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Protein

PWWP domain-containing protein MUM1

Gene

Mum1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. Recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. Required for efficient DNA repair and cell survival following DNA damage (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
PWWP domain-containing protein MUM1
Alternative name(s):
Mutated melanoma-associated antigen 1
Short name:
MUM-1
Gene namesi
Name:Mum1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1915364. Mum1.

Subcellular locationi

  • Nucleus By similarity

  • Note: Recuited to DNA damage sites via its interaction with the BRCT domain of TP53BP1.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 682682PWWP domain-containing protein MUM1PRO_0000295047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei168 – 1681PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6DID5.
MaxQBiQ6DID5.
PaxDbiQ6DID5.
PRIDEiQ6DID5.

PTM databases

PhosphoSiteiQ6DID5.

Expressioni

Gene expression databases

BgeeiQ6DID5.
CleanExiMM_MUM1.
ExpressionAtlasiQ6DID5. baseline and differential.
GenevisibleiQ6DID5. MM.

Interactioni

Subunit structurei

Interacts with TP53BP1 (via BRCT domain); the interaction is not dependent on its phosphorylation status. Binds nucleosomes. Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3) (in vitro) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ6DID5. 1 interaction.
MINTiMINT-8174112.
STRINGi10090.ENSMUSP00000020365.

Structurei

3D structure databases

ProteinModelPortaliQ6DID5.
SMRiQ6DID5. Positions 380-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini383 – 44462PWWPAdd
BLAST

Domaini

The PWWP domain mediates the interaction with nucleosomes.

Sequence similaritiesi

Belongs to the MUM1 family.Curated
Contains 1 PWWP domain.Curated

Phylogenomic databases

eggNOGiENOG410IKQG. Eukaryota.
ENOG4111FZN. LUCA.
GeneTreeiENSGT00390000001700.
HOGENOMiHOG000232141.
HOVERGENiHBG054002.
InParanoidiQ6DID5.
OMAiQAIGWCV.
OrthoDBiEOG7BS494.
PhylomeDBiQ6DID5.
TreeFamiTF328774.

Family and domain databases

InterProiIPR033368. MUM1.
[Graphical view]
PANTHERiPTHR31333:SF4. PTHR31333:SF4. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6DID5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDAKYVLCR WGKRLWPAKV LARTETSAKN KKKKEFFLDV QILSLKEKIQ
60 70 80 90 100
VKSSAVEALQ KSHIENIAAF LASQNEVPAT PLEELTYRRS LRVALDVLNE
110 120 130 140 150
RTSLSPESHP IEDGITLSQK EKTDADVASQ VSSAPSPSLL GEDGQAVVAQ
160 170 180 190 200
CASKRRSEYS SKSLLPSSAL EDHLRCQVGP KTGLSESGAG DKSQDDSGLQ
210 220 230 240 250
LDHGQESTTK KRQRNLGEKP TRRRRSESGL SKGESVLKSQ GQASSCVALA
260 270 280 290 300
SPRPPSQTRD EEPCAGVKGC DWVKSSGNIR PLSASERSRG CPTKRPRLDG
310 320 330 340 350
GQNPPTRQLG TRTVGAAPCP RSCSGEVTML CSAGAGDKPE EDPVSSEEST
360 370 380 390 400
GFKSTHSLLE EEEEEEEEPP RILLYHEPRS FEVGMLVWLK YQKYPFWPAV
410 420 430 440 450
VKSVRRRDKK ASVLFIEGNM NPKGRGITVS LRRLKHFDCK EKHALLDRAK
460 470 480 490 500
EDFAQAIGWC VSLITDYRVR LGCGSFAGSF LEYYAADISY PVRKSIQQDV
510 520 530 540 550
LGTRFPQLGK GDPEEPVGDS QLGQWRPCRK VLPDRSRAAR DRANQKLVEY
560 570 580 590 600
IVKAKGAESH LRAILHSRKP SRWLKTFLSS SQCVTCMETY LEDEAQLDEV
610 620 630 640 650
VEYLQGVCRD MDGQVPERGS GDRIRFILDV LLPEAIICAI SAVEAVDYKT
660 670 680
AEQKYIRGPT LSYREKEIFD NELLEERNRR RR
Length:682
Mass (Da):76,069
Last modified:August 16, 2004 - v1
Checksum:i53C3B9085ECD2733
GO

