K1328_HUMAN
ID K1328_HUMAN Reviewed; 577 AA.
AC Q86T90; Q05DL0; Q49AG6; Q9P2L8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein hinderin {ECO:0000303|PubMed:15656913};
GN Name=KIAA1328;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH SMC3, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=15656913; DOI=10.1186/1471-2121-6-3;
RA Patel C.A., Ghiselli G.;
RT "Hinderin, a five-domains protein including coiled-coil motifs that binds
RT to SMC3.";
RL BMC Cell Biol. 6:3-3(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-490, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Competes with SMC1 for binding to SMC3. May affect the
CC availability of SMC3 to engage in the formation of multimeric protein
CC complexes. {ECO:0000269|PubMed:15656913}.
CC -!- SUBUNIT: Interacts (via N- and C-terminal domains) with SMC3 (via
CC central hinge region). {ECO:0000269|PubMed:15656913}.
CC -!- INTERACTION:
CC Q86T90; A2BDD9: AMOT; NbExp=3; IntAct=EBI-3437878, EBI-17286414;
CC Q86T90; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-3437878, EBI-11954519;
CC Q86T90; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-3437878, EBI-1047414;
CC Q86T90; Q13895: BYSL; NbExp=3; IntAct=EBI-3437878, EBI-358049;
CC Q86T90; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-3437878, EBI-11530605;
CC Q86T90; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-3437878, EBI-10961312;
CC Q86T90; Q96LX7-5: CCDC17; NbExp=3; IntAct=EBI-3437878, EBI-12165781;
CC Q86T90; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-3437878, EBI-10175300;
CC Q86T90; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-3437878, EBI-10250303;
CC Q86T90; O15078: CEP290; NbExp=3; IntAct=EBI-3437878, EBI-1811944;
CC Q86T90; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-3437878, EBI-749051;
CC Q86T90; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-3437878, EBI-11980535;
CC Q86T90; P53618: COPB1; NbExp=3; IntAct=EBI-3437878, EBI-359063;
CC Q86T90; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-3437878, EBI-11521003;
CC Q86T90; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-3437878, EBI-745369;
CC Q86T90; Q96JC9: EAF1; NbExp=3; IntAct=EBI-3437878, EBI-769261;
CC Q86T90; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-3437878, EBI-747840;
CC Q86T90; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-3437878, EBI-744099;
CC Q86T90; Q3B820: FAM161A; NbExp=3; IntAct=EBI-3437878, EBI-719941;
CC Q86T90; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-3437878, EBI-7225287;
CC Q86T90; Q92805: GOLGA1; NbExp=3; IntAct=EBI-3437878, EBI-6164177;
CC Q86T90; Q96LB3-2: IFT74; NbExp=3; IntAct=EBI-3437878, EBI-12066130;
CC Q86T90; P25800: LMO1; NbExp=3; IntAct=EBI-3437878, EBI-8639312;
CC Q86T90; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-3437878, EBI-739832;
CC Q86T90; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-3437878, EBI-2548751;
CC Q86T90; Q96QG7: MTMR9; NbExp=3; IntAct=EBI-3437878, EBI-744593;
CC Q86T90; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-3437878, EBI-11750983;
CC Q86T90; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3437878, EBI-79165;
CC Q86T90; Q16512: PKN1; NbExp=3; IntAct=EBI-3437878, EBI-602382;
CC Q86T90; P54646: PRKAA2; NbExp=3; IntAct=EBI-3437878, EBI-1383852;
CC Q86T90; Q99816: TSG101; NbExp=3; IntAct=EBI-3437878, EBI-346882;
CC Q86T90; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-3437878, EBI-744794;
CC Q86T90; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-3437878, EBI-8994397;
CC Q86T90; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-3437878, EBI-9090990;
CC Q86T90; P40222: TXLNA; NbExp=3; IntAct=EBI-3437878, EBI-359793;
CC Q86T90; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-3437878, EBI-6116822;
CC Q86T90; Q8N5A5-2: ZGPAT; NbExp=5; IntAct=EBI-3437878, EBI-10183064;
CC Q86T90; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-3437878, EBI-740727;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86T90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86T90-2; Sequence=VSP_029810;
CC Name=3;
CC IsoId=Q86T90-3; Sequence=VSP_029809, VSP_029811, VSP_029814,
CC VSP_029815;
CC Name=4;
CC IsoId=Q86T90-4; Sequence=VSP_029809, VSP_029812, VSP_029813;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15656913}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92566.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037749; BAA92566.2; ALT_INIT; mRNA.
DR EMBL; AL832625; CAD89947.1; -; mRNA.
DR EMBL; AC009854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008670; AAH08670.1; -; mRNA.
DR EMBL; BC037903; AAH37903.1; -; mRNA.
DR CCDS; CCDS45855.1; -. [Q86T90-1]
DR RefSeq; NP_065827.1; NM_020776.1. [Q86T90-1]
DR RefSeq; XP_005258374.1; XM_005258317.3. [Q86T90-2]
DR AlphaFoldDB; Q86T90; -.
DR SMR; Q86T90; -.
DR BioGRID; 121595; 47.
DR IntAct; Q86T90; 51.
DR MINT; Q86T90; -.
DR STRING; 9606.ENSP00000280020; -.
DR iPTMnet; Q86T90; -.
DR PhosphoSitePlus; Q86T90; -.
DR BioMuta; KIAA1328; -.
DR DMDM; 296434548; -.
DR EPD; Q86T90; -.
DR jPOST; Q86T90; -.
DR MassIVE; Q86T90; -.
DR MaxQB; Q86T90; -.
