASRQSSPRSTNDSTTVAPIGDGGGGSSIASAAPLDLSSQPPAAKRFKAERRASSTATTATTATTGSSTSTPSPPPLEQHDDINSGNANATLGTRSGTGTGESSAAGSGAGVAKARRRCQAQSEEVNSWSVDDVCGFVGGIDICAEYVQSFRDQSIDGTGLPLLTEDHLVNSLGMKLGPALKLRSILAKKLGGPCPCVACVAQAQQMLALQTGGAAAATGATAGAGTVTGAVAGAGATSATTSCSIKSEIFNGGSNGSSSGSSSNQGSDVAAPPAATASSPSSNMLLPVLPCSGLQDAS
Protein: Large ribosomal subunit protein bL9m (39S ribosomal protein L9, mitochondrial) (L9mt) (MRP-L9) (Q99N94)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BYD2}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS3
Sequence:
MAASVAPGVRTLWWAGAAWLRQGGIRELFRPRIEGSTPGRDFSLSHYQSTVIVERWWKVPLAGEGRKPHLHRRHRVYKLVEDTKHRPKDNLELILTQSVDEIGVRGDLVSVKKSVGRNKLLSQGLAVYASPENRKLFEEEKSLRREGKLEKIQTKAGEATVKFLRSCHLEVGMKNNVKWELNPEIVARHFFKNLGVVVAPHALRLPEEPITRWGEYWCDVTVNGLDTVRVPMSVVLFQKPKTKRYKHWLAQQAAKSVAPTNPQAV
Protein: cyclic-guanylate-specific phosphodiesterase (EC 3.1.4.52) (Q9I1R7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- diguanylate cyclase
- diguanylate cyclase
- Diguanylate cyclase
- diguanylate cyclase
- FAD dependent oxidoreductase domain-containing protein
- Diguanylate cyclase
- Tryptophan 2-monooxygenase
- Diguanylate cyclase TpbB
- Diguanylate cyclase DgcP
- diguanylate cyclase
Sequence:
MSERGTAAEGRINWRRILPILLTTTLVGGVCGIFVINELDRQHDGAHLRSYTERALERALEISSAADQMLREMNAGSAPACSDRDLEMLRSIVLESRFMSDVGRISGDRVMCTGVRGRLRAPWGLSAPDRVDAAGTRFWSEGMPLPLQALPTGLVSRGNAVVFIAPHAYFDVDHPAPGISAAAVSSGGDYIYHRFAWDDDQPLEALGRPGWPRFIGARQISLCDPTQDICVVSLLRERGLLGTEPGRAAMAAAIGGGLLFGVMLLLSYLFGFLNDEKLPARLLRALKREALEVHYQPIVRLASGRCAGVEALARWTDSSLGRVSPDVFIGALEESGDIELLTRFVFRRALKQLGPLLREQRSFYVSVNVTGKDIADPGFIDFAMRQMARESVRPEQVALELTERTTEAQGCLLAGMNRLRELGLKIYVDDFGTGHSNLVYLANLPVDAIKIDKVFTQSIGDSSAVELIFDKLCSMAEHLEIGVVVEGIETQAQADHVLRRSPEALGQGWHFGKALPLEAFLDYYRNQPAGR
Protein: Thioester-containing protein 4, isoform A (Q9VIT9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRADAFAVSLCVILALLQTMEPVKAEGKYTIVGPGTIHSHRDYNVAVAVHQTKEPVTLKVGITGPSYNKTETVELATAGEFKQITFKLPPLEAGEYNLTAEGVKGLEFKNSTKLNWENFKPYIKIQTDKGKYKPGDTINYRVIFLDENLRPDTAKDEVVVWFEDSKRNRIKQEKHIKTTGGVYTGKFELSEFATLGSWSLHVQNGDQHHDGGIYFGGRKQFGGFGHRWHRSDELVNFEVEKYVLPKYSVKMDATQQVSVRDGEFNVVLKANYTYGKPVNGKVLVNVHLDSTSSWENVDGKTVQTDYPGHSVVGTADMVGGKAKLTMDLKDFASYLPHKTSSSYAQITATVEEDFTGVKLNETGGVQLYPYRYEMSCTDYSSCFSFKPDKEHELNFKITYVDGSLITDTKSVVKAKFTEGIRRNYAFYAFGTDHQEPELPTIEKKTFVFESHLNASGVAPFKVVLPDLPDIANFTRYYSIELEFVDEKRDLYTTYPYREPKQIENPSSEEEKEWFRAEVQRPKDVWNLKIGQEYQVILNSSRPLKYFVYNIVGRGNILETKRVDLAEPQTTVNVTIKPTFLTTPYGRVYFYYVDETGEFRYTEETFSVEVELQNQIEIKAPAEVKPGADVALEIKTSPKSFVGLLAVDQSVLLLGSNNDLNKESFNWRLNGYDTSTPWQGGYSYYPGERTGVVTMTNAYFFYNRTAPDYNIQGFGGSSFAMRKTTVAHDSHVFHSGAGGPTQAVGFSAESASASAAPVVRKNFAETWIFADIESTEEEVFKWVKTIPDTITNWVVTGFSLHPQKGLGVTNDQTNIKTFQPFFVSVRLPYSVKRGEVINVPALVFNYLPKTLDVELTLDNEDQEYDFVDASNEVIGDQKRTQNIRVGANEAAGASFLIRPKVIGNILLKFKAISPLAGDAIHKPLKVVPEGITQYQNRAFFINLKDTGEFKNTFELEVPEDVVPDSERVEFGLVGDLLGPVVKNLENLLRLPSGCGEQTMSKLVPNYLVRDYLKSIKKLTPALDTRIKRNLQDGYQHMLHYRHDDGSFSSFGPTKWRQEDPVRNGSTWLTAYVLRSFSKIKDIIDLDEQILAKGYEFLLTRQAENGSFTEHGEYFYSSQRSLLTLTANSLLALLEEEKPNQAAIDKAVAYLSANTAESIELLPKSIAIYALQKAKAPEAAKQVASLKSLAKHEDDRTWWTEDLDKLRASKNCGRWWCWIWSQDVEITSYALLSLLDSDQETADSVLNTVRWLIAQRNGFGGFASSQDTVVGLTALIKFAEKSGYEAAKWEVTVSNKGKREKTEKLNTSEENDLLLQTVEFPQGTKSLEFEAKGTGAAMVQISYQYNLVEKEPKPSFKIQTTVLPESSPANLELSVCVDYVEEGESKESNMAILEVSLPSGYTADEDSFADIRNIERVRLVETKNGDSVVVIYFENLAKNEEKCIRIEAYRTHAVANQKPSSVVLYDYYDTNKKATEYYSIKSKLCDICEGDDCKSKC
Protein: Chromosomal replication initiator protein DnaA (O83047)
Organism: Treponema pallidum (strain Nichols)
Function: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
Interaction partners:
- Beta sliding clamp
- Uncharacterized protein
- DNA polymerase III subunit gamma/tau
- DNA polymerase III subunit epsilon
- DNA polymerase III, gamma and tau subunits, putative
- Single-stranded DNA-binding protein
- Single-stranded DNA-binding protein
- Uncharacterized protein TP_0183
- Replicative DNA helicase DnaB
- DNA polymerase I
Sequence:
MDAVGYEVFWNETLSQIRSESTEAEFNMWFAHLFFIASFENAIEIAVPSDFFRIQFSQKYQEKLERKFLELSGHPIKLLFAVKKGTPHGNTAPPKHVHTYLEKNSPAEVPSKKSFHPDLNRDYTFENFVSGEETKFSHSAAISVSKNPGTSYNPLLIYGGVGLGKTHLMQAIGHEIYKTTDLNVIYVTAENFGNEFISTLLNKKTQDFKKKYRYTADVLLIDDIHFFENKDGLQEELFYTFNELFEKKKQIIFTCDRPVQELKNLSSRLRSRCSRGLSTDLNMPCFETRCAILIKKIQNYNSTYPHKAIHISDDVVRLVSENISSNIRDLEGALTKIIAFIEVSGSITIDIVPSLLKEFFLSARPKHITVETILHVVADHFNISYSDLKGKKRNKSVVYPRQIAMFLSKELTELSTTELGIEFGGRDHSTVIYGCQKIEGEILTNPSLQANLDLLKSKVQDSIR
Protein: cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed] (P07802)
Organism: Sus scrofa (Pig)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Protein kinase cAMP-dependent X-linked catalytic subunit
- A-kinase anchor protein 10, mitochondrial
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- Protein kinase cAMP-dependent type II regulatory subunit beta
- Hormone-sensitive lipase
- Protein kinase cAMP-dependent type I regulatory subunit beta.
- non-specific serine/threonine protein kinase
Sequence:
MASGSTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKASARADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGNDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
Protein: Ankyrin repeat and SAM domain-containing protein 3 (Q9CZK6)
Organism: Mus musculus (Mouse)
Function: May be involved in vasopressin signaling in the kidney.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:26327442}. Cytoplasm {ECO:0000269|PubMed:26188091}.
