wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized inositol polyphosphate kinase C970.08 (EC 2.7.-.-) (O74561)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Inositol-pentakisphosphate 2-kinase
- Adenylate kinase
- Putative inorganic phosphate transporter C8E4.01c
Sequence:
MQNAPKCYLPNSRKGRDVNFHDRGPETLKCLYDESEDNNNFTMHSESIGPKSLDSLSPRRLSNYSSAVDPRTTSLEDVPRLILTRSNSQEQTPLRTHTPVEYMSDSIHKSLADLQLGGSSYSVAESPVPVLQSSAVSEADDMASAHSAHPSRKASRSLRLFESSTSNNLETGNSTNTALHNVSSPLESVSERLSKSGSPSVGAQHDLDEVISEKDTSLSRRSSRGRSSAPKRRKDSGSSKTTATYIPHNPSKKSSQHLPLLPDASFELERSVSRSYQSPASTPRSSVSSVSSSPPEDHPFFHWNVDYPVTVRLEPFKHQVGGHTAFFRFSKRAVCKPLTRNENTFYETIEACHPELLPFIPKYIGVLNVTHTITKTEENDSTTEYVNTESSSKTPAPHKHTFNSCYQKKDYGYIPEVSVEQNRHIFPEWMLPDKRSHSYGSPKSLHHKSSSAGERPVSPTFVADIPPKTPWGTTLINRKLREEVLREVFAPKHARRRLGTRFHSRSSHRPSVFRDNSVAFGQLDNGNTSSRARDKDADPNKSLSCSVEDKHYDLHSAVAEENEEVDEELLNVPSNNQGKSYRRFSSDAVWEEPESNEFPRVSGTMEDYDSRESTGHTIKELRSTPNSHGTVPDDSIFAMDNEENSELPPPLEPAEIGDPFRSVNDPRRVLSLPHMASADEDHRIPASDNQNNNNNDANALAENSESQHSTQIERYIVIEDLTSGMKRPCVLDVKMGTRQYGIMATEKKKASQTKKCAMTTSRVLGVRICGMQVWHPWLQSYTFEDKYVGRDIKAGEEFQHALMRYLGKTDDDEDNSHLLVHHIPTIIRKLEQLEQIVRFLKGSRLYASSLLFLYDGEPPPSDKSSKEKVKPREIDIRIVDFANCVFAEDKELLAKATCPPQHKDTYDRGYVRGLRTLRLYFLKIWKEAKGMQIAERGYEDSLSNAYDELGGLMSYSNDDDSCGETST
Protein: Cytochrome b-c1 complex subunit Rieske-2, mitochondrial (EC 7.1.1.8) (Complex III subunit 5-2) (Rieske iron-sulfur protein 2) (RISP2) (Ubiquinol-cytochrome c reductase iron-sulfur subunit 2) (Q9LYR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11870776, ECO:0000269|PubMed:12606038, ECO:0000269|PubMed:18189341}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 7-2, mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 6-2, mitochondrial
- Cytochrome b-c1 complex subunit 6-1, mitochondrial
- Cytochrome c oxidase subunit 1
- NADH dehydrogenase 1 alpha subcomplex subunit 9
Sequence:
MLRVAGRRLFSVSQRSSTATSFVLSRDHTLSDGGNSSSASRSVPSADLSSFNSYHRSVIRGFASQVITQGNEIGFGSEVPATVEAVKTPNSKIVYDDHNHERYPPGDPSKRAFAYFVLSGGRFVYASVLRLLVLKLIVSMSASKDVLALASLEVDLGSIEPGTTVTVKWRGKPVFIRRRTEDDIKLANSVDVGSLRDPQEDSVRVKNPEWLIVVGVCTHLGCIPLPNAGDYGGWFCPCHGSHYDISGRIRKGPAPYNLEVPTYSFLEENKLLIG
Protein: MRH domain-containing protein (Q383K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Derlin
- Derlin
- RING-type domain-containing protein
- E3 ubiquitin-protein ligase CHFR
- RING-type E3 ubiquitin transferase
- UBX domain-containing protein
Sequence:
MYATRAKVLLFRLATFVLVSVVRGQEEVTEHKYNIVFSRDPVPSGLSEEQYYPMRLSNGSAYLCVLPDITVEEKKTLQAEDSELDVPLSLEHVAVVNRALKNMCYTMEESWWTYRLCWGSGVEQFHRSAVAGDSKSNAPKQMKEDPHFVLGVAPPADVLDLRYGVNTKGLRYIYTIYSDGLTCDLTQLPRTTEVQLYCAREGEGNSPTMRVREAEVCRYIVSLTAKEVCLLGLKEIQQRYGVITCHETKPTNTVDWNNKQQG
Protein: Voltage-gated potassium channel KCNC1 (NGK2) (Potassium voltage-gated channel subfamily C member 1) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4) (P48547)
Organism: Homo sapiens (Human)
Function: Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well. Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25401298}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P25122}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P25122}. Note=Localizes in parallel fiber membranes, distributed on the perisynaptic and extrasynaptic membranes away from the active zones. {ECO:0000250|UniProtKB:P25122}.
