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Q9BXY0 (MAK16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein MAK16 homolog
Alternative name(s):
NNP78
Protein RBM13
Gene names
Name:MAK16
Synonyms:RBM13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleusnucleolus Ref.5 Ref.6.

Sequence similarities

Belongs to the MAK16 family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Protein MAK16 homolog
PRO_0000203794

Regions

Compositional bias198 – 24952Asp-rich
Compositional bias255 – 2595Poly-Glu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.12
Modified residue1971Phosphoserine Ref.11
Modified residue1991Phosphoserine By similarity
Modified residue2001Phosphoserine Ref.11
Modified residue2291Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue2321Phosphoserine Ref.7 Ref.10 Ref.11

Natural variations

Natural variant2771Q → R. Ref.1 Ref.4
Corresponds to variant rs6468171 [ dbSNP | Ensembl ].
VAR_023076

Experimental info

Sequence conflict2001S → L in BAB55134. Ref.2
Sequence conflict2811A → V in AAH39740. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9BXY0 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 2A757589C4749760

FASTA30035,369
        10         20         30         40         50         60 
MQSDDVIWDT LGNKQFCSFK IRTKTQSFCR NEYSLTGLCN RSSCPLANSQ YATIKEEKGQ 

        70         80         90        100        110        120 
CYLYMKVIER AAFPRRLWER VRLSKNYEKA LEQIDENLIY WPRFIRHKCK QRFTKITQYL 

       130        140        150        160        170        180 
IRIRKLTLKR QRKLVPLSKK VERREKRREE KALIAAQLDN AIEKELLERL KQDTYGDIYN 

       190        200        210        220        230        240 
FPIHAFDKAL EQQEAESDSS DTEEKDDDDD DEEDVGKREF VEDGEVDESD ISDFEDMDKL 

       250        260        270        280        290        300 
DASSDEDQDG KSSSEEEEEK ALSAKHKGKM PLRGPLQRKR AYVEIEYEQE TEPVAKAKTT 

« Hide

References

« Hide 'large scale' references
[1]Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S., Tang R., Chen X., Wu C.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-277.
[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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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], VARIANT ARG-277.
Tissue: Brain, Testis and Uterus.
[5]"Directed proteomic analysis of the human nucleolus."
Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I.
Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[6]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 SER-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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 SER-197; SER-200; SER-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF251062 mRNA. Translation: AAK34952.1.
AK027469 mRNA. Translation: BAB55134.1.
AK314491 mRNA. Translation: BAG37091.1.
CH471080 Genomic DNA. Translation: EAW63400.1.
BC028230 mRNA. Translation: AAH28230.1.
BC039740 mRNA. Translation: AAH39740.1.
BC050528 mRNA. Translation: AAH50528.1.
CCDSCCDS6089.1.
RefSeqNP_115898.2. NM_032509.3.
UniGeneHs.583805.

3D structure databases

ProteinModelPortalQ9BXY0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124134. 5 interactions.
IntActQ9BXY0. 1 interaction.
MINTMINT-3058483.
STRING9606.ENSP00000353246.

PTM databases

PhosphoSiteQ9BXY0.

Polymorphism databases

DMDM71152029.

2D gel databases

SWISS-2DPAGEQ9BXY0.

Proteomic databases

MaxQBQ9BXY0.
PaxDbQ9BXY0.
PRIDEQ9BXY0.

Protocols and materials databases

DNASU84549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360128; ENSP00000353246; ENSG00000198042.
GeneID84549.
KEGGhsa:84549.
UCSCuc003xjj.3. human.

Organism-specific databases

CTD84549.
GeneCardsGC08P033342.
HGNCHGNC:13703. MAK16.
HPAHPA044417.
HPA050574.
neXtProtNX_Q9BXY0.
PharmGKBPA162394925.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5129.
HOGENOMHOG000201538.
HOVERGENHBG055328.
InParanoidQ9BXY0.
KOK14831.
OMASPAHMWE.
OrthoDBEOG7TJ3KB.
PhylomeDBQ9BXY0.
TreeFamTF105759.

Gene expression databases

BgeeQ9BXY0.
CleanExHS_MAK16.
GenevestigatorQ9BXY0.

Family and domain databases

InterProIPR029004. L28e/Mak16.
IPR006958. Mak16.
[Graphical view]
PfamPF04874. Mak16. 1 hit.
PF01778. Ribosomal_L28e. 1 hit.
[Graphical view]
PIRSFPIRSF003352. MAK16. 1 hit.
ProtoNetSearch...

Other

GeneWikiRBM13.
GenomeRNAi84549.
NextBio74427.
PROQ9BXY0.

Entry information

Entry nameMAK16_HUMAN
AccessionPrimary (citable) accession number: Q9BXY0
Secondary accession number(s): B2RB44 expand/collapse secondary AC list , Q5U5T1, Q86UC4, Q96SY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM