wanglab/gogpt-training-data huggingface dataset:
Protein: Cystathionine gamma-lyase (CGL) (CSE) (EC 4.4.1.1) (Cysteine desulfhydrase) (Cysteine-protein sulfhydrase) (Gamma-cystathionase) (Homocysteine desulfhydrase) (EC 4.4.1.2) (P32929)
Organism: Homo sapiens (Human)
Function: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione. Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L-homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce the endogenous gaseous signaling molecule hydrogen sulfide (H2S). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, also two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia (which is a risk factor for cardiovascular disease, diabetes, and Alzheimer's disease). Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function. By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (Probable). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (By similarity). Can also accept homoserine as substrate (By similarity). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Cystathionine beta-synthase
- Cystathionine beta-synthase-like protein
- 3-mercaptopyruvate sulfurtransferase
- Thiosulfate sulfurtransferase
- Methylenetetrahydrofolate reductase
- Methionine synthase
- Betaine--homocysteine S-methyltransferase 1
- Adenosylhomocysteinase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Cysteine dioxygenase type 1
Sequence:
MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEYSRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVLKNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS
Protein: KAT8 regulatory NSL complex subunit 3 (NSL complex protein NSL3) (Non-specific lethal 3 homolog) (A2RSY1)
Organism: Mus musculus (Mouse)
Function: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9P2N6}. Mitochondrion {ECO:0000250|UniProtKB:Q9P2N6}.
Interaction partners:
- KAT8 regulatory NSL complex subunit 2
- PHD finger protein 20
- Microspherule protein 1
- KAT8 regulatory NSL complex subunit 1
- WD repeat-containing protein 5
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Host cell factor 1
- Histone acetyltransferase KAT8
- KAT8 regulatory NSL complex subunit 1-like protein
- MSL complex subunit 3
Sequence:
MAHRGGERDFQTSARRMGTSLLFQLSVHERELDLVFLDHSYAKPWSAHPDASSARPTRMLFVTPRRQQENTIESDVPIDVETVTATPVPLYDNQKARSVMNECERHVIFARTDADAPPPPEDWEEHVNRTGWTVAQNKLFNKILKALQSDRLARLANEGACNEPVLRRVAVDKCARRVRQALASVSWDTKLTQWLHTTLVETLSLPMLAAYLDALQTLKGKIPTLIDRMLVSSNTKTGAAGAEALSLLLKRPWDPAVGVLSHNKPSKLPGSPLILIVSSGPSSSVFPASRRHRFWQSQLSCLGKVIPVATHLLNNGSGVGVLQCLEHMIGAVRSKVLEIHSHFPHKPIILIGWNTGALVACHVSVMEYVTAVVCLGFPLLTVDGPRGDVDDPLLDMKTPVLFVIGQNSLQCHPEAMEDFREKIRAENSLVVVGGADDNLRISKAKKKSEGLTQSMVDRCIQDEIVDFLTGVLTRAEGHVGSEPRDQDAEKKKKPRDLTRRDLAFEIPERGSRPASPAARLPTSPSGSEDLSSVSSSPTSSPKTKVTTVTSTQKSSQIGTSQLLKRHVQRTEAVLTHRQAQAQFAAFLKQNMLVRKAFPPGTSSCLFVPISSESVEDIEKEELRVQLKRHHSSSPLPGAKPSKRPKIKVSLISQGDTVGGPCTLSQGGTPEAAGGKPITMTLGASAGAKELTGLLTTAKSSSSEGGGTASTTPSVASSSATPNAIHTLQSRLVATSPGSSLPGTASASSLLQGLSFSLQDISSKTSGLPGSPSPGPAPQATSVKLPTPMQSLGAITTGTSTIVRTIPVATTLSSLGATPGGKPTAIHQLLTNGSLAKLASSLPGLAQISNQASGLKVPTTITLTLRGQPSRITTLSPMGSGATPSEEPNSQMLPSSSQRLPPAP
Protein: nicotinamidase (EC 3.5.1.19) (Nicotinamide deamidase) (Q38FD5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- nicotinate phosphoribosyltransferase