Sequence cautioni

The sequence AAH23031.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA82658.1 differs from that shown. Reason: Frameshift at positions 413, 482 and 488. Curated
The sequence BAC37397.1 differs from that shown.Intron retention. This sequence is incomplete at the 5'-end.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591L → M in BAC37397 (PubMed:16141072).Curated
Sequence conflicti374 – 3741L → Q in BAA82658 (Ref. 3) Curated
Sequence conflicti400 – 4067VVKSVRR → PTRPVRP in AAH69883 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078792 mRNA. Translation: BAC37397.1. Sequence problems.
AK158750 mRNA. Translation: BAE34640.1.
AK170459 mRNA. Translation: BAE41811.1.
BC023031 mRNA. Translation: AAH23031.1. Different initiation.
BC069883 mRNA. Translation: AAH69883.1.
BC075617 mRNA. Translation: AAH75617.1.
AB030505 mRNA. Translation: BAA82658.1. Frameshift.
CCDSiCCDS24014.1.
RefSeqiNP_075920.4. NM_023431.5.
XP_006514088.1. XM_006514025.2.
UniGeneiMm.273418.

Genome annotation databases

EnsembliENSMUST00000020365; ENSMUSP00000020365; ENSMUSG00000020156.
GeneIDi68114.
KEGGimmu:68114.
UCSCiuc007gch.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078792 mRNA. Translation: BAC37397.1. Sequence problems.
AK158750 mRNA. Translation: BAE34640.1.
AK170459 mRNA. Translation: BAE41811.1.
BC023031 mRNA. Translation: AAH23031.1. Different initiation.
BC069883 mRNA. Translation: AAH69883.1.
BC075617 mRNA. Translation: AAH75617.1.
AB030505 mRNA. Translation: BAA82658.1. Frameshift.
CCDSiCCDS24014.1.
RefSeqiNP_075920.4. NM_023431.5.
XP_006514088.1. XM_006514025.2.
UniGeneiMm.273418.

3D structure databases

ProteinModelPortaliQ6DID5.
SMRiQ6DID5. Positions 380-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6DID5. 1 interaction.
MINTiMINT-8174112.
STRINGi10090.ENSMUSP00000020365.

PTM databases

PhosphoSiteiQ6DID5.

Proteomic databases

EPDiQ6DID5.
MaxQBiQ6DID5.
PaxDbiQ6DID5.
PRIDEiQ6DID5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020365; ENSMUSP00000020365; ENSMUSG00000020156.
GeneIDi68114.
KEGGimmu:68114.
UCSCiuc007gch.1. mouse.

Organism-specific databases

CTDi84939.
MGIiMGI:1915364. Mum1.

Phylogenomic databases

eggNOGiENOG410IKQG. Eukaryota.
ENOG4111FZN. LUCA.
GeneTreeiENSGT00390000001700.
HOGENOMiHOG000232141.
HOVERGENiHBG054002.
InParanoidiQ6DID5.
OMAiQAIGWCV.
OrthoDBiEOG7BS494.
PhylomeDBiQ6DID5.
TreeFamiTF328774.

Miscellaneous databases

ChiTaRSiMum1. mouse.
NextBioi326454.
PROiQ6DID5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6DID5.
CleanExiMM_MUM1.
ExpressionAtlasiQ6DID5. baseline and differential.
GenevisibleiQ6DID5. MM.

Family and domain databases

InterProiIPR033368. MUM1.
[Graphical view]
PANTHERiPTHR31333:SF4. PTHR31333:SF4. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Testis and Visual cortex.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain, Eye and Salivary gland.
  3. "Ubiquitously expressing genes."
    Goto M., Eddy E.M.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 276-682.
    Strain: CD-1.
    Tissue: Testis.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-345 AND SER-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiMUM1_MOUSE
AccessioniPrimary (citable) accession number: Q6DID5
Secondary accession number(s): Q3TCZ4
, Q6NST9, Q8C5E3, Q8R1V6, Q9R1R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: August 16, 2004
Last modified: May 11, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.