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Q5SSJ5

- HP1B3_HUMAN

UniProt

Q5SSJ5 - HP1B3_HUMAN

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Protein
Heterochromatin protein 1-binding protein 3
Gene
HP1BP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Component of heterochromatin, may be involved in chromatin structure and function By similarity.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterochromatin protein 1-binding protein 3
Alternative name(s):
Protein HP1-BP74
Gene namesi
Name:HP1BP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24973. HP1BP3.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: InterPro
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 553552Heterochromatin protein 1-binding protein 3
PRO_0000339642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei142 – 1421Phosphoserine2 Publications
Modified residuei155 – 1551Phosphoserine1 Publication
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei190 – 1901N6-acetyllysine By similarity
Modified residuei248 – 2481Phosphoserine2 Publications
Modified residuei249 – 2491Phosphoserine2 Publications
Modified residuei441 – 4411Phosphoserine1 Publication
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei446 – 4461Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5SSJ5.
PaxDbiQ5SSJ5.
PRIDEiQ5SSJ5.

PTM databases

PhosphoSiteiQ5SSJ5.

Expressioni

Gene expression databases

ArrayExpressiQ5SSJ5.
BgeeiQ5SSJ5.
CleanExiHS_HP1BP3.
GenevestigatoriQ5SSJ5.

Organism-specific databases

HPAiHPA028215.
HPA054295.

Interactioni

Subunit structurei

Interacts with CBX5 By similarity.

Protein-protein interaction databases

BioGridi119128. 53 interactions.
IntActiQ5SSJ5. 5 interactions.
MINTiMINT-4719917.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi161 – 17515
Helixi180 – 19011
Helixi194 – 1974
Turni198 – 2025
Helixi203 – 21412
Turni224 – 2263
Turni231 – 2344

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQPNMR-A153-237[»]
ProteinModelPortaliQ5SSJ5.
SMRiQ5SSJ5. Positions 153-237, 255-334.

Miscellaneous databases

EvolutionaryTraceiQ5SSJ5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 23276H15 1
Add
BLAST
Domaini255 – 33076H15 2
Add
BLAST
Domaini337 – 41377H15 3
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi454 – 553100Lys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG285312.
HOVERGENiHBG097678.
InParanoidiQ5SSJ5.
OMAiASMKQRG.
OrthoDBiEOG75QR72.
PhylomeDBiQ5SSJ5.
TreeFamiTF106395.

Family and domain databases

Gene3Di1.10.10.10. 3 hits.
InterProiIPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 3 hits.
[Graphical view]
SMARTiSM00526. H15. 3 hits.
[Graphical view]
PROSITEiPS51504. H15. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5SSJ5-1) [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

MATDTSQGEL VHPKALPLIV GAQLIHADKL GEKVEDSTMP IRRTVNSTRE    50
TPPKSKLAEG EEEKPEPDIS SEESVSTVEE QENETPPATS SEAEQPKGEP 100
ENEEKEENKS SEETKKDEKD QSKEKEKKVK KTIPSWATLS ASQLARAQKQ 150
TPMASSPRPK MDAILTEAIK ACFQKSGASV VAIRKYIIHK YPSLELERRG 200
YLLKQALKRE LNRGVIKQVK GKGASGSFVV VQKSRKTPQK SRNRKNRSSA 250
VDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL 300
LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI 350
AAMNEPKTCS TTALKKYVLE NHPGTNSNYQ MHLLKKTLQK CEKNGWMEQI 400
SGKGFSGTFQ LCFPYYPSPG VLFPKKEPDD SRDEDEDEDE SSEEDSEDEE 450
PPPKRRLQKK TPAKSPGKAA SVKQRGSKPA PKVSAAQRGK ARPLPKKAPP 500
KAKTPAKKTR PSSTVIKKPS GGSSKKPATS ARKEVKLPGK GKSTMKKSFR 550
VKK 553
Length:553
Mass (Da):61,207
Last modified:December 21, 2004 - v1
Checksum:iD18B28EE0156F09B
GO
Isoform 2 (identifier: Q5SSJ5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:515
Mass (Da):57,211
Checksum:i130AD6B3FFD97525
GO
Isoform 3 (identifier: Q5SSJ5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.

Show »
Length:401
Mass (Da):44,435
Checksum:i31A31A118D2508B7
GO
Isoform 4 (identifier: Q5SSJ5-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-133: DEKDQSKEKEKKVKKTI → ERADSIHSTLFIIGQNS
     134-553: Missing.

Show »
Length:133
Mass (Da):14,594
Checksum:i87E1DE4A3A8FB907
GO

Sequence cautioni

The sequence AAF14871.1 differs from that shown. Reason: Frameshift at positions 226, 237 and 243.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 152152Missing in isoform 3.
VSP_034168Add
BLAST
Alternative sequencei1 – 3838Missing in isoform 2.
VSP_034169Add
BLAST
Alternative sequencei117 – 13317DEKDQ…VKKTI → ERADSIHSTLFIIGQNS in isoform 4.
VSP_034170Add
BLAST
Alternative sequencei134 – 553420Missing in isoform 4.
VSP_034171Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621V → G in AAF14871. 1 Publication
Sequence conflicti267 – 2671F → S in BAF83941. 1 Publication
Sequence conflicti499 – 4991P → S in BAG64972. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113534 mRNA. Translation: AAF14871.1. Frameshift.
AK023129 mRNA. Translation: BAG51160.1.
AK291252 mRNA. Translation: BAF83941.1.
AK304065 mRNA. Translation: BAG64972.1.
AL833978 mRNA. Translation: CAD38822.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12528.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12530.1.
AL606477 Genomic DNA. Translation: CAI12531.1.
AL606477 Genomic DNA. Translation: CAI12532.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12533.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23387.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23388.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23389.1.
CH471134 Genomic DNA. Translation: EAW94953.1.
BC032139 mRNA. Translation: AAH32139.1.
BC045660 mRNA. Translation: AAH45660.1.
CCDSiCCDS30621.1. [Q5SSJ5-1]
RefSeqiNP_057371.2. NM_016287.3. [Q5SSJ5-1]
XP_005245932.1. XM_005245875.2. [Q5SSJ5-1]
XP_005245933.1. XM_005245876.2. [Q5SSJ5-1]
XP_005245934.1. XM_005245877.2. [Q5SSJ5-1]
XP_005245935.1. XM_005245878.2. [Q5SSJ5-1]
XP_005245936.1. XM_005245879.2. [Q5SSJ5-2]
UniGeneiHs.142442.

