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Protein

Multiple myeloma tumor-associated protein 2

Gene

MMTAG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Multiple myeloma tumor-associated protein 2
Short name:
hMMTAG2
Gene namesi
Name:MMTAG2
Synonyms:C1orf35
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:19032. C1orf35.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38781.

Polymorphism and mutation databases

BioMutaiMMTAG2.
DMDMi73621220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Multiple myeloma tumor-associated protein 2PRO_0000096518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki104 – 104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei215 – 2151PhosphothreonineCombined sources
Modified residuei216 – 2161PhosphoserineCombined sources
Modified residuei217 – 2171PhosphoserineCombined sources
Modified residuei219 – 2191PhosphothreonineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BU76.
MaxQBiQ9BU76.
PaxDbiQ9BU76.
PeptideAtlasiQ9BU76.
PRIDEiQ9BU76.

PTM databases

iPTMnetiQ9BU76.
PhosphoSiteiQ9BU76.

Expressioni

Gene expression databases

BgeeiQ9BU76.
CleanExiHS_C1orf35.
GenevisibleiQ9BU76. HS.

Organism-specific databases

HPAiHPA046175.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DACH1Q9UI36-23EBI-742459,EBI-10186082
FXR2P511163EBI-742459,EBI-740459
GOLGA2Q083794EBI-742459,EBI-618309
SRPK2P783622EBI-742459,EBI-593303
TERF1P542742EBI-742459,EBI-710997
THAP1Q9NVV94EBI-742459,EBI-741515

Protein-protein interaction databases

BioGridi122586. 28 interactions.
IntActiQ9BU76. 18 interactions.
MINTiMINT-1443747.
STRINGi9606.ENSP00000272139.

Structurei

3D structure databases

ProteinModelPortaliQ9BU76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi184 – 20623Lys-richAdd
BLAST
Compositional biasi226 – 2294Poly-His

Phylogenomic databases

eggNOGiKOG4520. Eukaryota.
ENOG41123ER. LUCA.
GeneTreeiENSGT00390000005590.
HOGENOMiHOG000242968.
HOVERGENiHBG066325.
InParanoidiQ9BU76.
OMAiCSESHKK.
OrthoDBiEOG70S77G.
PhylomeDBiQ9BU76.
TreeFamiTF332234.

Family and domain databases

InterProiIPR019315. Kinase_phosphorylation_domain.
[Graphical view]
PfamiPF10159. MMtag. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BU76-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFGSSRGGVR GGQDQFNWED VKTDKQRENY LGNSLMAPVG RWQKGRDLTW
60 70 80 90 100
YAKGRAPCAG PSREEELAAV REAEREALLA ALGYKNVKKQ PTGLSKEDFA
110 120 130 140 150
EVCKREGGDP EEKGVDRLLG LGSASGSVGR VAMSREDKEA AKLGLSVFTH
160 170 180 190 200
HRVESGGPGT SAASARRKPR AEDQTESSCE SHRKSKKEKK KKKKRKHKKE
210 220 230 240 250
KKKKDKEHRR PAEATSSPTS PERPRHHHHD SDSNSPCCKR RKRGHSGDRR
260
SPSRRWHDRG SEA
Length:263
Mass (Da):29,412
Last modified:June 1, 2001 - v1
Checksum:i51A7DEE260DBD787
GO
Isoform 2 (identifier: Q9BU76-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-141: SGSVGRVAMSREDKEAA → RCGRVSRGGQHWARLLG
     142-263: Missing.

Note: No experimental confirmation available.
Show »
Length:141
Mass (Da):15,521
Checksum:iF23E1755F88CF093
GO
Isoform 3 (identifier: Q9BU76-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-155: HHRVES → VIPRPA
     156-263: Missing.

Note: No experimental confirmation available.
Show »
Length:155
Mass (Da):16,842
Checksum:i437074D523DB3AA1
GO
Isoform 4 (identifier: Q9BU76-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     178-189: SCESHRKSKKEK → RGVSRVTLEERS
     190-263: Missing.

Note: No experimental confirmation available.
Show »
Length:189
Mass (Da):20,536
Checksum:iDBEC809E97848129
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291N → I in AAN15215 (PubMed:12545221).Curated
Sequence conflicti154 – 1541E → K in AAN15215 (PubMed:12545221).Curated
Sequence conflicti262 – 2621E → K in AAN15215 (PubMed:12545221).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei125 – 14117SGSVG…DKEAA → RCGRVSRGGQHWARLLG in isoform 2. 1 PublicationVSP_015129Add
BLAST
Alternative sequencei142 – 263122Missing in isoform 2. 1 PublicationVSP_015130Add
BLAST
Alternative sequencei150 – 1556HHRVES → VIPRPA in isoform 3. 1 PublicationVSP_015131
Alternative sequencei156 – 263108Missing in isoform 3. 1 PublicationVSP_015132Add
BLAST
Alternative sequencei178 – 18912SCESH…SKKEK → RGVSRVTLEERS in isoform 4. 1 PublicationVSP_015133Add
BLAST
Alternative sequencei190 – 26374Missing in isoform 4. 1 PublicationVSP_015134Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY137773 mRNA. Translation: AAN15215.1.
AK123377 mRNA. Translation: BAC85598.1.
AK126087 mRNA. Translation: BAC86431.1.
AL136379 Genomic DNA. Translation: CAI23119.1.
BC002843 mRNA. Translation: AAH02843.1.
BC062585 mRNA. Translation: AAH62585.1.
CCDSiCCDS1566.1. [Q9BU76-1]
RefSeqiNP_077295.1. NM_024319.3. [Q9BU76-1]
UniGeneiHs.445952.

Genome annotation databases

EnsembliENST00000272139; ENSP00000272139; ENSG00000143793. [Q9BU76-1]
GeneIDi79169.
KEGGihsa:79169.
UCSCiuc001hrx.4. human. [Q9BU76-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY137773 mRNA. Translation: AAN15215.1.
AK123377 mRNA. Translation: BAC85598.1.
AK126087 mRNA. Translation: BAC86431.1.
AL136379 Genomic DNA. Translation: CAI23119.1.
BC002843 mRNA. Translation: AAH02843.1.
BC062585 mRNA. Translation: AAH62585.1.
CCDSiCCDS1566.1. [Q9BU76-1]
RefSeqiNP_077295.1. NM_024319.3. [Q9BU76-1]
UniGeneiHs.445952.

3D structure databases

ProteinModelPortaliQ9BU76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122586. 28 interactions.
IntActiQ9BU76. 18 interactions.
MINTiMINT-1443747.
STRINGi9606.ENSP00000272139.

PTM databases

iPTMnetiQ9BU76.
PhosphoSiteiQ9BU76.

Polymorphism and mutation databases

BioMutaiMMTAG2.
DMDMi73621220.

Proteomic databases

EPDiQ9BU76.
MaxQBiQ9BU76.
PaxDbiQ9BU76.
PeptideAtlasiQ9BU76.
PRIDEiQ9BU76.

Protocols and materials databases

DNASUi79169.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272139; ENSP00000272139; ENSG00000143793. [Q9BU76-1]
GeneIDi79169.
KEGGihsa:79169.
UCSCiuc001hrx.4. human. [Q9BU76-1]

Organism-specific databases

CTDi79169.
GeneCardsiC1orf35.
HGNCiHGNC:19032. C1orf35.
HPAiHPA046175.
neXtProtiNX_Q9BU76.
PharmGKBiPA38781.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4520. Eukaryota.
ENOG41123ER. LUCA.
GeneTreeiENSGT00390000005590.
HOGENOMiHOG000242968.
HOVERGENiHBG066325.
InParanoidiQ9BU76.
OMAiCSESHKK.
OrthoDBiEOG70S77G.
PhylomeDBiQ9BU76.
TreeFamiTF332234.

Miscellaneous databases

ChiTaRSiC1orf35. human.
GenomeRNAii79169.
PROiQ9BU76.

Gene expression databases

BgeeiQ9BU76.
CleanExiHS_C1orf35.
GenevisibleiQ9BU76. HS.

Family and domain databases

InterProiIPR019315. Kinase_phosphorylation_domain.
[Graphical view]
PfamiPF10159. MMtag. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of tumor-associated gene hMMTAG2 from human multiple myeloma cell line ARH-77."
    Tian J.Y., Hu W.X., Tian E.M., Shi Y.W., Shen Q.X., Tang L.J., Jiang Y.S.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:143-148(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Myeloma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
    Tissue: Caudate nucleus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 3).
    Tissue: Blood and Lymph.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215 AND SER-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-127; SER-216; SER-217 AND SER-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMMTA2_HUMAN
AccessioniPrimary (citable) accession number: Q9BU76
Secondary accession number(s): Q6P5Y0
, Q6ZTZ6, Q6ZWA6, Q8IZH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM

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.