Interaction partners:
- A-type potassium channel modulatory protein KCNIP1
- Calsenilin
- A-type potassium channel modulatory protein KCNIP2
- Kv channel-interacting protein 4
- Ubiquitin-like protein FUBI
- Voltage-gated potassium channel KCNC4
- Voltage-gated potassium channel subunit beta-1
- Caveolin-3
- A-type potassium channel modulatory protein DPP6
- Voltage-gated potassium channel subunit beta-2
Sequence:
MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVIFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRAGRKPLRGMSI
Protein: Reticulon-like protein B6 (AtRTNLB6) (Q6DBN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9SH59}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15060130}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Reticulon-like protein B21
- Reticulon-like protein B18
- AT3g15480/MJK13_14
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- Reticulon-like protein B17
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- Tetraspanin-3
- Protein PHLOEM UNLOADING MODULATOR
Sequence:
MAEELEKSMHKEESLMEKIADKIHDHDSSSSSDSEHEKPESPSALKAKIYRLFGREKPVHKVLGGGLPADVFLWRDKKLSASVLGVATAIWVLFELVEYHFLSLVCHILIFALAALFLLSNAHAFMNKTPPKIPEIHIKEEHFLMIVSALRNELNQAFVILRSIALGRDLKKFLMVVFGLWIISVVGNWFNFLTLVYICFVVLHTVPMLYEKHEDKVDPVAEKTLKELKKHYMVFDEKVLSKLPVASLKAKLG
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (F1NTD3)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MPLLSSSKLSVESRKEDGEGTAPAPPQKKLSCQCHHHCPEDSVNSTCSTDGYCFTIIEEDDSGGHLVTKGCLGLEGSDFQCRDTPIPHQRRSIECCTGQDYCNKHLHPTLPPLKNRDFAEGNIHHKALLISVTVCSILLVLIIIFCYFRYKRQEARPRYSIGLEQDETYIPPGESLKDLIEQSQSSGSGSGLPLLVQRTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDTKGMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEIARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMMECWAHNPASRLTALRVKKTLAKMSESQDIKL
Protein: DNA repair protein rad26 (P36632)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cell cycle arrest when DNA synthesis is inhibited by hydroxyurea, and in mitosis arrest after treatment with DNA-damaging agents. This protein is S phase-specific.
Subcellular location: Nucleus {ECO:0000269|PubMed:12697061}.
