wanglab/gogpt-training-data huggingface dataset:
Protein: Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC 2.7.11.10) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (B5DF32)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MERPPGLRPGAGGPWEMRERLGTGGFGNVSLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNFLINDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIMHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMTGEVRFSSHLPQPNNLCSLIVEPMESWLQLMLNWDPQQRGGPIDPPLKQPKCFVLMDNILNLKIVHILNMTSAKIISFLLPYDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPVTQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFRKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYSEVGVIGYLEDQIMSLHTEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPTDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGTVTPPVSAWLPPTLADREHPLTCVRDVSTNDRRKSELSWPFKYYYS
Protein: BCL11 transcription factor A (A0A2U3TZJ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIAGKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVLHTPPFGVVPRELKMCGSFRMEAREPLSSEKI
Protein: GTP-binding protein Rit1 (EC 3.6.5.2) (Ras-like protein expressed in many tissues) (Ras-like without CAAX protein 1) (Q92963)
Organism: Homo sapiens (Human)
Function: Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation.
Subcellular location: Cell membrane.
Interaction partners:
- GTP-binding protein Rit2
- Leucine-zipper-like transcriptional regulator 1
- Serine/threonine-protein kinase B-raf
- Ral guanine nucleotide dissociation stimulator-like 3
Sequence:
MDSGTRPVGSCCSSPAGLSREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKIRIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYRVRRTDDTPVVLVGNKSDLKQLRQVTKEEGLALAREFSCPFFETSAAYRYYIDDVFHALVREIRRKEKEAVLAMEKKSKPKNSVWKRLKSPFRKKKDSVT
Protein: Endonuclease/exonuclease/phosphatase family domain-containing protein 1 (Q3TGW2)
Organism: Mus musculus (Mouse)
Interaction partners:
- RNA polymerase-associated protein LEO1
- Protein IWS1 homolog
- FACT complex subunit SPT16
- Transcription elongation factor SPT4-A
- Parafibromin
- DNA-directed RNA polymerase II subunit RPB7
- RNA polymerase-associated protein RTF1 homolog
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MGSTLGCHRSIPRDPSDLSHNRKFSAACNFSNILVNQERLNINTATEEELMTLPGVTRAVARSIVEYREYIGGFKKVEDLALVSGVGATKLEQVKFEICVSSKGNSAQHSPSSLRRDLLAEQQPHHLTTTVPLTPRVNINTATLAQLMSVRGLSEKMALSIVDYRREHGPFRSVEDLVRMDGINAAFLDRIRHQVFAERSRPPSTHTNGGLTFTAKPHPSPTSLSLQSEDLDLPPGGPTQIISMRPSVEAFGGMRDGRPVFRLATWNLQGCSVEKANNPGVREVVCMTLLENSIKLLAVQELLDKEALEKFCTELNQPILPNIRKWKGSRGCWRSIVAEKPSNQLQKGPCYSGFLWDTAANVELRDIPGRESSPSNGHAKAVGPSPFLARFKVGSNDLTLVNLQLTALALPGAENSSKNHSDGHRLLNFALTLQETLKGEKDVVILGDFGQGPDSNDYDILRREKFHHLVPAHTFTNISTRNPQGSKSVDNIWISKSLKKVFTGHWAVVREGLTNPWIPDNWSWGGVASEHCPVLAELYMEKDWSKKEVPRNGNGVTLEPSEANIKHER
Protein: Protein ALP1-like (EC 3.1.-.-) (Q9M2U3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transposase-derived protein that may have nuclease activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q94K49, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Fantom protein