Interaction partners:
- Ankyrin repeat and SAM domain-containing protein 6
- Serine/threonine-protein kinase Nek7
- Serine/threonine-protein kinase Nek8
- Leucine-rich repeat-containing protein 45
- Transcription factor E4F1
- Nephrocystin-1
- Nephrocystin-3
Sequence:
MSELSDEASEPELLKRSLSMWHGLGAQGSPEELDVPLDLHTAASIGQHEVVKECVQRGELDLNKKNGGGWTALMYASYIGHDTIVHLLLEAGVSVNVPTPEGQTPLMLASSCGNESIAYFLLQQGAELEMKDIHGWTALFHCTSAGHQQMVKFLLESGANANVREPVYGYTPLMEAAASGHEIIVQYFLNHGVKVDTRDHSGATACMLARQFGHMKIVALMETHSPVLPKSLYRSPEKYEDLSSSDESWPVPQRQRPCRKKGLSIHEGPRALAKITAIGLGGKTQTTYEQVPPRGYVTFTSSDENTMESEGLCYRDVTSPINEQDVESSSSSSREEPTFCASLGPVWRSSSSDGLARAQGLSSEASIESNEDSDHARKSSVRKQTRSYLKNKSRHGNSDGHWPSSTGPASIPGSEPQTEKSPYSGPQDLATLLEQIGCLKYLQVFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHSSARPPSDALELAYADRLETEMQELAIQLHKCCEEAEALRGQVSQEQELRAVVESCLLEQDSARKDIHAQLQEAQTLAQDAALVLDQLRACQAELSARLRQHHSPREGTPNPHFLSADSKGWPIPLQALSLPELSGALEDRVHEMGQALCSVTQSLEKLQMLNAKKWREP
Protein: Envelope protein OPG155 (P68633)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation).
Subcellular location: Virion membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. Note=Component of the mature virion (MV) membrane.
Interaction partners:
Sequence:
MNSLSIFFIVVATAAVCLLFIQGYSIYENYGNIKEFNATHAAFEYSKSIGGTPALDRRVQDVNDTISDVKQKWRCVVYPGNGFVSASIFGFQAEVGPNNTRSIRKFNTMQQCIDFTFSDVININIYNPCVVPNINNAECQFLKSVL
Protein: Checkpoint protein (Q9VN60)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cell cycle checkpoint control protein Rad9
- DNA repair protein Rad1
- Rad17
- Replication factor C subunit 2
- Mutagen-sensitive 101
- Replication factor C subunit 2
- Replication factor C subunit 3
- Activator 1 subunit 5
- Serine/threonine-protein kinase ATR
- Bub1-related kinase
Sequence:
MKFRALMQDPLYMKEFQAIVATLTKLAKDCVMILGSRQMHFIVNEDQSSAASPLVWAGITAEEYFPEYRMEAAHPDQEYIVLGVSSANLGRALSVLRGGGVNSCKLKLQRIQFPCISVIASVLTSSSTEAREVVHDVPVTIIPGSDWSAYVVPRVPNSQLALGLPSLRLLKSLIDKLKNISPSLEFQVNVDGELNVIATSEMSTVTSRFQKLLIRTVSGSQQEASCSVDSRKASAFFGALQLPNEELTIGIDREHSIHLQIDVRQDVVLHSILPAVCM
Protein: Protein Tat (Transactivating regulatory protein) (Q1PAB4)
Organism: Human immunodeficiency virus type 1 (HIV-1)
Subcellular location: Host nucleus, host nucleolus {ECO:0000256|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04079}. Secreted {ECO:0000256|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000256|HAMAP-Rule:MF_04079}.
Interaction partners:
Sequence:
MEPVDPRLEPWKHPGSQPRTACTNCYCKKCCFHCQVCFIRKALGISYGRKKRRQRRRAPQDSETHQVSPPKQPASQPRGDPTGPKESKKKVERETETHPVN
Protein: Talin-B (Q54K81)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Actin-binding protein required for multicellular morphogenesis. Substrate of pkgB and/or pkbA.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm, cell cortex {ECO:0000305}.