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MSTSRITLSSQHDALIIVDMQNDFVLPDGALSVTGATEIIPIINRVVGDHQFRAVVASMDWHPPGHMSFRNEDGTGGPWPPHCVRSTTGAQLHSEMKQGEITHLIHKATSLDSESYSAFSDDSGKTTGLAAMLRAMDVRRVFMCGVASDYCVYFTSLHAIQEEFTVVVLEDAVRPVDPVAMEKKRAHLEKEGVIFARSTDLSSF
Protein: G-protein coupled receptors family 1 profile domain-containing protein (A0A060YND6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Anaphylatoxin-like domain-containing protein
- Ig-like domain-containing protein
Sequence:
MDDMCSILTEEELSLYNITDCEFVKPGGLGPVLGPRHLSALVFYGLVFLLGVPGNALVVWVTGFRMPRSVTSLWFLNLALADLLCCLSLPLLMVPLAMDQHWPFGPVACKLLKGLLYLIMFCSVLLLVLISLDRFLLVSWPVWCQNWRRPRKAGWVCVGVWLLALLGSIPQFVYVKEVQLSTSKSECLGLYTVASAWANTTARFLVGFVLPFITIVTCHWVVYSRARRGSGVGPGRVSEARSRRTLRVIVAVSLSFFLCWFPLHILDFLVLSTPRHSSHSANIQLAHTLALCLAYCNSCLNPLLYVCLGRGFKQNINRSLRNMFNFATEESVTRQSMFKSTSERTQEMNM
Protein: Transmembrane protein (Q54TI1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MENNNLNITIDPGLTNNIENYNNNNINNNNINNNNNNNNNNNNNNNNNNNNNNNNNEEIKNEIKISNDQNLIGSPYSNLGMSTEDIMSNSSMVGSCERLRISKMDSSVCSSYNEDKLKNFEDSETKGEENEKNGKMKEMDINTPNEMEDGEIGWRGLKTLRLIAERYLFGIIVAAVVGLLIILLSLPDWSNGPAGFNEKTYNIFFIISSIFFGPLYVVGGFIASYGIERVKDARIIIYGTSIGIGFIVLYVVFAVKEIRYWYYYLDVVSVVLIFSFVEVIFSFRMSNVIQKAERSVVCTMKSVWTAYNYAAPDIVVTLFSLVYMFFLIPVYLTIENSIFRLGWRLVIHPIYWTVIVMIARQFLDRDISTTDIMLNTNIVLHTFFHHQTLGKIFVFTFDDSGSTQLTYIGICVSAIEDIFLRSIALKRDEWFFTFLYDKSRAVKQVYSQESLQLRAAILNIQTALDFSGLITAPLFVFMFSKHKHVFHVLEGSTVVPLTLFIQSLLSIFLDFGVEITCTYIETKYYRLPIKTTWDWMKSHKLSFMTWLIYGSCTMGLLAMIWLMAMIPRVGQSVYN
Protein: NEDD8-activating enzyme E1 regulatory subunit (Amyloid beta precursor protein-binding protein 1, 59 kDa) (APP-BP1) (Amyloid protein-binding protein 1) (Q9Z1A5)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14557245}. Note=Colocalizes with APP in lipid rafts.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-like protein NEDD8
- Amyloid-beta precursor protein
- NEDD8-conjugating enzyme UBC12
- NEDD8-conjugating enzyme UBE2F
- Cullin-1
- Origin recognition complex subunit 4
- E3 ubiquitin-protein ligase RBX1
- Sentrin-specific protease 8
- Cullin-3
Sequence:
MAQQGKILKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDVGNNFFLQKCSIGKNRAQAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKSYKEKEDFRELIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSNKYIKLQNVYREKAKKDAAAVGNHVAKLLQSCGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLHTVNKDEIISSMDNPDNEIVLYLMLRAVDRFHKQHGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTVAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL
Protein: Nebulin (Q61953)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KYTMDPELPQFIQAKVNAINMSDAHYKADWKKTLAKGYDLRPDAIPIVAAKSSRNIASDCKYKEAYEKARGKQIGFLSLQDDPKLVHYMNVAKIQSDREYKKGYEASKTRYHTPLDMFSVTAAKKSQEVATNSNYRQPYHNYTLLPDALNVEHSRNAMQIQSDNLYKSDFTHWMKGIGWVPIDSLEVEKAKKAGEILSERKYRQHPEKLKFTYSMDTMEQALNKTNKLTMDKRLYTEKWNKDKTSIHVMPDTPDILLSRVNQITMSDKLYKAGWEEEKKKGYDLKPDAIAIKAAKASRDIASDYKYKQAYEQAKGKHIAFRSLEDDPKLVHFMQVAKIQSDREYKKGYEKSKTSFHTPVDMFSVVAAKKSQEVATNANYRNIIHTYNMLPDAMSFELAKNMMQIQSDNQYKADYADFMKGIGWL
Protein: Prolactin (PRL) (P06879)
Organism: Mus musculus (Mouse)
Function: Prolactin acts primarily on the mammary gland by promoting lactation.
