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Description:
Structural maintenance of chromosome 3 (Chondroitin sulfateproteoglycan 6) (Chromosome-associated polypeptide) (hCAP) (Bamacan)(Basement membrane-associated chondroitin proteoglycan).
Molecular weight: 1415
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
07-MAR-2006, entry version 41.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein SMC3_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AF020043 | AAC14893.1 | - |
| EMBL | AF067163 | AAD32447.1 | ALT_FRAME |
| EMBL | AJ005015 | CAA06289.1 | - |
| IntAct | Q9UQE7 | -.1 | |
| Ensembl | ENSG00000108055 | Homo sapiens.1 | |
| HGNC | HGNC:2468 | CSPG6.1 | |
| MIM | 606062 | gene. | |
| Reactome | Q9UQE7 | -.1 | |
| GO | GO:0005604 | C:basement membrane | TAS. |
| GO | GO:0008278 | C:cohesin complex | NAS. |
| GO | GO:0005737 | C:cytoplasm | IDA. |
| GO | GO:0016363 | C:nuclear matrix | IDA. |
| GO | GO:0000922 | C:spindle pole | IDA. |
| GO | GO:0045502 | F:dynein binding | IDA. |
| GO | GO:0003777 | F:microtubule motor activity | NAS. |
| GO | GO:0046982 | F:protein heterodimerization activity | IPI. |
| GO | GO:0007001 | P:chromosome organization and biogenesis (sen... | TAS. |
| GO | GO:0009294 | P:DNA mediated transformation | TAS. |
| GO | GO:0007126 | P:meiosis | IDA. |
| GO | GO:0007052 | P:mitotic spindle organization and biogenesis | IEP. |
| GO | GO:0007165 | P:signal transduction | IDA. |
| GO | GO:0007062 | P:sister chromatid cohesion | NAS. |
| InterPro | IPR010935 | SMC_hinge. | |
| InterPro | IPR003395 | SMC_N. | |
| Pfam | PF06470 | SMC_hinge | 1. |
| Pfam | PF02463 | SMC_N | 1. |
| ProDom | PD000006 | ABC_transporter | 1. |
Keywords:
ATP-binding; Cell cycle; Cell division; Chromosome partition; Coiled coil; DNA damage; DNA repair; Meiosis; Mitosis; Nuclear protein; Nucleotide-binding; Phosphorylation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH KIFAP3, AND
RP IDENTIFICATION IN A COMPLEX WITH KIFAP3 AND KIF3B.
RC TISSUE=B-cell;
RX MEDLINE=98175913; PubMed=9506951; DOI=10.1074/jbc.273.12.6591;
RA Shimizu K., Shirataki H., Honda T., Minami S., Takai Y.;
RT "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated
RT protein, with a human chromosome-associated polypeptide.";
RL J. Biol. Chem. 273:6591-6594(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1217.
RC TISSUE=Umbilical cord blood;
RX MEDLINE=20499367; PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 827-1217.
RC TISSUE=Neuron;
RA Stanchi F., Bertocco E., Simionati B., Zimbello R., Lanfranchi G.,
RA Valle G.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION, FUNCTION, AND IDENTIFICATION IN A COHESIN COMPLEX
RP WITH SMC1L1, STAG1 OR STAG2.
RX MEDLINE=20530656; PubMed=11076961; DOI=10.1083/jcb.151.4.749;
RA Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.;
RT "Characterization of vertebrate cohesin complexes and their regulation
RT in prophase.";
RL J. Cell Biol. 151:749-762(2000).
RN [5]
RP INTERACTION WITH NUMA1.
RX MEDLINE=21601651; PubMed=11590136; DOI=10.1074/jbc.M103364200;
RA Gregson H.C., Schmiesing J.A., Kim J.-S., Kobayashi T., Zhou S.,
RA Yokomori K.;
RT "A potential role for human cohesin in mitotic spindle aster
RT assembly.";
RL J. Biol. Chem. 276:47575-47582(2001).
RN [6]
RP PHOSPHORYLATION SITES SER-1065; SER-1067; SER-1074 AND SER-1083.