Interaction partners:
- Probable vinculin
- Paxillin-B
- LIM domain-containing protein DDB_G0271356
- Integrin beta-like protein A
- Gelation factor
Sequence:
MSLTLKIQIVRDKQVKAMKFSPTQTVAEVCAQVREKINETSGDDHGLFQPGIDAKRPSRWLKMDKTLQFYDLKINDELDYKKKHRPLKVRLMDETVKTMLVDDSLTAGEILEIIGKRIGIKNYEEFSLQTEGAAAGEWINHAQPLHEQGVPDDAVVLLKKKFFVDDFNVNRDDPIQLHLVYVQSRDAIISGSHPCSYEEAVQFGALQCQIQLGNHNPNLHKPGYLKIKEYFPPSFHKKKDAEKDIYKEFRKLTGMSESNSKFRYVQLCRSLKTYGITFFLTKERVKGQKKPVPKLLGITRDSILRLDAETKEVEHEYPLNHLRRWAASPQSFTLDFGDYEDDYVSVITTEGEAISQLLSGYIEILMKKRKDTGTVIDENETDIANVESVGRIRGQTSQATTSSSLSGYDGNGGREGQYSAPGQAIGYRGGLGGPLSIKVTNIDSASAAVANLLNEMELDPNAVIGQKSSLTPQQWRQQLAIHAKAVAAAAGKLLGNLNNPNGMDKNQMDSNARDVALTIDQLVHAARAASIASGEDPDGEMPLFDGAKAVAESISKLLKATKDLSSNPNDENARNLIAQAADQLKLMTSYLDGACNGVITDSGTLRLLMEAGKAIAIATQDLVNQANVAIQDINDPIRKNQLNMAIDETMKAGIHASAVSQALAATILDPNCRQQFNTAAKTAQDTNNYLLSAAKAAQMDPALLEKLRASAKSIAEAYASLIQSADLAQPKSGDDVEFTSASKTILSAAAQLLGSQGKSDNIMQQAKVIEEAMGHLIAGARRAALKTDDPGVRDRLIQCSKAVAEAVRNLMEIAQDSADNPEDKVLFAKLQESSKRVATAVKQLVGDAGKESAFQLLRTNAKLACAATTGLMNTSRQSMLQGHLSDQESNKLLLACVQAGPAITNLLNSITSSQKAPNDLPAQNQLIEVARVSAPIAYQVVAVAKGAIPHFTDQHSKQEVSNSSNTASDAIRALLDAIGDLTSAVGQQEFDDALDTVQALEADMESSTMLVQAGTTHQIPGQTRENALELLNVAARALGSSAKQVLLQYKTSPEKLGETSKDLATSVSQVTNAAKSVCFTTQNRSVQKAVLGAAKQITTESTNLVSCARAVSSNPGDPSLESALQSSVKAIAEALANLLTTSKGGDPGGKDLDDAIEAIKNDTKRINNPPVNLGGEGGVNSEKAISSSKALVGAVSQVAANARSNPSALGASARTTSTTFTLLVDTINLCTGTIVNKQLAIEIVKGGQLLGIETIKLLQASRFAASRPGEGEGELNQTQQSVSNTVKQLIYNIQSSVPGQAEIADALEIVKQAIIALNSSESSGSRPNALESLTQAAKNLADYTAQVVQSKGNSEKMGTQCKSASESLKDVVEYTKASLSTAEGHPDSIKTLASKVDDSSNALFNSCKKTGQLSDQDKKNAALDAKNLALSVPNLMGAAKKISASLVQSNPEKSKDILLVAQNITIATSKLVNIAKSVASGQSQADVSQLAATKKEVSELISKLLNATNGHDQDATTISIDLDSLSKSEQALLDASRSTANYMSQFMAIGKTISTGTKDPNVHQQFSGAAQNVSSGVQQLLSAINGMKPEQKDLDESIEIIQNAVVDLDSATLNAAIGLLENTAPVGKTAQVCQEELVDISRELATSMKTFLAAPKQDPTNLGQSAKDTANILPKIVNISKQLASLTTNPDIKQTQLLLSKKLADNMLELMISAKSGDVSDSKQAFNASQSIADILTSVKGGVMQSRDCDESIQIIGKSKENLQKPANDTHGKTYQQYRDEMTEIAKQLALGVSQLANSAKSKPEEIGSSSLKIASIIPRLAETARSTAAATNDVAAKKKLIDSTTGIIDATSNIISDAKLASADHKNTQLQQKISNNFKDITTQIANLIAALRAGATADRDIENACNEVNHVTTDLDAASLFAAAGQIDIDTDGHTTQNIQEQVGKLAQDLKDSKNQLAEASGKTIEDVGTSAKATASINQKLAHATKVCAALTSDSTTQQNLLSAARTVSSNLQQTISASKNAQKNPNAGNKAILDKSSQELEESIDSLANLVQSSTTTKGISELEGVSSEIRKQLAAYDSATANVNANATAEDVVNSAKNLAESIAYLVSSCNNSPEDIAEASKGTTLAIKSLLANAKGASVLTDDAVIQQNVTESAKAAAQTVLKLIQAAKQQRNDPSNPAHQNKLSEISSEVVESISTCVNAAEDLPEGKRAKLLFAAGESLEETAEKELKAAAAIIEEATAALLNAKKKREQNRIASGIDEAGIDESILEAARAITSATGVLVQCATNVQHELVLAGKVGNKGNMYRRDPTWARGLISAAQAVAGSVQGLVHSANSSSQGKVDEEQLVASAKGVAAATARLVTASRAKADLNSASNSQLAQAAKQVSNATAALVEAAKQVNEEPEVEFDTTNLSNAQIISKEMDQQIQILKLKKELEQAEKKLFSIRKKEYSDQTGNPSPAKDSDNKPTTSISVGITPTKRTTQASPPSPPLTPTQQAAGTPTLPPRPLMKKPAPSQAPSSPVAPVSAPVSKPSPKPAPKPAAPTAAAPNKTYTLEELKKKPANIDHSNLEIYLSDEEFKAVFNCERSELAAMPTWKRNNIKTKLGLF