- Xyloglucan endotransglucosylase/hydrolase protein 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Beta-galactosidase 12
- Calcium-binding protein PBP1
- Protein SUPPRESSOR OF NPR1-1 CONSTITUTIVE 4
Sequence:
MGPIKTIKKKKRAEKKVDRNVLLAATAAATSASAAAALNNNDDDDDSSSQSLDWWDGFSRRIYGGSTDPKTFESVFKISRKTFDYICSLVKADFTAKPANFSDSNGNPLSLNDRVAVALRRLGSGESLSVIGETFGMNQSTVSQITWRFVESMEERAIHHLSWPSKLDEIKSKFEKISGLPNCCGAIDITHIVMNLPAVEPSNKVWLDGEKNFSMTLQAVVDPDMRFLDVIAGWPGSLNDDVVLKNSGFYKLVEKGKRLNGEKLPLSERTELREYIVGDSGFPLLPWLLTPYQGKPTSLPQTEFNKRHSEATKAAQMALSKLKDRWRIINGVMWMPDRNRLPRIIFVCCLLHNIIIDMEDQTLDDQPLSQQHDMNYRQRSCKLADEASSVLRDELSDQLCGKNSSA
Protein: Nuclear hormone receptor family member nhr-23 (Steroid hormone receptor family member chr-3) (P41828)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor. Transcription factor. Modulates expression of target genes, such as Period protein homolog lin-42 and microRNA let-7, by binding to hormone response elements (HRE). Involved in promoting oscillatory expression of the primary transcripts of let-7 and paralogous microRNAs miR-48, miR-84, and miR-241. Plays a role in normal development and required to regulate each larval molt. Involved in regulating both the frequency and number of molts, acting as part of a negative feedback loop with the let-7 family of microRNAs, perhaps contributing to a self-sustaining molecular-genetic oscillator. Positively modulates expression of collagen and hedgehog-related genes. Involved in development of the gonad and associated epidermal structures. Required in spermatogenesis, acting following the sperm/oocyte cell fate decision, downstream of the canonical sex-determination pathway. Involved in regulating formation of the sperm-specific fibrous body-membranous organelle (FB-MO) complexes, acting independently of transcription regulator spe-44.
Subcellular location: Nucleus {ECO:0000269|PubMed:9521900}.
Interaction partners:
- Uncharacterized protein
- Nuclear receptor corepressor 1
- Molting protein mlt-10
- Aryl hydrocarbon receptor nuclear translocator homolog
Sequence:
MACKVTGPNRHLTSVLEMSSFVYWPRSRQQAHNFPMQAVEQKLADATRTLHAKSSLQPSLSIETPKSKENDESGCESSNCMFHPHTIKSEPNFCFAREFKSVPDDFRIGGGDLQMGNNSKRLTCVIDTNRVDMAGILPDNMSFRGLPENKSLLVSAQIEVIPCKVCGDKSSGVHYGVITCEGCKGFFRRSQSSIVNYQCPRQKNCVVDRVNRNRCQYCRLKKCIELGMSRDAVKFGRMSKKQREKVEDEVRMHKELAANGLGYQAIYGDYSPPPSHPSYCFDQSMYGHYPSGTSTPVNGYSIAVAATPTTPMPQNMYGATPSSTNGTQYVAHQATGGSFPSPQVPEEDVATRVIRAFNQQHSSYTTQHGVCNVDPDCIPHLSRAGGWELFARELNPLIQAIIEFAKSIDGFMNLPQETQIQLLKGSVFELSLVFAAMYYNVDAQAVCGERYSVPFACLIAEDDAEMQLIVEVNNTLQEIVHLQPHQSELALLAAGLILEQVSSSHGIGILDTATIATAETLKNALYQSVMPRIGCMEDTIHRIQDVETRIRQTARLHQEALQNFRMSDPTSSEKLPALYKELFTADRP
Protein: Potassium channel toxin alpha-KTx 18.1 (Toxin Tc32) (Toxin To32) (P60211)
Organism: Tityus obscurus (Amazonian scorpion) (Tityus cambridgei)
Function: Reversible blocker of both Kv1.3/KCNA3 potassium channels (high affinity) and Shaker B (mammalian Kv1.1 analog) potassium channels (very low affinity).
Subcellular location: Secreted {ECO:0000269|PubMed:15025998}.
