MMTAG2

Functionⁱ

GO - Molecular functionⁱ

poly(A) RNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 22658674
- 22681889

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Multiple myeloma tumor-associated protein 2 Short name: hMMTAG2
Gene namesⁱ	Name:MMTAG2 Synonyms:C1orf35
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

HGNCⁱ	HGNC:19032. C1orf35.

HGNCⁱ

HGNC:19032. C1orf35.

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA38781.

PharmGKBⁱ

PA38781.

Polymorphism and mutation databases

BioMutaⁱ	MMTAG2.
DMDMⁱ	73621220.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 263	263	Multiple myeloma tumor-associated protein 2		PRO_0000096518	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Cross-linkⁱ	104 – 104		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	123 – 123	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	127 – 127	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.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].
Modified residueⁱ	164 – 164	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	215 – 215	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	216 – 216	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	217 – 217	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	219 – 219	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	220 – 220	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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].

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9BU76.
MaxQBⁱ	Q9BU76.
PaxDbⁱ	Q9BU76.
PeptideAtlasⁱ	Q9BU76.
PRIDEⁱ	Q9BU76.

PTM databases

iPTMnetⁱ	Q9BU76.
PhosphoSiteⁱ	Q9BU76.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000143793.
CleanExⁱ	HS_C1orf35.
Genevisibleⁱ	Q9BU76. HS.

Organism-specific databases

HPAⁱ	HPA046175.

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
DACH1	Q9UI36-2	3	EBI-742459,EBI-10186082
FXR2	P51116	3	EBI-742459,EBI-740459
GOLGA2	Q08379	4	EBI-742459,EBI-618309
SRPK2	P78362	2	EBI-742459,EBI-593303
TERF1	P54274	2	EBI-742459,EBI-710997
THAP1	Q9NVV9	4	EBI-742459,EBI-741515

With

Entry

#Exp.

IntAct

Notes

DACH1

Q9UI36-2

3

EBI-742459,EBI-10186082

FXR2

P51116

3

EBI-742459,EBI-740459

GOLGA2

Q08379

4

EBI-742459,EBI-618309

SRPK2

P78362

2

EBI-742459,EBI-593303

TERF1

P54274

2

EBI-742459,EBI-710997

THAP1

Q9NVV9

4

EBI-742459,EBI-741515

Protein-protein interaction databases

BioGridⁱ	122586. 28 interactions.
IntActⁱ	Q9BU76. 18 interactions.
MINTⁱ	MINT-1443747.
STRINGⁱ	9606.ENSP00000272139.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q9BU76.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Compositional biasⁱ	184 – 206	23	Lys-rich			Add BLAST
Compositional biasⁱ	226 – 229	4	Poly-His

Phylogenomic databases

eggNOGⁱ	KOG4520. Eukaryota. ENOG41123ER. LUCA.
GeneTreeⁱ	ENSGT00390000005590.
HOGENOMⁱ	HOG000242968.
HOVERGENⁱ	HBG066325.
InParanoidⁱ	Q9BU76.
OMAⁱ	CSESHKK.
OrthoDBⁱ	EOG091G0LCC.
PhylomeDBⁱ	Q9BU76.
TreeFamⁱ	TF332234.

Family and domain databases

InterProⁱ	IPR019315. Kinase_phosphorylation_domain. [Graphical view]
Pfamⁱ	PF10159. MMtag. 1 hit. [Graphical view]

Sequences (4)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

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

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

« 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 
EVCKREGGDP EEKGVDRLLG LGSARCGRVS RGGQHWARLL G

Note: No experimental confirmation available.

Show »

Length:141

Mass (Da):15,521

Checksum:ⁱF23E1755F88CF093

GO

Isoform 3 (identifier: Q9BU76-3) [UniParc]FASTA Add to basket

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

« 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 AKLGLSVFTV 

IPRPA

Note: No experimental confirmation available.

Show »

Length:155

Mass (Da):16,842

Checksum:ⁱ437074D523DB3AA1

GO

Isoform 4 (identifier: Q9BU76-4) [UniParc]FASTA Add to basket

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

« 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 
HRVESGGPGT SAASARRKPR AEDQTESRGV SRVTLEERS

Note: No experimental confirmation available.