Interaction partners:
- Protein kinase rad3
- DNA damage checkpoint control protein rad1
- Checkpoint protein hus1
- DNA repair protein rad9
- S-M checkpoint control protein rad4
- Serine/threonine-protein kinase chk1
- DNA repair protein crb2
- Serine/threonine-protein kinase cds1
- Checkpoint protein rad17
- DNA repair protein rhp26
Sequence:
MMADESFDLESLGSDEIFEGVNLDELEQQAQTQVQAQSSQVVVPSEKQKQNLNLPNSYTNSSQKVRESTVNSQASLSSNDLRTELLIKSGENAILRANLLKQSEANNAALESLNNSIKQKQDEYQRKLEELKKEIEYAKTKSLFHEREAQDAIETMKKMKRDVKNSPIMKKSHEEDGDNKLLSSSDQLAKSTKHAAKNSPSKKKRKTSVATAEDASTDSVSSSIAISDASLSLSLMKDLLSLQKREDLYFSSRTLAYVFGGCMHSLETIEGEEEGECLFNNLKALIYSPDLSMDSSNYVQSVVQTSSSILNYSMKKLLYNASFAITSLFNALLILDPKSSTFIFQENVVSLISGFLLKEYEKSNFLDSKFYVLIDFLYLYLSIARESADDFANITKAVDPSLFESCIRVQNAPSLIKCGVCLIISSTTPSFCASVNLLNADDKSQESLMQLFTTMAHILVVTTRERINFPELNEWITLHRFVISFFTVFIQMSGNIGKEILKVCNPLIVCIGLAITWYHQQLLSSMYPQNECVEILVSLVRLLYILSSEDLSSKFMLAENALQPRFVYAIACCAFGDTEQKAFGNLGEEMYFLTTELLEVCVSPEELEQLYTNF
Protein: Cilium assembly protein DZIP1L (DAZ-interacting zinc finger protein 1-like) (Protein warpy) (Q499E4)
Organism: Mus musculus (Mouse)
Function: Involved in primary cilium formation. Probably acts as a transition zone protein required for localization of PKD1/PC1 and PKD2/PC2 to the ciliary membrane (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8IYY4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IYY4}. Note=Localizes to centrioles and to the distal ends of basal bodies. {ECO:0000250|UniProtKB:Q8IYY4}.
Interaction partners:
Sequence:
MQYPAATAEGLSGPLSGAYTLPAFKFQPRRESIDWRRISAVDVDRVARELDVATLQENIAGVTFCNLDGEVCNHCRQPVDPVLLKVLRLAQLIIEYLLHCQDCLSASVAQLEARLQASLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLLQTSAHSYHTCHLCDKTFMNATFLRGHIQRRHAGMADVGKQKQEQPLGEVLEELRAKLKWTQGELEAQREAERQRQVQELEMARQREMEAKKKFDEWKEKERSKLYGEIDKLKQLFWDEFKTVANQNSTLEEKLKALQSYSMTESHLGSLRDEESEERLKHAQEVQALQEKMEVQKTEWKRKMKALHEERAAERRQLQEENERLHVSLSQDQKKAAAQSQRHINALRAQLQEQARLIESQEETIQTLSLRKVEEVQEMPKAVATEEDSSEEELEASLEERQEQRKVLAALRKNPTWLKQFRPILEDTLEEKLEGLGIKRDTKGISAQTVRRLEPLLRTQREQIARSFREFPSLREKLNKEVSSRVKQRWESTTQPDGQPPVKSQRVTLATREVRPKTRTLTVALPSKPAEPSTPTLQGHSSHGPGLTQVSTPIPRPRVHGPSSTPVSPGSGLSSTPPFSSEEEPEGDVVQRVSLQPPKVLPRSAAKPEDNWGWSDSETSEESAQPPGKGSGGLASSGTLVQSIVKNLEKQLETPAKKPSGGVNMFLRPNAALQRASTPARKSQLSEDESDVEISSLEDLSQDLGQKGKPKPLSHSKLPEKFDVSPWSSGSRPRIPGW
Protein: Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43 (EC 3.6.4.13) (O42945)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 19
- G-patch domain-containing protein C1486.03
- Pre-mRNA-processing factor 17
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-splicing factor cwf3
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor spp42
Sequence:
MEPAQKKLRQESKNPYLAHLNNGDDSEEVVSSKGLTRRATTVAQAAKAEEGPNNFFNDKPFSQNYFKILETRRELPVYQQREEFLKIYHENQIIVFVGETGSGKTTQIPQFVLYDELPHLTNTQIACTQPRRVAAMSVAKRVADEMDVDLGEEVGYNIRFEDCSGPNTLLKYMTDGMLLREAMTDHMLSRYSCIILDEAHERTLATDILMGLMKRLATRRPDLKIIVMSATLDAKKFQKYFFDAPLLAVPGRTYPVEIYYTQEPERDYLEAALRTVLQIHVEEGPGDILVFLTGEEEIEDACRKITLEADDLVREGAAGPLKVYPLYGSLPPNQQQRIFEPTPEDTKSGYGRKVVISTNIAETSLTIDGIVYVVDPGFSKQKIYNPRIRVESLLVSPISKASAQQRAGRAGRTRPGKCFRLYTEEAFRKELIEQTYPEILRSNLSSTVLELKKLGIDDLVHFDYMDPPAPETMMRALEELNYLNCLDDNGDLTPLGRKASEFPLDPNLAVMLIRSPEFYCSNEVLSLTALLSVPNVFVRPNSARKLADEMRQQFTHPDGDHLTLLNVYHAYKSGEGTADWCWNHFLSHRALISADNVRKQLRRTMERQEVELISTPFDDKNYYVNIRRALVSGFFMQVAKKSANGKNYVTMKDNQVVSLHPSCGLSVTPEWVVYNEFVLTTKSFIRNVTAIRPEWLIELAPNYYDLDDFDNNKEVKSALQKVYQMAARSKKNARR
Protein: Alpha-(1,6)-fucosyltransferase (EC 2.4.1.68) (F1QW63)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
- Alpha-mannosidase
- Alpha-mannosidase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1.
- Beta-1,4-galactosyltransferase
- Beta-1,4-galactosyltransferase
- UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 3.
- Beta-1,4-galactosyltransferase
Sequence:
MRPWTGSWRWIMLVLLAWGTLLFYIGGHLVKDSEHPERSSRELSKILAKLERLKQQNEDLRRMAETLRLPDGQADGGPGAVGKLRNLEEQLIRAKEKINSYRSLPADGPGKDHEELRRKVENGVRELWYFVRSEVKKLPLMETGAMHKHVDTLMQDLGHQQRSVMTDLYHLSQADGAGDWREKEANELSDLVQNRIMYLQNPQDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATGGWETVFKPVSDTCTDRTGASTGHWSGEANDRDVQVIELPIVDSLHPRPPYLPLAIPEDLADRLQRLHGDPAVWWVSQFVKYLIRPQAWLMKEMQEVTTKLGFKHPIIGVHVRRTDKVGTEAAFHPIEEYMVHVEDHYQSLAQRMHVDKKRVYLATDDPSLLQEAKTKYPDYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSRTNYLVCTFSSQVCRVAYEIMQTLHPDASSYFYSLDDIYYFGGQNAHNQIAIYPHQPRNSDDIPLEPGDVIGVAGNHWDGYSKGINRKTGRTGLYPSYKVKEKIETVKYPTYPEADKLLKKP
Protein: PDZ domain containing 7 (A0A2R8Y892)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MAQGFAVGFDPLGLGDLSSGSLSSLSSRGHLGSDSGSTATRYLLRKQQRLLNGPPRGIRASSPMGRVILINSPIEANSDESDIIHSVRVEKSPAGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVKVLTSSSRLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCGSTPSDTSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSCASSAPYSSGSLPSDRMDICLGQEEPGSRGPGWGRADTAMQTEPDAGGRVETWCSVRPTVILRDTAIRSDGPHPGRRLDSALSESPKTALLLALSRPRPPITRSQSYLTLWEEKQQRKKEKSGSPGEKGALQRSKTLMNLFFKGGRQGRLARDGRREAWTLDSGSLAKTYPRLDIEKVCARGRHRGPGEAPAGHPRQAGEAATAAGHQECGGPHRPGPLRQHGDACGAGGF
Protein: Probable E3 ubiquitin-protein ligase RHC1A (EC 2.3.2.27) (RING-H2 finger C1a) (RING-H2 zinc finger protein RHC1a) (RING-type E3 ubiquitin transferase RHC1A) (O22197)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Interaction partners:
- At1g47570
- AT-hook motif nuclear-localized protein 1
- FYD
- C2H2-like zinc finger protein
- AT-rich interactive domain-containing protein 5
- RNA-binding
- Serine/threonine-protein kinase AFC2
Sequence:
MSSSRNTHWCHRCQRAVRLHGQEPVCFYCGGGFVEELDMAQASPFDMFRSHRGVVERDQTFDLMDAFSVFMRNRLAERSHDREIRGRTISSGPENFPGLAPLLIFGGQVPYRLTGDNAVEALFNGGSPGIGITRGNTGDYFFGPGLEELFEQLSAGTTRRGPPPAPRSAIDALPTIKIAQRHLRSSDSNCPVCKDEFELGSEAKQMPCNHIYHSDCIVPWLVQHNSCPVCRQELPSASGPSSSQNRTTPTRNYRSSSSSSSSNSRENGNERRNPFSSFWPFRSSGSSSSSTQNRGGTRNSDTSDENHNYHQQQHQQSYMGYSGWPFDY
Protein: Fibroblast growth factor-binding protein 2 (FGF-BP2) (FGF-binding protein 2) (FGFBP-2) (37 kDa killer-specific secretory protein) (Ksp37) (HBp17-related protein) (HBp17-RP) (Q9BYJ0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:11342666}.