Interaction partners:
Sequence:
MRFTGIILILISMTLIDSFFEMKVEATGPQTTCQAAMCEAGCKGLGKSMESCQGDTCKCKA
Protein: Immunoglobulin lambda constant 6 (Ig lambda-6 chain C region) (P0CF74)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVKVAWKADGSPVNTGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPAECS
Protein: CurA (Q6DNF2)
Organism: Lyngbya majuscula
Interaction partners:
Sequence:
MLELINRYEHGFVYIPVILACREKGLFELIKKKRITHRQIANTLGANTGNLQVALTMMESLGWLSKNEADEYSLKDNCQAYLSIPEEILYLYNLPIESYLLGKEKPGIIKNWIELSQQQWNINDRTIADLLDGVLIIPIMLGLHKHNLLAVDEDKPLFYNVTPHIREELSRLFIAKGWADKSLIKVQKHSQKSNKNKNYLCLTDIGKCLGQRTIIKSISLNCFENNYYNLRHPKIEDLRDLIALETLCWSENLQVDNEEIYRRIFKIPQGQFILELEDKIVGAIYSQRIDNPQLLDNKTCTQVPLLHTESGVVVQLLAVNILPELQNQGLGDRLLEFMLQYCAQISGVEKVVAVTLCRNYPDYSPMPMAEYIHQKNESGLLVDPLLRFHQIHGAKIEKLLPGYRPKDWENQTCGVLVSYDIQHRQRFDGATVEKNRQTKVKLTEDIDEVVASCVRKVMHQKKSFDAQRALMEMGIESLELLELRYLLQKKLGVEIDPNLFFKYGTAAAIASYFKGETTERSGEVSEVLPKPEAIKTDSGFSTAQLENGVAIIGMACRFPGDADSPQQYWSLLHDGIDGITEVPPTRWDIEQYYHPEKNQPGKIANRYGGFLTEVDKFEPDFFRISAREALYMDPQQRLLLEEHWKALEDAGINPESLSGTETGIFVGIAFHDYERLQDKYYQEQDLNIYFATGSSTAIGAGRLSYFFQLNGPSITVDTACSSSLSAVHLACQSIRNGECQLALASGVNLLLSPELSISFSQAGMLSPDGRCKTFDAAANGYVRSEGCGVVVLKSLKQAIADNDRILAVVRGTAINQDGASNGLTAPNQSAQEAVLKRALSVAGVSANQISYVEAHGTGTSLGDPVEIKAIEAVYGKDRSADRPLMIGSVKTNIGHTEAAAGIAGLIKVVLSLQNQYIPPHLHWKQLNPYISLAGIPGVIPTEGKVWEQYEGDETRVAALSSFGFSGTNSHAIVEEAPEGRSQEPGARSQEPGARSQEPPYLLTVSAKKEQALKELVSSYQHHLETNPELELADVCYTANTGRADFNHRLAIIATNPQQLTNKLRQYQAGEEESGVFSGQLSHSSSPAKVAFLFTGQGSQYVQMGRQLYQTQPVFRQVLDQCDELLRPYLERPLLEVLYPQDTPNSNSYLLDQTAYTQPTLFALEYALCKLWESWGIKPQVVMGHSVGEYVAATIAGVLSLEDGLKLIALRGRLMQQLPAGGEMVSVMASKSQVKDAIANHTKQVTIAAINGPESVVISGEAGAIQAIVTKLESKLIKTKQLQVSHAFHSPLMTPMLAEFAAVAQQITYHQPRIPVISNVTGTIADKSIATADYWVEHVVKPVRFVAGIKTLAEQDIRIFLEIGPKPVLLVMGRECLIGSKKIWLPSLRPGKPDWLQMLQSLGQLYVQGVKVDWLGFYPDDAPQKVVLPTYPWQRKRYWISDLQQYKNKGKNGKVAPQVASDNNQSKNSVVTNNSSGSKMLPGIKESEQPRIKEREQPRIKESEQDARTTINIQKSDAPDIEQPQRRLSNPASLSLSKTTVAKQQPAKRELAQLRVPLTQVEPAQITQQYLESEKITQTLGKALHQDILINQKTTKEPKTMNREQVEQLKQEYEEKGYCQIKKIFDFSAIKTIQKTLDQAKQESQISKEKVTLKLGGIDDIDTNDHAYDLVKYDFVSSFIQEKLALLNYITGKNLMIMHNALFSVEPNHKGLPWHVGVGSFSFTKTEDFGASIWIPLDKITKEHRGGMQYVSTKIFPGQFYYSVFDLHLKNNIKWDESQGDLNEYVANANTIYNKITEDVIDYTIKDGYEEDEYNLGDAFFFNKYVLHQSVPLKPGLHKLRRAFVIRLVDYDTRVDEERLGLFSKYSQLHSRYYKTLPRYNKDSVLVMVSRAVQKGLKSPYLRDIPHVQQTLAARMAAGAISFEETPSISSAPQTQQPLKTLQPLRTPQVNQVNLSEIKQVLKQQLAEALYTEESEIAEDQKFVDLGLDSIVGVEWTTTINQTYNLNLKATKLYDYPTLLELSGYIAQILSSQGTKPISSSSQTQQSLKTLQPLPTPQVNQVNLSEIKQVLKQQLAEALYTEESEIAEDQKFVDLGLDSIVGVEWTTTINQTYNLNLKATKLYDYPTLLELAAYIAQTLASQGTKPQVSQQPLKTLQPLPQPQVNLSEIKQVLKQQLAEALYTEESEIAEDQKFVDLGLDSIVGVEWTTTINQTYNLNLKATKLYDYPTLLELAPYIAQEIAATGGSKLFQGNGNGGHPQESLPNNGSPVNSSEEMDPKLRLRAILNKVAKKELTIQEANKLVQQIKKQVTV