Protein: Protein DETOXIFICATION 43 (AtDTX43) (Multidrug and toxic compound extrusion protein 43) (MATE protein 43) (Protein FERRIC REDUCTASE DEFECTIVE 3) (AtFRD3) (Protein MANGANESE ACCUMULATOR 1) (Q9SFB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Citrate transporter responsible for loading citrate into xylem tissues, which helps facilitate iron transport to shoots. Mediates the citrate release in the apoplastic spaces during plant development allowing iron nutrition between symplastically disconnected tissues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15310833}; Multi-pass membrane protein {ECO:0000269|PubMed:15310833}.
Interaction partners:
- Ferric reduction oxidase 2
- Protein DETOXIFICATION 19
- Solute carrier family 40 member 1
- Nicotianamine synthase 2
- Nicotianamine synthase 1
- Fe
- Protein DETOXIFICATION 1
- Probable nicotianamine synthase 4
- Putative cadmium/zinc-transporting ATPase HMA4
- Metal-nicotianamine transporter YSL3
Sequence:
MTETGDDLATVKKPIPFLVIFKDLRHVFSRDTTGREILGIAFPAALALAADPIASLIDTAFVGRLGAVQLAAVGVSIAIFNQASRITIFPLVSLTTSFVAEEDTMEKMKEEANKANLVHAETILVQDSLEKGISSPTSNDTNQPQQPPAPDTKSNSGNKSNKKEKRTIRTASTAMILGLILGLVQAIFLIFSSKLLLGVMGVKPNSPMLSPAHKYLSIRALGAPALLLSLAMQGIFRGFKDTKTPLFATVVADVINIVLDPIFIFVLRLGIIGAAIAHVISQYFMTLILFVFLAKKVNLIPPNFGDLQFGRFLKNGLLLLARTIAVTFCQTLAAAMAARLGTTPMAAFQICLQVWLTSSLLNDGLAVAGQAILACSFAEKDYNKVTAVASRVLQMGFVLGLGLSVFVGLGLYFGAGVFSKDPAVIHLMAIGIPFIAATQPINSLAFVLDGVNFGASDFAYTAYSMVGVAAISIAAVIYMAKTNGFIGIWIALTIYMALRAITGIARMATGTGPWRFLRGRSSSSSS
Protein: E3 ubiquitin-protein ligase RMND5A (EC 2.3.2.27) (Protein RMD5 homolog A) (Q6GLP4)
Organism: Xenopus laevis (African clawed frog)
Function: E3 ubiquitin-protein ligase component of the CTLH complex.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:25793641}. Cytoplasm {ECO:0000269|PubMed:25793641}.
Interaction partners:
Sequence:
MDQCGTVERELEKVLHKFGGYGQLCERSLEELIDYAGGLRREILQAAEQDGELSGTLSLVLTQCCKRIKDTVQKLASDHKDIHSSVSRVGKAIDKNFDADISSVGIDGCWQTDSQRILSEVMVEHFFRQGMLDVAEELCQEASLSIDASQKEPFVELNRILEALKVRVLRPALEWAVSNREMLMAQNSSLEFKLHRLYFISLLMGGTVNQQEALQYAKNFQPFAENHQKDIQVLMGSLVYLRQGIENSPYVHLLDANQWADICDIFTRDACSLLGLSVESPLSVSFSAGCVALPALINIKAVIEQRQCSGVWNQKDELPIEVDLGKKCWYHSIFACPILRQQTTENNPPMKLVCGHIISRDALNKMFNGSKLKCPYCPMEQSPGDAKQIFF