HECA2_HUMAN
ID HECA2_HUMAN Reviewed; 462 AA.
AC A8MVW5; B3KTT4; B4DPJ1; B9EG93; E9PDV5; Q6UXI0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=HEPACAM family member 2;
DE AltName: Full=Mitotic kinetics regulator;
DE Flags: Precursor;
GN Name=HEPACAM2; Synonyms=MIKI; ORFNames=UNQ305/PRO346;
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).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP TISSUE SPECIFICITY, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=19358830; DOI=10.1016/j.bbrc.2009.04.004;
RA Asou H., Matsui H., Ozaki Y., Nagamachi A., Nakamura M., Aki D., Inaba T.;
RT "Identification of a common microdeletion cluster in 7q21.3 subband among
RT patients with myeloid leukemia and myelodysplastic syndrome.";
RL Biochem. Biophys. Res. Commun. 383:245-251(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND ADP-RIBOSYLATION.
RX PubMed=22864114; DOI=10.1016/j.molcel.2012.06.033;
RA Ozaki Y., Matsui H., Asou H., Nagamachi A., Aki D., Honda H., Yasunaga S.,
RA Takihara Y., Yamamoto T., Izumi S., Ohsugi M., Inaba T.;
RT "Poly-ADP ribosylation of Miki by tankyrase-1 promotes centrosome
RT maturation.";
RL Mol. Cell 47:694-706(2012).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-31.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [8]
RP VARIANT LEU-114.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Required during prometaphase for centrosome maturation.
CC Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates
CC from the Golgi apparatus to mitotic centrosomes and plays a key role in
CC the formation of robust microtubules for prompt movement of
CC chromosomes: anchors AKAP9/CG-NAP, a scaffold protein of the gamma-
CC tubulin ring complex and promotes centrosome maturation.
CC {ECO:0000269|PubMed:22864114}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}; Single-pass
CC type I membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. Midbody
CC {ECO:0000269|PubMed:22864114}. Note=In interphase, localizes to the
CC Golgi apparatus. Localizes to centrosomes and spindles during prophase,
CC prometaphase, and metaphase of mitosis, and to midbodies at telophase.
CC Translocation to mitotic centrosomes is the result of poly-ADP-
CC ribosylation (PARsylation). {ECO:0000269|PubMed:19358830,
CC ECO:0000269|PubMed:22864114}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A8MVW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MVW5-2; Sequence=VSP_033355;
CC Name=3;
CC IsoId=A8MVW5-3; Sequence=VSP_044322;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19358830}.
CC -!- PTM: Poly-ADP-ribosylated (PARsylated) by tankyrase TNKS during late G2
CC and prophase, leading to translocation to mitotic centrosomes.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19358830,
CC ECO:0000269|PubMed:22864114}.
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DR EMBL; AY358345; AAQ88711.1; -; mRNA.
DR EMBL; AK096002; BAG53196.1; -; mRNA.
DR EMBL; AK298361; BAG60603.1; -; mRNA.
DR EMBL; AC000119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136300; AAI36301.1; -; mRNA.
DR EMBL; BC136301; AAI36302.1; -; mRNA.
DR EMBL; BC139906; AAI39907.1; -; mRNA.
DR CCDS; CCDS43616.1; -. [A8MVW5-1]
DR CCDS; CCDS5629.1; -. [A8MVW5-2]
DR CCDS; CCDS75632.1; -. [A8MVW5-3]
DR RefSeq; NP_001034461.1; NM_001039372.3. [A8MVW5-1]
DR RefSeq; NP_001275733.1; NM_001288804.2. [A8MVW5-3]
DR RefSeq; NP_001275739.1; NM_001288810.2.
DR RefSeq; NP_937794.1; NM_198151.3. [A8MVW5-2]
DR AlphaFoldDB; A8MVW5; -.
DR BioGRID; 128949; 52.
DR IntAct; A8MVW5; 24.
DR STRING; 9606.ENSP00000390204; -.
DR GlyGen; A8MVW5; 4 sites.
DR iPTMnet; A8MVW5; -.
DR PhosphoSitePlus; A8MVW5; -.
DR BioMuta; HEPACAM2; -.
DR jPOST; A8MVW5; -.
DR MassIVE; A8MVW5; -.
DR PaxDb; A8MVW5; -.
DR PeptideAtlas; A8MVW5; -.
DR PRIDE; A8MVW5; -.
DR ProteomicsDB; 19755; -.