Protein: Phospholipase A2 phaiodactylipin (PLA2) [Cleaved into: Phaiodactylipin large subunit (EC 3.1.1.4); Phaiodactylipin small subunit] (Q6PXP0)
Organism: Anuroctonus phaiodactylus (Mafia scorpion)
Function: Scorpion venom phospholipase A2 (PLA2) that is lethal to crickets and crustaceae. Causes inflammation in mice and lysis of human erythrocytes. Has a mild anticoagulant effect on human platelets. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:15066171}.
Interaction partners:
Sequence:
MVKRVSKEEMDALERSCSQPFEEERFLIVSGTKWCGNNNIAANYSDLGFLEADKCCRDHDHCDHIASGETKYGLENKGLFTILNCDCDEAFDHCLKEISNNVTTDIRQKGGAENVWRFYFQWYNANCYRLYCKDEKSARDEACTNQYAVVKKNFTVQ
Protein: Transcription factor sem-2 (Sex muscle abnormal protein 2) (Q8T3B9)
Organism: Caenorhabditis elegans
Function: Probable transcription factor required for embryogenesis, vulval development and cell fate specification of the postembryonic mesoderm (also known as the M lineage). Specifically, required for the specification of sex myoblast cells and their development into the muscles that are necessary for egg-laying. In addition, may be involved in RME GABAergic motor neuron progenitor cell fate specification.
Subcellular location: Nucleus {ECO:0000269|PubMed:21307099}.
Interaction partners:
- SXP/RAL-2 family protein Ani s 5-like cation-binding domain-containing protein
Sequence:
MDLQKPPNFMLDCGMAPHMMPPINWAAAAIAVASSTSGATNATSSNSVATSQQLQHHPYGTAAGGYKHAQQAIPKSVTPYSDATNCKKSSNHIKRPMNAFMVWSQMERRKICEHQPDMHNAEISKQLGSRWRSLTDEEKAPFVAEAERLRVCHMQEYPDYKYKPRKKPKKNPDGTLQQPAQPQAPQQQQAPPRGASPQARQRKRPNTDQQSETQQFQNFKSVKVEQDWMGNAHMSHAQKMPFHPSYPSPSEFGHAPLTPESGFYDDYFTQQHHQQHFASQHHNSAGSPLRMTNLGMDMGMPPQMMGHNSGFGAGNHPFYLHTSPPSVDQDDMRSLSSGSSGYADCSASEQSTSSPNSAGVVTMATAATTTTHLDDLEQICPTVTTGELVNYPWSDALGIDINFS
Protein: Plakophilin-1 (Band 6 protein) (B6P) (Q13835)
Organism: Homo sapiens (Human)
Function: Seems to play a role in junctional plaques. Contributes to epidermal morphogenesis. May facilitate the formation of intermediate filaments.