Interaction partners:
- Granzyme H
- Granulysin
- Protein NKG7
Sequence:
MKFVPCLLLVTLSCLGTLGQAPRQKQGSTGEEFHFQTGGRDSCTMRPSSLGQGAGEVWLRVDCRNTDQTYWCEYRGQPSMCQAFAADPKPYWNQALQELRRLHHACQGAPVLRPSVCREAGPQAHMQQVTSSLKGSPEPNQQPEAGTPSLRPKATVKLTEATQLGKDSMEELGKAKPTTRPTAKPTQPGPRPGGNEEAKKKAWEHCWKPFQALCAFLISFFRG
Protein: ATP synthase F(0) complex subunit a (F-ATPase protein 6) (Proton-conducting channel, ATP synthase F(0) complex subunit a) (P05504)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- Cytochrome c oxidase subunit 3
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- Uncharacterized protein
- ATP synthase F
Sequence:
MNENLFASFITPTMMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMDISPPTATITFIILLLLTVLEFAVALIQAYVFTLLVSLYLHDNT
Protein: Manganese import ATP-binding protein ScaC (EC 7.2.2.5) (ORF1) (P42360)
Organism: Streptococcus gordonii
Function: Part of the high-affinity ABC transporter complex ScaABC involved in manganese import. Probably responsible for energy coupling to the transport system. Essential for growth under Mn(2+)-limiting conditions.
Subcellular location: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLRYINTVGVIYMIEIQNLSVSYQGQLALDKANVTIKGPTITGIIGPNGAGKSTLIKGLLGIVDHQGQALLDGQPLDKELKRIAYVEQKINIDYNFPIKVKECVSLGLYPKIKLFQRLKTSDWDKVNQALKIVGLEDFAERQISQLSGGQFQRVLIARCLVQEADYIFLDEPFVGIDSVSEEIIMKTLRQLRKDGKTILIVHHDLSKVVAYFDQVLLLNKKVVAFGSTESTFTKENMQQTYGSQLFMNGGA
Protein: Sperm-associated antigen 8 (Sperm membrane protein 1) (SMP-1) (Sperm membrane protein BS-84) (Q3V0Q6)
Organism: Mus musculus (Mouse)
Function: Plays a role in spermatogenesis by enhancing the binding of CREM isoform tau to its coactivator FHL5 and increasing the FHL5-regulated transcriptional activation of CREM isoform tau. Involved in the acrosome reaction and in binding of sperm to the zona pellucida. Plays a role in regulation of the cell cycle by controlling progression through the G2/M phase, possibly by delaying the activation of CDK1 which is required for entry into mitosis (By similarity). May play a role in fertility and microtubule formation through interaction with RANBP9 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20488182}. Nucleus {ECO:0000269|PubMed:20488182}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:17187156, ECO:0000269|PubMed:20488182}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q99932}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:E1BNS6}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}. Note=In mature sperm cells, detected in the acrosomal region of the head and in the middle piece of the tail (PubMed:20488182). Localized to the nucleus and cytoplasm of spermatocytes and round spermatids while, in elongating spermatids, expressed in the cytoplasm but not in the nucleus (PubMed:20488182). During the cell cycle, localized on the microtubule-organizing center (MTOC) during prophase. In metaphase, extends along spindle microtubules. In anaphase, detected on the astral microtubules and mid-zone. In telophase, remains at the mid-zone. After cytokinesis, returns to the MTOC (By similarity). Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme (By similarity). {ECO:0000250|UniProtKB:E1BNS6, ECO:0000250|UniProtKB:Q99932, ECO:0000269|PubMed:20488182}.