Subcellular location: Secreted.
Interaction partners:
- Prolactin receptor
- Somatotropin
- Leptin
- Glycoprotein hormones alpha chain
- Pro-opiomelanocortin
- Erythropoietin
- Tyrosine-protein kinase JAK2
- Thrombopoietin
- Granulocyte colony-stimulating factor
- Ciliary neurotrophic factor
Sequence:
MNSQGSAQKAGTLLLLLISNLLFCQNVQPLPICSAGDCQTSLRELFDRVVILSHYIHTLYTDMFIEFDKQYVQDREFMVKVINDCPTSSLATPEDKEQALKVPPEVLLNLILSLVQSSSDPLFQLITGVGGIQEAPEYILSRAKEIEEQNKQLLEGVEKIISQAYPEAKGNGIYFVWSQLPSLQGVDEESKILSLRNTIRCLRRDSHKVDNFLKVLRCQIAHQNNC
Protein: Sodium/potassium/calcium exchanger 1 (Na(+)/K(+)/Ca(2+)-exchange protein 1) (Retinal rod Na-Ca+K exchanger) (Solute carrier family 24 member 1) (Q28139)
Organism: Bos taurus (Bovine)
Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Critical component of the visual transduction cascade, controlling the calcium concentration of outer segments during light and darkness. Light causes a rapid lowering of cytosolic free calcium in the outer segment of both retinal rod and cone photoreceptors and the light-induced lowering of calcium is caused by extrusion via this protein which plays a key role in the process of light adaptation (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:1582405}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ssu-2 homolog
- Rhodopsin kinase GRK7
- Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3
- Retinol dehydrogenase 12
Sequence:
MGKLIRMGAQERRSLWPKRLHWSRPLFLLGMLIIGSTYQYLTSPQGLPTLWAAVSSQHPVKVASRDLSNKEMMMVSSETSKSSSEMEVEAWAPEATAGRDGTPPGIARKNTPSTPRGTASITPAIPNNYSPTPTGTGKVKEDTSATPSGVLNHYTQSRPMVNSYTRLTARGEVKSSRPTQSRGKEEKYSPSPLGRMVNSYAPSTLMTMPRSHGITPRTTVKDREIMATKKMLATNPSKRLVEKTTPTPLKGITDNTPTFLLSDLETDTLTSPRNVVEKKTLTTPRRVDSNSSTNHQGLVGKNNLTTPQGMVLEHTAAVSEGQVTISTMTRSSPTETKASTDAWKVRNPLPRTSAPIIRISSATFRGLLKNPSKAPSTPAAPRVRANPTIQVRHCLVVEPAPVAPTAPSPSWTTAVIPGIPSPSGQPDLYPKAEYPRDLFSVEERRQGWVVLHIFGMMYVFVALAIVCDEYFVPALGVITDKLQISEDVAGATFMAAGGSAPELFTSLIGVFISHSNVGIGTIVGSAVFNILFVIGTCALFSREILNLTWWPLFRDITFYIFDLMMLILFFLDSLIAWWESVLLLLAYAFYVFTMKWNQQLELWVKEQLNKRPVAKVMALGDLSKPGDGTVVVDEQQDNKKLKLSSMLTRGSSSASLHNSTIRSTIYQLMLHSLDPLGEARPSKDKEEETLIPEAKATPQAKAESKPEEEPAKLPEVTVTPAPAPDVKGDQEEDPGSQGVGAEAENTGERTGGEAEAPAEGENGERSGGDAALGGESEGKAENESEGDIPAERRGDDEDEGEIQAEGGEVKGDEDEGEIQAGEGGEVEGDEDEGEIQAGEGGEVEGDEDEGEIQAGEAGEVEGDEDEGEIQAGEGGEVEGDEDEGEIQAGEAGEVEGDEDEGEIQAGEGGEVKGDEGEIQAGEAGEVEGEDGEVEGGEDEGEIQAGEGGEGETGEQELNAEIQGEAKDDEEGVDGEGGGDGGDSEDEEEEDEEEEDEEEEEEEEEEEEEENEQPLSLEWPETRRKQAIYLFLLPIVFPLWLTVPDVRRLEAKKFFVITFLGSILWIAMFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWMLFSLINGLQPVAVSSNGLFCAIVLLFLMLLFVISSIALCKWRMNKILGFTMFLLYFVFLIISVMLEDRIISCPVSV
Protein: Neutral sphingomyelinase activation associated factor (Q7TSY5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAFTRKRQREQQLQLYSKERFSLLLLNLEEYYFEQHTAFHVQHQGSPEERKIRGSLKICSKSVIFEPDAISQPILKIPLRDCLKIGKHGENGANKHFAKAKSLGISLISSQVYFIKEHNIVAPYKIERGKMEYVFQLEVSGKVEDVVETLLQLHRASCLDKLGDQMAMITAILQSRLARTSFDKNRFQSVSEKLHMECKAEMMTPLVTNSGHVCITDTNLYFQPLNGYPKPVVQITLQDVRRIYKRRHGLMPLGLEVFCTEDDLCSDIYLKFYEPQDRDDLYFYIATYLEHHVAEHTAESYMLQWQRGHLSNYQYLLHFNNLADRGCNDLSQYPVFPWVISDYSNPELDLSNPATFRDLSKPVGALNPERLERLLTRYQEMPEPKFMYGSHYSSPGYVLFYLVRIAPEYMLCLQNGRFDNADRMFNSIVETWKNCLDGATNFKELIPEFYDEDASFLINSLKLDLGKRQGGQMVDDVELPAWASSPQDFLQKNKDALESSYVSEHLHEWIDLIFGYKQKGSEAIGAHNVFHPLTYEGGVDLNSIEDPDDKVAMLTQILEFGQTPKQLFVTPHPRRITPKFKSLSQASSYNASMTDSPVSPGEESFEDLTEESKTLAWNNITKLQLHEQYKIHKEAVTGIAVSCNGSSVFTTSQDSTLKMFSKESKMLQRSISFSIWALSSCLLLPGDTTVISSSWDNNVYFYSIAFGRRQDTLMGHDDAVSKICWHNDRLYSASWDSTVKVWSGVPAEMPGTKRHQFDLLAELEHDVSVNTINLNAVSTLLVSGTKEGLVNIWDLTTATLLHQISCHSGTVCDAAFSPDSRHVLSTGVDGCLNVIDVQTGMLISSMASEEPQRCFVWDGNSVVSGSRTGELLVWDLLGAKVSERIQGHTGAVTCIRMNEQCSSIITGGEDRQVMFWKLQY
Protein: Pseudouridylate synthase 1 homolog (EC 5.4.99.-) (tRNA pseudouridine synthase 1) (EC 5.4.99.12) (tRNA pseudouridine(38-40) synthase) (tRNA pseudouridylate synthase I) (tRNA-uridine isomerase I) (Q9WU56)
Organism: Mus musculus (Mouse)
Function: Pseudouridylate synthase that catalyzes pseudouridylation of tRNAs and mRNAs. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' (By similarity). Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions (By similarity). Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing (By similarity). Involved in regulation of nuclear receptor activity through pseudouridylation of SRA1 mRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y606}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y606}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y606}.