Subcellular location: [Isoform 1]: Cell junction, desmosome {ECO:0000269|PubMed:9369526}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:9369526}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:20613778}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20156963}. Cytoplasm {ECO:0000269|PubMed:20613778, ECO:0000269|PubMed:23444369}. Cell junction, desmosome {ECO:0000269|PubMed:20613778, ECO:0000269|PubMed:23444369}. Cell membrane {ECO:0000269|PubMed:20156963, ECO:0000269|PubMed:30949721}. Cytoplasm, Stress granule {ECO:0000269|PubMed:20156963}. Note=Colocalizes with EIF4A1 in stress granules following arsenate or hydrogen peroxide treatment (PubMed:20156963). Localizes to nucleoli following DNA damage (PubMed:20613778). Located in the cytoplasm during early tooth development, however localizes to the cell membrane in ameloblasts during molar growth (By similarity). Ca(2+)-mediated localization to the cell membrane in dental epithelial cells is inhibited via WNT3A (By similarity). Localizes to the cytoplasm when the phosphorylated form interacts with YWHAG (By similarity). Initially localized to the cytoplasm however as keratinocyte differentiation proceeds becomes localized to cell junctions as early cell-cell contacts become linear as part of membrane sealing (By similarity). Localized to lateral cell contacts in colocalization with DSP as epithelial sheet formation completes (By similarity). Protein stability is increased and localizes to the cytoplasm when phosphorylated at the N-terminus by AKT2 (PubMed:23444369). The unphosphorylated form is preferentially localized to desmosomes (PubMed:23444369). {ECO:0000250|UniProtKB:P97350, ECO:0000269|PubMed:20156963, ECO:0000269|PubMed:20613778, ECO:0000269|PubMed:23444369}.
Interaction partners:
- Desmoplakin
- Desmoglein-1
- Desmoglein-3
- Junction plakoglobin
- Plakophilin-3
- Desmocollin-1
- Desmoglein-2
- Desmocollin-3
- Envoplakin
- Periplakin
Sequence:
MNHSPLKTALAYECFQDQDNSTLALPSDQKMKTGTSGRQRVQEQVMMTVKRQKSKSSQSSTLSHSNRGSMYDGLADNYNYGTTSRSSYYSKFQAGNGSWGYPIYNGTLKREPDNRRFSSYSQMENWSRHYPRGSCNTTGAGSDICFMQKIKASRSEPDLYCDPRGTLRKGTLGSKGQKTTQNRYSFYSTCSGQKAIKKCPVRPPSCASKQDPVYIPPISCNKDLSFGHSRASSKICSEDIECSGLTIPKAVQYLSSQDEKYQAIGAYYIQHTCFQDESAKQQVYQLGGICKLVDLLRSPNQNVQQAAAGALRNLVFRSTTNKLETRRQNGIREAVSLLRRTGNAEIQKQLTGLLWNLSSTDELKEELIADALPVLADRVIIPFSGWCDGNSNMSREVVDPEVFFNATGCLRKRLGMRELLALVPQRATSSRVNLSSADAGRQTMRNYSGLIDSLMAYVQNCVAASRCDDKSVENCMCVLHNLSYRLDAEVPTRYRQLEYNARNAYTEKSSTGCFSNKSDKMMNNNYDCPLPEEETNPKGSGWLYHSDAIRTYLNLMGKSKKDATLEACAGALQNLTASKGLMSSGMSQLIGLKEKGLPQIARLLQSGNSDVVRSGASLLSNMSRHPLLHRVMGNQVFPEVTRLLTSHTGNTSNSEDILSSACYTVRNLMASQPQLAKQYFSSSMLNNIINLCRSSASPKAAEAARLLLSDMWSSKELQGVLRQQGFDRNMLGTLAGANSLRNFTSRF
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Q9JKA9)
Organism: Rattus norvegicus (Rat)
Function: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21796099}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