Show »

Length:189

Mass (Da):20,536

Checksum:ⁱDBEC809E97848129

GO

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	29 – 29	1	N → I in AAN15215 (PubMed:12545221).Curated
Sequence conflictⁱ	154 – 154	1	E → K in AAN15215 (PubMed:12545221).Curated
Sequence conflictⁱ	262 – 262	1	E → K in AAN15215 (PubMed:12545221).Curated

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	125 – 141	17	SGSVG…DKEAA → RCGRVSRGGQHWARLLG in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).	VSP_015129	Add BLAST
Alternative sequenceⁱ	142 – 263	122	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).	VSP_015130	Add BLAST
Alternative sequenceⁱ	150 – 155	6	HHRVES → VIPRPA in isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.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).	VSP_015131
Alternative sequenceⁱ	156 – 263	108	Missing in isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.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).	VSP_015132	Add BLAST
Alternative sequenceⁱ	178 – 189	12	SCESH…SKKEK → RGVSRVTLEERS in isoform 4. 1 Publication Manual assertion based on opinion inⁱ Ref.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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).	VSP_015133	Add BLAST
Alternative sequenceⁱ	190 – 263	74	Missing in isoform 4. 1 Publication Manual assertion based on opinion inⁱ Ref.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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).	VSP_015134	Add 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.
CCDSⁱ	CCDS1566.1. [Q9BU76-1]
RefSeqⁱ	NP_077295.1. NM_024319.3. [Q9BU76-1]
UniGeneⁱ	Hs.445952.

Genome annotation databases

Ensemblⁱ	ENST00000272139; ENSP00000272139; ENSG00000143793. [Q9BU76-1]
GeneIDⁱ	79169.
KEGGⁱ	hsa:79169.
UCSCⁱ	uc001hrx.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.
CCDSⁱ	CCDS1566.1. [Q9BU76-1]
RefSeqⁱ	NP_077295.1. NM_024319.3. [Q9BU76-1]
UniGeneⁱ	Hs.445952.

3D structure databases

ProteinModelPortalⁱ	Q9BU76.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	122586. 28 interactions.
IntActⁱ	Q9BU76. 18 interactions.
MINTⁱ	MINT-1443747.
STRINGⁱ	9606.ENSP00000272139.

PTM databases

iPTMnetⁱ	Q9BU76.
PhosphoSiteⁱ	Q9BU76.

Polymorphism and mutation databases

BioMutaⁱ	MMTAG2.
DMDMⁱ	73621220.

Proteomic databases

EPDⁱ	Q9BU76.
MaxQBⁱ	Q9BU76.
PaxDbⁱ	Q9BU76.
PeptideAtlasⁱ	Q9BU76.
PRIDEⁱ	Q9BU76.

Protocols and materials databases

DNASUⁱ	79169.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000272139; ENSP00000272139; ENSG00000143793. [Q9BU76-1]
GeneIDⁱ	79169.
KEGGⁱ	hsa:79169.
UCSCⁱ	uc001hrx.4. human. [Q9BU76-1]

Organism-specific databases

CTDⁱ	79169.
GeneCardsⁱ	C1orf35.
HGNCⁱ	HGNC:19032. C1orf35.
HPAⁱ	HPA046175.
neXtProtⁱ	NX_Q9BU76.
PharmGKBⁱ	PA38781.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG4520. Eukaryota. ENOG41123ER. LUCA.
GeneTreeⁱ	ENSGT00390000005590.
HOGENOMⁱ	HOG000242968.
HOVERGENⁱ	HBG066325.
InParanoidⁱ	Q9BU76.
OMAⁱ	CSESHKK.
OrthoDBⁱ	EOG091G0LCC.
PhylomeDBⁱ	Q9BU76.
TreeFamⁱ	TF332234.

Miscellaneous databases

ChiTaRSⁱ	C1orf35. human.
GenomeRNAiⁱ	79169.
PROⁱ	Q9BU76.

Gene expression databases

Bgeeⁱ	ENSG00000143793.
CleanExⁱ	HS_C1orf35.
Genevisibleⁱ	Q9BU76. HS.

Family and domain databases

InterProⁱ	IPR019315. Kinase_phosphorylation_domain. [Graphical view]
Pfamⁱ	PF10159. MMtag. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

MMTA2_HUMAN

Accessionⁱ

Primary (citable) accession number: Q9BU76
Secondary accession number(s): Q6P5Y0

Q8IZH3

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 1, 2001
Last modified:	September 7, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9BU76 (MMTA2_HUMAN)

UniProt

Q9BU76 - MMTA2_HUMAN

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Multiple myeloma tumor-associated protein 2

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<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (4)i

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequences (4)ⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