Interaction partners:
- tRNA
- Pseudouridylate synthase 7 homolog
- Pseudouridylate synthase TRUB1
- H/ACA ribonucleoprotein complex subunit DKC1
- tRNA pseudouridine synthase Pus10
- Pseudouridylate synthase TRUB2, mitochondrial
- Pseudouridylate synthase RPUSD4, mitochondrial
- tRNA
- Mitochondrial mRNA pseudouridine synthase Rpusd3
- Pseudouridylate synthase PUS7L
Sequence:
MGFPRLWAALLRNWGRWTARPGPRVPGLPPMAGNKVPPALASHQPDRKGRGGWVWEETEHPAKRVKGGEDEEPPRKLPKRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKDRDVQDESYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVDVPKAPGLGLVLERVHFEKYNQRFGGDGLHEPLDWTQEEGKVTAFKEQYIYPTIVSTERDERSMAQWLNTLPIHNFSGTALGAADTGAKVPSSLEGSEGDGDTD
Protein: Regulator of g protein signaling domain containing protein (C4LYV4)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Interaction partners:
Sequence:
MAATETAILEGWPTLQEVLEDSFMKRLLRCYLSDERSEENLDFLESVGLYESQFDKLTPKVRLEALNFIKDQFLDRNSERQVNLSYQIQQSILKKLSEVTSNAPKDVFNEAKKATEYLLYTEQYTYFINKLNANTIGTGKKDVYSLYLNQFPKTNPQPLYKPTLNKIIEIEKKSWNEDEVKRNTESIKSLVESLIQDECNYVGVLTSLSEFSEIMTKKQILGPDVLKELFDHIPVLIQHHQKFISSLQEAKADEKVGEKLNSGLHFLVLYRYYLRHVPKNIAKLCSIGMTDEIEVGRELYPLPVIEEFDKQQKMTKKMSVLQMLVYPYFRVRTYQAYVDDFIKITKKDSQEVKELEVVHSQLAIFQELINTYSDINKIERISDALKLLFPFSFTSIMPLFEGKNGICGIASLDRFDKTDINQLSMSLNSRKKLTLIILYRGVVVTDVPVIRKKGNVSNSIDKSFYSFTLIGDIRDFGTEDSTETIYIDVPEIKKRIWFGCESTEEFKSCVEALRTILSN
Protein: LIM and senescent cell antigen-like-containing domain protein (C0KUC6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|PIRNR:PIRNR038003}. Cell membrane {ECO:0000256|PIRNR:PIRNR038003}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR038003}.
Interaction partners:
- Scaffold protein ILK
- Alpha-parvin
- Ras suppressor protein 1
- Parvin, beta
- Cytoplasmic protein
- Gamma-parvin
- FERM domain containing kindlin 2
Sequence:
MAFPGRARPSTIPENEEIPQTALNSVLEANGNEDERAVSNLQRRHSDIKVYKEFCDFYAKFNMANALASATCERCKGGFDPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVSCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSETLGRK
Protein: Carbonic anhydrase 15 (EC 4.2.1.1) (Carbonate dehydratase XV) (Carbonic anhydrase XV) (CA-XV) (Q99N23)
Organism: Mus musculus (Mouse)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MWALDFLLSFLLIQLAAQVDSSGTWCYDSQDPKCGPAHWKELAPACGGPTQSPINIDLRLVQRDYTLKPFIFQGYDSAPQDPWVLENDGHTVLLRVNSCQQNCPAIRGAGLPSPEYRLLQLHFHWGSPGHQGSEHSLDEKHGSMEMHMVHMNTKYQSMEDARSQPDGFAILAVLLVEEDRDNTNFSAIVSGLKNLSSPGVAVNLTSTFALASLLPSALRLLRYYRYSGSLTTPGCEPAVLWTVFENTVPIGHAQVVQFQAVLQTGPPGLHPRPLTSNFRPQQPLGGRRISASPEASVRSSVSTLPCLHLALVGLGVGLRLWQGP
Protein: General transcription factor IIH subunit (Q8IEG6)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR015919}.