Sequence:
MDARGGGGRPGDSPGATPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRSRLCSRDSSCTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPAAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGAPAPSPAASARPASSSTPRLGPAPTTRTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL
Protein: Phosphoserine aminotransferase (EC 2.6.1.52) (Phosphohydroxythreonine aminotransferase) (PSAT) (P9WQ73)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Possible D-3-phosphoglycerate dehydrogenase SerA2
- D-3-phosphoglycerate dehydrogenase
- Phosphoserine phosphatase SerB2
- Uncharacterized protein Rv0885
- Threonine synthase
- L-cysteine desulfhydrase Cds1
- O-acetylserine sulfhydrylase
- S-sulfocysteine synthase
- Phosphoserine phosphatase SerB1
- Transcriptional regulator WhiB1
Sequence:
MADQLTPHLEIPTAIKPRDGRFGSGPSKVRLEQLQTLTTTAAALFGTSHRQAPVKNLVGRVRSGLAELFSLPDGYEVILGNGGATAFWDAAAFGLIDKRSLHLTYGEFSAKFASAVSKNPFVGEPIIITSDPGSAPEPQTDPSVDVIAWAHNETSTGVAVAVRRPEGSDDALVVIDATSGAGGLPVDIAETDAYYFAPQKNFASDGGLWLAIMSPAALSRIEAIAATGRWVPDFLSLPIAVENSLKNQTYNTPAIATLALLAEQIDWLVGNGGLDWAVKRTADSSQRLYSWAQERPYTTPFVTDPGLRSQVVGTIDFVDDVDAGTVAKILRANGIVDTEPYRKLGRNQLRVAMFPAVEPDDVSALTECVDWVVERL
Protein: Aconitase-ribosomal protein bL21m fusion protein [Includes: Homocitrate dehydratase, mitochondrial (EC 4.2.1.-) (Aconitase 2); Large ribosomal subunit protein bL21m (54S ribosomal protein L49, mitochondrial)] (Q9P7D4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Subcellular location: [Isoform Long]: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:25724335}. Nucleus {ECO:0000269|PubMed:25724335}.; SUBCELLULAR LOCATION: [Isoform Short]: Mitochondrion {ECO:0000269|PubMed:25724335}.
Interaction partners:
- Probable citrate synthase, mitochondrial
- Probable isocitrate dehydrogenase, mitochondrial
- Uncharacterized membrane protein C365.16
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Large ribosomal subunit protein uL4m
- Mitochondrial 2-methylisocitrate lyase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- NAD-dependent malic enzyme
- Uncharacterized protein P4H10.18c
Sequence:
MATFARMKLCLSGSSQAIPSKGISLVAARFQSTASRASYVTPPYEKLMGKLQQVRKFLPGQKLTLAEKVLYSHLVNPEESFSGVSPSDIRGSLYLKLNPDRVAMQDASAQMALLQFMTCGLEKTMIPASIHCDHLIVGHRGANSDIPDSIANNKEIFDFLQSAAKKYGIQFWGPGSGIIHQIVLENYAAPGGMMLGTDSHTPNAGGLGMIAIGVGGADAVDAMTNTPWELKAPKIIGVNLTGAMSGWTTPKDLILHLAGKLTVRGGTGHIIEYFGPGVASLSCTGMATVCNMGAEVGATTSIFPYTDSMRRYLIATHRAEVADAASEVHSEYNYLAADTGAKYDQIIDINLSELTPSLNGPFTPDLSTPVSKFGEAIEKNKWPKKLSAGLIGSCTNSSYQDMTCVVDVVEQAISAGLKPKVPFLVTPGSEQIRATIERDGITERLEEAGATVLANACGPCIGMWKRTDDIASGEPNAILTSFNRNFRSRNDGNPSTMNFLTSPVIVAAKIFSSDLAFDPTHDTLQTPDGKAFKFRPPQGVELPSAGFIAGDSSYIPEPNPQPVPETEVTIDPKSDRLEALEPFEPYQGGEMENLKVAVKVKGKCTTDHISAAGKWLKYKGHLSNICNNTLIGAMNAATGEVNRAYDNGKGMTIPELMWKWKKDGQPWLVVAEHNYGEGSAREHAALQPRAMNGRIILTKSFARIHETNLKKQGVLPLTFVNEADYEKIDAEDKVSTRGIEQLLEGVLDQPITLVVTKKDGSVVEIPCKHTMSKDQIEFFKAGSALNLIREKAHSGVVNQKVIDSIKQQPDHYADAYIFNRHFVIAKGDQLGLPFHLKGVQVGDTIRLDKIASFGSRDFTLFGNPYVDPSLFTIEAVVLSFPKSALSVRVKHKRRHRHDRVMKHKQTYTILRVTELKLN