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH CDCA5; SMC3L1; RAD21; PDS5A AND
RP PDS5B.
RX PubMed=15837422; DOI=10.1016/j.molcel.2005.03.017;
RA Rankin S., Ayad N.G., Kirschner M.W.;
RT "Sororin, a substrate of the anaphase-promoting complex, is required
RT for sister chromatid cohesion in vertebrates.";
RL Mol. Cell 18:185-200(2005).
RN [8]
RP ERRATUM.
RA Rankin S., Ayad N.G., Kirschner M.W.;
RT "Sororin, a substrate of the anaphase- promoting complex, is required
RT for sister chromatid cohesion in vertebrates.";
RL Mol. Cell 18:609-609(2005).
Feature:
CHAIN 1 1217 Structural maintenance of chromosome 3.
/FTId=PRO_0000119001.
NP_BIND 32 39 ATP (Potential).
REGION 505 667 Flexible hinge.
COILED 179 350 Potential.
COILED 393 503 Potential.
COILED 669 916 Potential.
COILED 958 989 Potential.
COMPBIAS 1115 1150 Ala/Asp-rich (DA-box).
MOD_RES 1013 1013 Phosphoserine (By similarity).
MOD_RES 1065 1065 Phosphoserine.
MOD_RES 1067 1067 Phosphoserine.
MOD_RES 1074 1074 Phosphoserine.
MOD_RES 1083 1083 Phosphoserine.
CONFLICT 462 462 K -> T (in Ref. 2).
CONFLICT 509 509 I -> V (in Ref. 2).
CONFLICT 526 526 Q -> P (in Ref. 2).
Comments:
-!- FUNCTION: Involved in chromosome cohesion during cell cycle and in
DNA repair. Central component of cohesin complex. The cohesin
complex is required for the cohesion of sister chromatids after
DNA replication. The cohesin complex apparently forms a large
proteinaceous ring within which sister chromatids can be trapped.
At anaphase, the complex is cleaved and dissociates from
chromatin, allowing sister chromatids to segregate. The cohesin
complex may also play a role in spindle pole assembly during
mitosis and in chromosome movement.
-!- SUBUNIT: Interacts with MXI1, MXD3 and MXD4. Interacts with SYCP2.
Found in a complex with SMC1L1, CDCA5 and RAD21, PDS5A/APRIN and
PDS5B/SCC-112 (By similarity). Forms a heterodimer with SMC1L1 or
SMC1L2 in cohesin complexes. Cohesin complexes are composed of the
SMC1 (SMC1L1 or SMC1L2) and SMC3 heterodimer attached via their
hinge domain, RAD21 which link them, and one STAG protein (STAG1,
STAG2 or STAG3), which interacts with RAD21. Also found in
meiosis-specific cohesin complexes. Interacts with NUMA1, and
forms a ternary complex with KIF3B and KIFAP3, suggesting a
function in tethering the chromosomes to the spindle pole and in
chromosome movement.
-!- SUBCELLULAR LOCATION: Nuclear protein. Associates with chromatin.
Before prophase it is scattered along chromosome arms. During
prophase, most of cohesin complexes dissociate from chromatin
probably because of phosphorylation by PLK, except at centromeres,
where cohesin complexes remain. At anaphase, the RAD21 subunit of
the cohesin complex is cleaved, leading to the dissociation of the
complex from chromosomes, allowing chromosome separation.
-!- DOMAIN: The flexible hinge domain, which separates the large
intramolecular coiled coil regions, allows the heterotypic
interaction with the corresponding domain of SMC1L1 or SMC1L2,
forming a V-shaped heterodimer. The two heads of the heterodimer
are then connected by different ends of the cleavable RAD21
protein, forming a ring structure (By similarity).
-!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
-!- CAUTION: Was originally isolated as a proteoglycan protein
(explaining its name). Although not excluded, such secreted
function is not clear.
-!- CAUTION: Ref.2 sequence differs from that shown due to frameshifts
in positions 457, 488 and 523.
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Sequence length: 1217
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV
ITAEMAKDFV EDDTTHG