Interaction partners:
- RNA polymerase II transcription factor B subunit 4, putative
- DNA 5'-3' helicase
- General transcription factor IIH subunit 4
- DNA 3'-5' helicase
- CDK-activating kinase assembly factor MAT1
- BSD domain-containing protein
- Transcription initiation factor IIE subunit alpha, putative
- Cyclin 1
- DNA-directed RNA polymerase II 16 kDa subunit, putative
- DNA-directed RNA polymerase II subunit RPB3, putative
Sequence:
MQNPQNSENKVIFVEDVVRDFDENEIFEEITGKFTWEQDVERSWNLLVENNGVLQHVSQENNENENKEKYRKNQGSSLRKGIFRHIIILFDMSSSMKERDLKPDRINVALECVESFLKNFFFKNPVGHVGVVALKNSSAKLIQPFTSNVDDILNSILKERTAGLQGSPSLEEGLQIAHDLLIDMPLYGTKEVLIMYGSIRTCDKKNILNVLELLVKSNIYVNCISIAPEMHILKHICEKSNGFYKICSSKNSLMNEINNNAETPLWMQGMEPQLIHICFPTKKKISTQIMCSCHGKLNTDTYVCNFCNSYTCKIPSKCKVCGIHLISMHDLSHITNNLQGSPLFIEIKNEQGNYKVCSSCNQQLYNKIYQCTKCQHIFCLECDIFIHEELNQCPFCLINDT
Protein: Nck-associated protein 1 (NAP 1) (Brain protein H19) (MH19) (Membrane-associated protein HEM-2) (p125Nap1) (P28660)
Organism: Mus musculus (Mouse)
Function: Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14765121}; Single-pass membrane protein {ECO:0000269|PubMed:14765121}; Cytoplasmic side {ECO:0000269|PubMed:14765121}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:14765121}; Single-pass membrane protein {ECO:0000269|PubMed:14765121}; Cytoplasmic side {ECO:0000269|PubMed:14765121}. Cytoplasm {ECO:0000269|PubMed:14765121}. Note=At the interface between the lamellipodial actin meshwork and the membrane.
Interaction partners:
- Cytoplasmic FMR1-interacting protein 1
- Abl interactor 2
- Protein BRICK1
- Actin-binding protein WASF1
- Abl interactor 1
- Cytoplasmic FMR1-interacting protein 2
- Actin-binding protein WASF3
- Actin-binding protein WASF2
- ABI gene family member 3
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MSRSVLQPSQQKLAEKLTILNDRGVGMLTRLYNIKKACGDPKAKPSYLIDKNLESAVKFIVRKFPAVETRNNNQQLAQLQKEKSEILKNLALYYFTFVDVMEFKDHVCDLLNTIDVCQVFFDITVNFDLTKNYLDLTVTYTTLMILLSRIEERKAIIGLYNYAHEMTHGASDREYPRLGQMIVDYENPLKKMMEEFVPHSKSLSDALISLQMVYPRRNLSADQWRNAQLLSLISAPSTMLNPAQSDTMPCEYLSLDAMEKWIIFGFILCHGMLNTEATALNLWKLALQSSSCLSLFRDEVFHIHKAAEDLFVNIRGYNKRINDIRECKEAAVSHAGSMHRERRKFLRSALKELATVLSDQPGLLGPKALFVFMALSFARDEIIWLLRHADNMPKKSADDFIDKHIAELIFYMEELRAHVRKYGPVMQRYYVQYLSGFDAVVLNELVQNLSVCPEDESIIMSSFVNTMTSLSVKQVEDGEVFDFRGMRLDWFRLQAYTSVSKASLSLADHRELGKMMNTIIFHTKMVDSLVEMLVETSDLSIFCFYSRAFEKMFQQCLELPSQSRYSIAFPLLCTHFMSCTHELCPEERHHIGDRSLSLCNMFLDEMAKQARNLITDICTEQCTLSDQLLPKHCAKTISQAVNKKSKKQTGKKGEPEREKPGVESMRKNRLVVTNLDKLHTALSELCFSINYVPNMAVWEHTFTPREYLTSHLEIRFTKSIVGMTMYNQATQEIAKPSELLTSVRAYMTVLQSIENYVQIDITRVFNNVLLQQTQHLDSHGEPTITSLYTNWYLETLLRQVSNGHIAYFPAMKAFVNLPTENELTFNAEEYSDISEMRSLSELLGPYGMKFLSESLMWHISSQVAELKKLVVENVDVLTQMRTSFDKPDQMAALFKRLSSVDSVLKRMTIIGVILSFRSLAQEALRDVLSYHIPFLVSSIEDFKDHIPRETDMKVAMNVYELSSAAGLPCEIDPALVVALSSQKSENISPEEEYKIACLLMVFVAVSLPTLASNVMSQYSPAIEGHCNNIHCLAKAINQIAAALFTIHKGSIEDRLKEFLALASSSLLKIGQETDKTTTRNRESVYLLLDMIVQESPFLTMDLLESCFPYVLLRNAYHAVYKQSVTSSA
Protein: Potassium voltage-gated channel subfamily KQT member 4 (KQT-like 4) (Potassium channel subunit alpha KvLQT4) (Voltage-gated potassium channel subunit Kv7.4) (Q9JK96)
Organism: Rattus norvegicus (Rat)
Function: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea.