Protein: Quinone oxidoreductase 1 (EC 1.6.5.5) (NADPH:quinone reductase 1) (Zeta-crystallin homolog protein) (P28304)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Malonyl CoA-acyl carrier protein transacylase
- Quinone oxidoreductase 2
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
Sequence:
MATRIEFHKHGGPEVLQAVEFTPADPAENEIQVENKAIGINFIDTYIRSGLYPPPSLPSGLGTEAAGIVSKVGSGVKHIKAGDRVVYAQSALGAYSSVHNIIADKAAILPAAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGTAQKAQSALKAGAWQVINYREEDLVERLKEITGGKKVRVVYDSVGRDTWERSLDCLQRRGLMVSFGNSSGAVTGVNLGILNQKGSLYVTRPSLQGYITTREELTEASNELFSLIASGVIKVDVAEQQKYPLKDAQRAHEILESRATQGSSLLIP
Protein: Cell division cycle-associated protein 4 (Hematopoietic progenitor protein) (Q9BXL8)
Organism: Homo sapiens (Human)
Function: May participate in the regulation of cell proliferation through the E2F/RB pathway. May be involved in molecular regulation of hematopoietic stem cells and progenitor cell lineage commitment and differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16984923}.
Interaction partners:
- SERTA domain-containing protein 1
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Borealin
- Sororin
Sequence:
MFARGLKRKCVGHEEDVEGALAGLKTVSSYSLQRQSLLDMSLVKLQLCHMLVEPNLCRSVLIANTVRQIQEEMTQDGTWRTVAPQAAERAPLDRLVSTEILCRAAWGQEGAHPAPGLGDGHTQGPVSDLCPVTSAQAPRHLQSSAWEMDGPRENRGSFHKSLDQIFETLETKNPSCMEELFSDVDSPYYDLDTVLTGMMGGARPGPCEGLEGLAPATPGPSSSCKSDLGELDHVVEILVET
Protein: tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] (EC 1.3.1.88) (Q57V78)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTYNEAALSKYRGLLDSGEPFRSRTCRYCSSGNTAVKHINSKKKPNSPWDFWNGIACSPTASHARAEGRKRTPMYVVGPMVDQSELPFRLLCRRYGATLAYTPMFHAKSFAQSAHYRQRYFSTTTFPPHSAMESGGNVAANDSTSNDGALDNDHPLFAQFCGNDPETVLAAARHVEDYCEAVDFNIGCPQGIARRGHYGSFLMEDWELLHNILHALAVELRVPVTAKMRIFDDEALTLKYAEMLRDTGIYVLCVHGRTRENKGQQQQPADLRMIRRVHEHLRGSIPIIANGNVLTFEDVPRNLAITGCEGYMCAEPLLWDPKLFAPLASSSTAEFAPNITDSTLSTSPAPSTVRSGRLFAESRPTRLKALATASEYLELVRRFPVDIGFVKAHFFKMLYHSYEMHPAHQQWLANFSINGSNVGNDVVENCATSHCGEQRETTVVGRDIFTAALDALTDHLHSLQKAELSLEHDGPQPKRQRELKVGEEGKERQQLKNGRRVDALTDTFADDETLGIDFLM
Protein: Metalloreductase STEAP2 (EC 1.16.1.-) (Six-transmembrane epithelial antigen of prostate 2) (Q8BWB6)
Organism: Mus musculus (Mouse)
Function: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- STEAP1 protein
Sequence:
MESISMMGSPKSLETFLPNGINGIKDARQVTVGVIGSGDFAKSLTIRLIRCGYHVVIGSRNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNMRVNQYPESNAEYLASLFPDSLIVKGFNVISAWALQLGPKDASRQVYICSNNIQARQQVIELARQLNFIPVDLGSLSSAKEIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYARNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLDTWLQCRKQLGLLSFFFAVVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENAWNEEEVWRIEMYISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLITTFHVLIYGWKRAFAEEYYRFYTPPNFVLALVLPSIVILGKMILLLPCISRKLKRIKKGWEKSQFLDEGMGGAVPHLSPERVTVM