DR PaxDb; Q86T90; -.
DR PeptideAtlas; Q86T90; -.
DR PRIDE; Q86T90; -.
DR ProteomicsDB; 69669; -. [Q86T90-1]
DR ProteomicsDB; 69670; -. [Q86T90-2]
DR ProteomicsDB; 69671; -. [Q86T90-3]
DR ProteomicsDB; 69672; -. [Q86T90-4]
DR Antibodypedia; 49207; 20 antibodies from 10 providers.
DR DNASU; 57536; -.
DR Ensembl; ENST00000280020.10; ENSP00000280020.5; ENSG00000150477.15. [Q86T90-1]
DR Ensembl; ENST00000586135.1; ENSP00000467507.1; ENSG00000150477.15. [Q86T90-3]
DR Ensembl; ENST00000586501.1; ENSP00000470371.1; ENSG00000150477.15. [Q86T90-4]
DR Ensembl; ENST00000591619.5; ENSP00000465550.1; ENSG00000150477.15. [Q86T90-2]
DR GeneID; 57536; -.
DR KEGG; hsa:57536; -.
DR MANE-Select; ENST00000280020.10; ENSP00000280020.5; NM_020776.3; NP_065827.1.
DR UCSC; uc002kzz.4; human. [Q86T90-1]
DR CTD; 57536; -.
DR DisGeNET; 57536; -.
DR GeneCards; KIAA1328; -.
DR HGNC; HGNC:29248; KIAA1328.
DR HPA; ENSG00000150477; Tissue enhanced (brain).
DR MIM; 616480; gene.
DR neXtProt; NX_Q86T90; -.
DR OpenTargets; ENSG00000150477; -.
DR PharmGKB; PA134875219; -.
DR VEuPathDB; HostDB:ENSG00000150477; -.
DR eggNOG; ENOG502QTY3; Eukaryota.
DR GeneTree; ENSGT00390000011152; -.
DR HOGENOM; CLU_033814_1_0_1; -.
DR InParanoid; Q86T90; -.
DR OMA; AKPQTYY; -.
DR OrthoDB; 626494at2759; -.
DR PhylomeDB; Q86T90; -.
DR TreeFam; TF332088; -.
DR PathwayCommons; Q86T90; -.
DR SignaLink; Q86T90; -.
DR BioGRID-ORCS; 57536; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; KIAA1328; human.
DR GenomeRNAi; 57536; -.
DR Pharos; Q86T90; Tdark.
DR PRO; PR:Q86T90; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q86T90; protein.
DR Bgee; ENSG00000150477; Expressed in calcaneal tendon and 113 other tissues.
DR ExpressionAtlas; Q86T90; baseline and differential.
DR Genevisible; Q86T90; HS.
DR InterPro; IPR032736; Hinderin.
DR PANTHER; PTHR28375; PTHR28375; 1.
DR Pfam; PF15369; KIAA1328; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..577
FT /note="Protein hinderin"
FT /id="PRO_0000312298"
FT REGION 251..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..167
FT /evidence="ECO:0000255"
FT COILED 358..402
FT /evidence="ECO:0000255"
FT COMPBIAS 476..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZK5"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZK5"
FT VAR_SEQ 1..284
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029809"
FT VAR_SEQ 1..20
FT /note="MADVAGPSRPSAAAFWSRDF -> MPDNIIVFSFMFSCVV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_029810"
FT VAR_SEQ 411
FT /note="C -> WLKAQALFKSRELVAEKQLTKPQELKLDMNGSDSGPS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029811"
FT VAR_SEQ 412..413
FT /note="LL -> SE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029812"
FT VAR_SEQ 414..577
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029813"
FT VAR_SEQ 509..527
FT /note="YETSLLDLVQSLSPNSAPK -> PGISTKICFLSNHFFILFS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029814"
FT VAR_SEQ 528..577
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029815"
FT VARIANT 383
FT /note="R -> C (in dbSNP:rs12326301)"
FT /id="VAR_037483"
FT CONFLICT 62
FT /note="A -> V (in Ref. 3; CAD89947)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="V -> A (in Ref. 3; CAD89947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 65373 MW; 0B977577ECDD5FF4 CRC64;
MADVAGPSRP SAAAFWSRDF SDEEQSVVYV PGISAEGNVR SRHKLMSPKA DVKLKTSRVT
DASISMESLK GTGDSVDEQN SCRGEIKSAS LKDLCLEDKR RIANLIKELA RVSEEKEVTE
ERLKAEQESF EKKIRQLEEQ NELIIKEREA LQLQYRECQE LLSLYQKYLS EQQEKLTMSL
SELGAARMQE QQVSSRKSTL QCSSVELDGS YLSIARPQTY YQTKQRPKSA VQDSASESLI
AFRNNSLKPV TLHHPKDDLD KIPSETTTCN CESPGRKPAV PTEKMPQEEL HMKECPHLKP
TPSQCCGHRL AADRVHDSHP TNMTPQHPKT HPESCSYCRL SWASLVHGGG ALQPIETLKK
QISEDRKQQL MLQKMELEIE KERLQHLLAQ QETKLLLKQQ QLHQSRLDYN CLLKSNCDGW
LLGTSSSIKK HQDPPNSGEN RKERKTVGFH SHMKDDAQWS CQKKDTCRPQ RGTVTGVRKD
ASTSPMPTGS LKDFVTTASP SLQHTTSRYE TSLLDLVQSL SPNSAPKPQR YPSREAGAWN
HGTFRLSPLK STRKKMGMHR TPEELEENQI LEDIFFI