Subcellular location: Basal cell membrane {ECO:0000269|PubMed:11042367}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56696}. Note=Situated at the basal membrane of cochlear outer hair cells. {ECO:0000269|PubMed:11042367}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily Q member 5
- Potassium voltage-gated channel subfamily KQT member 3
- Inward rectifier potassium channel 4
- ATP-sensitive inward rectifier potassium channel 12
- Inward rectifier potassium channel 2
- ATP-sensitive inward rectifier potassium channel 14
- Potassium voltage-gated channel subfamily E regulatory subunit 4
- Potassium voltage-gated channel subfamily E member 1
Sequence:
MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIIRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDTSRAYLTATWYYYDSILPSFRELALLFEHIQRARNGGLRPLEVRRAPVPDGAASRYPPVATCHRPGSASFCPGESSRMGIKDRIRMSSSQKRTGPSKQHLAPPPIPTSPSSEQVGEASSPSKVQKSWSFNDRTRFRASLRLKPRCSTEEGPSEEVAEEKSYQCELTVDDVMPTVKTVIRSVRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQARVDQIVGRGPGDRKTREKGDKGPSDTEAVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGTVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD
Protein: NADH dehydrogenase subunit 9 (Q2F951)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MDNQSIFQYSWEILPKKWVHKMKRSEHGNRSYTNTDYPFPLLCFLKWHTYTRVQVSIDICGVDHPSRKRRFEVVHNLLSTRYNSRIRVQTSADEVTRISPVVSPFPSAGRWEREVWDMSGVSSINHPDLRRISTDYGFEGHPLRKDFPLSGYVEVRYDDPEKRVVSEPIEMTQEFRYFDFASPWEQRSDG
Protein: TM2 domain-containing protein 3 (Beta-amyloid-binding protein-like protein 2) (BBP-like protein 2) (Q9BRN9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Threonine--tRNA ligase 2, cytoplasmic
Sequence:
MAGGVLPLRGLRALCRVLLFLSQFCILSGGEQSQALAQSIKDPGPTRTFTVVPRAAESTEIPPYVMKCPSNGLCSRLPADCIDCTTNFSCTYGKPVTFDCAVKPSVTCVDQDFKSQKNFIINMTCRFCWQLPETDYECTNSTSCMTVSCPRQRYPANCTVRDHVHCLGNRTFPKMLYCNWTGGYKWSTALALSITLGGFGADRFYLGQWREGLGKLFSFGGLGIWTLIDVLLIGVGYVGPADGSLYI
Protein: Endothelial cell-selective adhesion molecule (Q96AP7)
Organism: Homo sapiens (Human)
Function: Can mediate aggregation most likely through a homophilic molecular interaction.
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q925F2}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q925F2}. Cell membrane {ECO:0000269|PubMed:36996813}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q925F2}.
Interaction partners:
- Occludin
- Claudin-5
- Tight junction protein 1
- Cadherin-5
- Claudin-1
- Claudin-7
- Claudin-2
- P-selectin
- von Willebrand factor
- Sodium/potassium-transporting ATPase subunit beta-1
Sequence:
MISLPGPLVTNLLRFLFLGLSALAPPSRAQLQLHLPANRLQAVEGGEVVLPAWYTLHGEVSSSQPWEVPFVMWFFKQKEKEDQVLSYINGVTTSKPGVSLVYSMPSRNLSLRLEGLQEKDSGPYSCSVNVQDKQGKSRGHSIKTLELNVLVPPAPPSCRLQGVPHVGANVTLSCQSPRSKPAVQYQWDRQLPSFQTFFAPALDVIRGSLSLTNLSSSMAGVYVCKAHNEVGTAQCNVTLEVSTGPGAAVVAGAVVGTLVGLGLLAGLVLLYHRRGKALEEPANDIKEDAIAPRTLPWPKSSDTISKNGTLSSVTSARALRPPHGPPRPGALTPTPSLSSQALPSPRLPTTDGAHPQPISPIPGGVSSSGLSRMGAVPVMVPAQSQAGSLV