DR ProteomicsDB; 2210; -. [A8MVW5-1]
DR ProteomicsDB; 2211; -. [A8MVW5-2]
DR Antibodypedia; 2717; 146 antibodies from 22 providers.
DR DNASU; 253012; -.
DR Ensembl; ENST00000341723.8; ENSP00000340532.4; ENSG00000188175.10. [A8MVW5-2]
DR Ensembl; ENST00000394468.7; ENSP00000377980.2; ENSG00000188175.10. [A8MVW5-1]
DR Ensembl; ENST00000453812.2; ENSP00000390204.2; ENSG00000188175.10. [A8MVW5-3]
DR GeneID; 253012; -.
DR KEGG; hsa:253012; -.
DR MANE-Select; ENST00000394468.7; ENSP00000377980.2; NM_001039372.4; NP_001034461.1.
DR UCSC; uc003uml.5; human. [A8MVW5-1]
DR CTD; 253012; -.
DR DisGeNET; 253012; -.
DR GeneCards; HEPACAM2; -.
DR HGNC; HGNC:27364; HEPACAM2.
DR HPA; ENSG00000188175; Tissue enriched (intestine).
DR MIM; 614133; gene.
DR neXtProt; NX_A8MVW5; -.
DR OpenTargets; ENSG00000188175; -.
DR PharmGKB; PA162390849; -.
DR VEuPathDB; HostDB:ENSG00000188175; -.
DR eggNOG; ENOG502QRJQ; Eukaryota.
DR GeneTree; ENSGT01010000222242; -.
DR HOGENOM; CLU_049122_0_0_1; -.
DR InParanoid; A8MVW5; -.
DR OMA; ITPTIYY; -.
DR OrthoDB; 964418at2759; -.
DR PhylomeDB; A8MVW5; -.
DR TreeFam; TF331199; -.
DR PathwayCommons; A8MVW5; -.
DR SignaLink; A8MVW5; -.
DR BioGRID-ORCS; 253012; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; HEPACAM2; human.
DR GenomeRNAi; 253012; -.
DR Pharos; A8MVW5; Tbio.
DR PRO; PR:A8MVW5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A8MVW5; protein.
DR Bgee; ENSG00000188175; Expressed in ileal mucosa and 89 other tissues.
DR ExpressionAtlas; A8MVW5; baseline and differential.
DR Genevisible; A8MVW5; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Cell cycle; Cell division;
KW Cytoplasm; Cytoskeleton; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Immunoglobulin domain; Membrane; Mitosis; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..462
FT /note="HEPACAM family member 2"
FT /id="PRO_0000332220"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 149..233
FT /note="Ig-like C2-type 1"
FT DOMAIN 235..331
FT /note="Ig-like C2-type 2"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 170..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..26
FT /note="MGQDAFMEPFGDTLGVFQCKIYLLLF -> MWLKVFTTFLSFAT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033355"
FT VAR_SEQ 26
FT /note="F -> FDIVANCLLLRFKLSVSSYEIWKK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044322"
FT VARIANT 31
FT /note="G -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_042976"
FT VARIANT 86
FT /note="K -> T (in dbSNP:rs10281525)"
FT /id="VAR_042977"
FT VARIANT 114
FT /note="F -> L (found in a renal cell carcinoma sample;
FT somatic mutation; dbSNP:rs555587403)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064721"
FT CONFLICT 277
FT /note="P -> S (in Ref. 2; BAG60603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51407 MW; E38DE6E4CCAA6BC2 CRC64;
MGQDAFMEPF GDTLGVFQCK IYLLLFGACS GLKVTVPSHT VHGVRGQALY LPVHYGFHTP
ASDIQIIWLF ERPHTMPKYL LGSVNKSVVP DLEYQHKFTM MPPNASLLIN PLQFPDEGNY
IVKVNIQGNG TLSASQKIQV TVDDPVTKPV VQIHPPSGAV EYVGNMTLTC HVEGGTRLAY
QWLKNGRPVH TSSTYSFSPQ NNTLHIAPVT KEDIGNYSCL VRNPVSEMES DIIMPIIYYG
PYGLQVNSDK GLKVGEVFTV DLGEAILFDC SADSHPPNTY SWIRRTDNTT YIIKHGPRLE
VASEKVAQKT MDYVCCAYNN ITGRQDETHF TVIITSVGLE KLAQKGKSLS PLASITGISL
FLIISMCLLF LWKKYQPYKV IKQKLEGRPE TEYRKAQTFS GHEDALDDFG IYEFVAFPDV
SGVSRIPSRS VPASDCVSGQ DLHSTVYEVI QHIPAQQQDH PE
