P32908

PR
Gene name
SMC1 (CHL10, YFL008W)
Protein name
Structural maintenance of chromosomes protein 1
Names
DA-box protein SMC1
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YFL008W
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

230-543 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

4 structures for P32908

Entry ID Method Resolution Chain Position Source
1W1W X-ray 290 A PDB
6ZZ6 EM 340 A A 1003-1224 PDB
7OGT EM 550 A A 1-1225 PDB
AF-P32908-F1 Predicted AlphaFoldDB

18 variants for P32908

Variant ID(s) Position Change Description Diseaes Association Provenance
s06-119676 85 A>T No SGRP
s06-120010 196 A>V No SGRP
s06-120124 234 Q>R No SGRP
s06-120199 259 L>S No SGRP
s06-120236 271 N>K No SGRP
s06-120258 279 R>C No SGRP
s06-120361 313 R>L No SGRP
s06-120376 318 P>L No SGRP
s06-120511 363 A>V No SGRP
s06-120606 395 Y>N No SGRP
s06-121224 601 D>N No SGRP
s06-121388 655 E>D No SGRP
s06-121756 778 V>E No SGRP
s06-121804 794 S>N No SGRP
s06-122100 893 K>E No SGRP
s06-122192 923 R>S No SGRP
s06-122221 933 F>C No SGRP
s06-122266 948 N>S No SGRP

No associated diseases with P32908

4 regional properties for P32908

Type Name Position InterPro Accession
domain RecF/RecN/SMC, N-terminal 5 - 1211 IPR003395
domain SMCs flexible hinge 527 - 642 IPR010935
domain Smc1, ATP-binding cassette domain 4 - 162 IPR028468-1
domain Smc1, ATP-binding cassette domain 1117 - 1220 IPR028468-2

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Chromosome
  • Associates with chromatin
  • Before prophase it is scattered along chromosome arms
  • At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cohesin complex A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
mitotic cohesin complex A cohesin complex that mediates sister chromatid cohesion during mitosis; has a subunit composition distinct from that of the meiotic cohesin complex.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA secondary structure binding Binding to a DNA secondary structure element such as a four-way junction, a bubble, a loop, Y-form DNA, or a double-strand/single-strand junction.
double-stranded DNA binding Binding to double-stranded DNA.
identical protein binding Binding to an identical protein or proteins.
minor groove of adenine-thymine-rich DNA binding Binding to a DNA structure formed by the minor groove of adenine-thymine-rich DNA regions. Examples of proteins having this function are AT-rich interaction domain (ARID)-containing proteins.

7 GO annotations of biological process

Name Definition
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
double-strand break repair The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
establishment of meiotic sister chromatid cohesion The process in which the sister chromatids of a replicated chromosome become joined along the entire length of the chromosome during S phase during a meiotic cell cycle.
establishment of mitotic sister chromatid cohesion The process in which the sister chromatids of a replicated chromosome become joined along the entire length of the chromosome during S phase during a mitotic cell cycle.
mitotic sister chromatid cohesion The cell cycle process in which the sister chromatids of a replicated chromosome are joined along the entire length of the chromosome, from their formation in S phase through metaphase during a mitotic cell cycle. This cohesion cycle is critical for high fidelity chromosome transmission.
mitotic sister chromatid segregation The cell cycle process in which replicated homologous chromosomes are organized and then physically separated and apportioned to two sets during the mitotic cell cycle. Each replicated chromosome, composed of two sister chromatids, aligns at the cell equator, paired with its homologous partner. One homolog of each morphologic type goes into each of the resulting chromosome sets.
sister chromatid cohesion The cell cycle process in which the sister chromatids of a replicated chromosome become tethered to each other.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8NDV3 SMC1B Structural maintenance of chromosomes protein 1B Homo sapiens (Human) PR
Q14683 SMC1A Structural maintenance of chromosomes protein 1A Homo sapiens (Human) PR
Q9CU62 Smc1a Structural maintenance of chromosomes protein 1A Mus musculus (Mouse) PR
Q9Z1M9 Smc1a Structural maintenance of chromosomes protein 1A Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL GVRSNHLRSN
70 80 90 100 110 120
ILKDLIYRGV LNDENSDDYD NEGAASSNPQ SAYVKAFYQK GNKLVELMRI ISRNGDTSYK
130 140 150 160 170 180
IDGKTVSYKD YSIFLENENI LIKAKNFLVF QGDVEQIAAQ SPVELSRMFE EVSGSIQYKK
190 200 210 220 230 240
EYEELKEKIE KLSKSATESI KNRRRIHGEL KTYKEGINKN EEYRKQLDKK NELQKFQALW
250 260 270 280 290 300
QLYHLEQQKE ELTDKLSALN SEISSLKGKI NNEMKSLQRS KSSFVKESAV ISKQKSKLDY
310 320 330 340 350 360
IFKDKEKLVS DLRLIKVPQQ AAGKRISHIE KRIESLQKDL QRQKTYVERF ETQLKVVTRS
370 380 390 400 410 420
KEAFEEEIKQ SARNYDKFKL NENDLKTYNC LHEKYLTEGG SILEEKIAVL NNDKREIQEE
430 440 450 460 470 480
LERFNKRADI SKRRITEELS ITGEKLDTQL NDLRVSLNEK NALHTERLHE LKKLQSDIES
490 500 510 520 530 540
ANNQEYDLNF KLRETLVKID DLSANQRETM KERKLRENIA MLKRFFPGVK GLVHDLCHPK
550 560 570 580 590 600
KEKYGLAVST ILGKNFDSVI VENLTVAQEC IAFLKKQRAG TASFIPLDTI ETELPTLSLP
610 620 630 640 650 660
DSQDYILSIN AIDYEPEYEK AMQYVCGDSI ICNTLNIAKD LKWKKGIRGK LVTIEGALIH
670 680 690 700 710 720
KAGLMTGGIS GDANNRWDKE EYQSLMSLKD KLLIQIDELS NGQRSNSIRA REVENSVSLL
730 740 750 760 770 780
NSDIANLRTQ VTQQKRSLDE NRLEIKYHND LIEKEIQPKI TELKKKLDDL ENTKDNLVKE
790 800 810 820 830 840
KEALQNNIFK EFTSKIGFTI KEYENHSGEL MRQQSKELQQ LQKQILTVEN KLQFETDRLS
850 860 870 880 890 900
TTQRRYEKAQ KDLENAQVEM KSLEEQEYAI EMKIGSIESK LEEHKNHLDE LQKKFVTKQS
910 920 930 940 950 960
ELNSSEDILE DMNSNLQVLK RERDGIKEDI EKFDLERVTA LKNCKISNIN IPISSETTID
970 980 990 1000 1010 1020
DLPISSTDNE AITISNSIDI NYKGLPKKYK ENNTDSARKE LEQKIHEVEE ILNELQPNAR
1030 1040 1050 1060 1070 1080
ALERYDEAEG RFEVINNETE QLKAEEKKIL NQFLKIKKKR KELFEKTFDY VSDHLDAIYR
1090 1100 1110 1120 1130 1140
ELTKNPNSNV ELAGGNASLT IEDEDEPFNA GIKYHATPPL KRFKDMEYLS GGEKTVAALA
1150 1160 1170 1180 1190 1200
LLFAINSYQP SPFFVLDEVD AALDITNVQR IAAYIRRHRN PDLQFIVISL KNTMFEKSDA
1210 1220
LVGVYRQQQE NSSKIITLDL SNYAE