Interaction partners:
- Protein Flattop
- Tektin-3
- WD repeat-containing protein 90
- Cilia- and flagella-associated protein 95
- Tektin-4
- Cilia- and flagella-associated protein 52
- Cilia- and flagella-associated protein 276
- RIB43A-like with coiled-coils protein 2
- Tektin-1
- EF-hand domain-containing family member C2
Sequence:
METTESTEGSLSRSCDVQPSSERLDTPSEPVPSSSSSPRSTAPAEAPAQYSVLTEPSSDSLYGAPCPPAHHRGHGFGFQPFYVSCIPQDPCNMADLSSRADPTSSYPCHSSVHGSGSGTCGLGQSSEPSQGSGPTSGPAPASVPSLVSGPDSASGPDSSASGPALASGPGPADPGQGPKFSTCIPQGYRCIPVDLAPDYNAWCQHLHWKPQRSWEPLQVSEPGVRGPYKPPEPGALGPCEPCEPCEPPEAESEETLCKARPRGQCLLYNWEEERATNQLDQIPPLQDGSESYFFRHGHQGLLTTQPQSPMSSSTTQRDSYQLPRHICQPLRGKREAMLEMLLRHQICKEVQAEQEPARKLFETESVTHHDYRVELVRAAPPASTKPHDYRQEQPETFWIQRAARLPGVSDIRTLDTPFRKNCSFSTPVPLSLGQPLPYELESGPHQVGVISSLACQGGGQGCGRTKTTPI
Protein: Conserved hypothetical proline and threonine rich protein (O07239)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Chaperone protein HtpG
- Protein GrpE
- Chaperone protein DnaJ 2
- Chaperone protein DnaJ 1
- Exported repetitive protein
- Chaperonin GroEL 2
- Chaperonin GroEL 1
- Possible conserved transmembrane alanine and glycine rich protein
- ATP-dependent Clp protease ATP-binding subunit ClpC1
- Chaperone protein ClpB
Sequence:
MYDPLGLSIGTTNLVAAGNGGPPVTRRAVLTLYPHCAPKIGVPSQNPNLIEPGALMSGFVERIGDAVALVSPDGSVHDPDLLLVEALDAMVLTAGADASSSEIAIAVPAHWKPGAVHALRNGLRTHVGFVRSGMAPRLVSDAIAALTAVNSELGLPHGSVVGLLDFGGSATYVTLVETKSDSRTSDFQPVSATARYQDFSGSQIDQALLLRVIDQFGYGDDVDPASTAAVGQLGQLREQCRAAKERLSTDVATELFAELAGCSSSIEMTREQLEDLIQDPLTGFIYAFDDMLARHNASWADLAAVVTVGGGANIPLVTQRLSFHTRRPVLTASQPGCAAAMGALLLANRGGERDSRTRTSIGLATAAAAGTSVIELPAGDVMVIDHEALTDRELAWSQTDFPSEAPARFEGDSYNEGGPCWSMRLNAVEPPKGPAWRRIRVSQLLIGVSAVVAMTAIGGVALTLTAIERRPSPLPTPIVPGLAPMPPGSVVPSSRAPTPPPPPSTVAPLPSAAPAPTTVAPAPPPPTQVVTTTTAPPVTTTPRPSPTTTTTTAPPSTTTTTEPPVTTTSTIPTIPTTTTTVKMTTEWLHVPFLPVPIPVPIPQNPGAGEPQNPFGSLGSG