Genome annotation databases

EnsembliENST00000312239; ENSP00000312625; ENSG00000127483. [Q5SSJ5-1]
ENST00000375000; ENSP00000364139; ENSG00000127483. [Q5SSJ5-5]
ENST00000375003; ENSP00000364142; ENSG00000127483. [Q5SSJ5-3]
GeneIDi50809.
KEGGihsa:50809.
UCSCiuc001bdv.1. human. [Q5SSJ5-1]
uc001bea.2. human. [Q5SSJ5-2]
uc001beb.3. human. [Q5SSJ5-5]

Polymorphism databases

DMDMi74743691.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113534 mRNA. Translation: AAF14871.1 . Frameshift.
AK023129 mRNA. Translation: BAG51160.1 .
AK291252 mRNA. Translation: BAF83941.1 .
AK304065 mRNA. Translation: BAG64972.1 .
AL833978 mRNA. Translation: CAD38822.1 .
AL606477 , AL663074 Genomic DNA. Translation: CAI12528.1 .
AL606477 , AL663074 Genomic DNA. Translation: CAI12530.1 .
AL606477 Genomic DNA. Translation: CAI12531.1 .
AL606477 Genomic DNA. Translation: CAI12532.1 .
AL606477 , AL663074 Genomic DNA. Translation: CAI12533.1 .
AL663074 , AL606477 Genomic DNA. Translation: CAI23387.1 .
AL663074 , AL606477 Genomic DNA. Translation: CAI23388.1 .
AL663074 , AL606477 Genomic DNA. Translation: CAI23389.1 .
CH471134 Genomic DNA. Translation: EAW94953.1 .
BC032139 mRNA. Translation: AAH32139.1 .
BC045660 mRNA. Translation: AAH45660.1 .
CCDSi CCDS30621.1. [Q5SSJ5-1 ]
RefSeqi NP_057371.2. NM_016287.3. [Q5SSJ5-1 ]
XP_005245932.1. XM_005245875.2. [Q5SSJ5-1 ]
XP_005245933.1. XM_005245876.2. [Q5SSJ5-1 ]
XP_005245934.1. XM_005245877.2. [Q5SSJ5-1 ]
XP_005245935.1. XM_005245878.2. [Q5SSJ5-1 ]
XP_005245936.1. XM_005245879.2. [Q5SSJ5-2 ]
UniGenei Hs.142442.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RQP NMR - A 153-237 [» ]
ProteinModelPortali Q5SSJ5.
SMRi Q5SSJ5. Positions 153-237, 255-334.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119128. 53 interactions.
IntActi Q5SSJ5. 5 interactions.
MINTi MINT-4719917.

PTM databases

PhosphoSitei Q5SSJ5.

Polymorphism databases

DMDMi 74743691.

Proteomic databases

MaxQBi Q5SSJ5.
PaxDbi Q5SSJ5.
PRIDEi Q5SSJ5.

Protocols and materials databases

DNASUi 50809.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312239 ; ENSP00000312625 ; ENSG00000127483 . [Q5SSJ5-1 ]
ENST00000375000 ; ENSP00000364139 ; ENSG00000127483 . [Q5SSJ5-5 ]
ENST00000375003 ; ENSP00000364142 ; ENSG00000127483 . [Q5SSJ5-3 ]
GeneIDi 50809.
KEGGi hsa:50809.
UCSCi uc001bdv.1. human. [Q5SSJ5-1 ]
uc001bea.2. human. [Q5SSJ5-2 ]
uc001beb.3. human. [Q5SSJ5-5 ]

Organism-specific databases

CTDi 50809.
GeneCardsi GC01M021069.
HGNCi HGNC:24973. HP1BP3.
HPAi HPA028215.
HPA054295.
neXtProti NX_Q5SSJ5.
PharmGKBi PA142671673.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285312.
HOVERGENi HBG097678.
InParanoidi Q5SSJ5.
OMAi ASMKQRG.
OrthoDBi EOG75QR72.
PhylomeDBi Q5SSJ5.
TreeFami TF106395.

Miscellaneous databases

ChiTaRSi HP1BP3. human.
EvolutionaryTracei Q5SSJ5.
GeneWikii HP1BP3.
GenomeRNAii 50809.
NextBioi 53250.
PROi Q5SSJ5.

Gene expression databases

ArrayExpressi Q5SSJ5.
Bgeei Q5SSJ5.
CleanExi HS_HP1BP3.
Genevestigatori Q5SSJ5.

Family and domain databases

Gene3Di 1.10.10.10. 3 hits.
InterProi IPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00538. Linker_histone. 3 hits.
[Graphical view ]
SMARTi SM00526. H15. 3 hits.
[Graphical view ]
PROSITEi PS51504. H15. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hypothalamus.
  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 AND 2).
    Tissue: Teratocarcinoma and Trachea.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 3 AND 4).
    Tissue: Brain and Testis.
  7. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 132-146; 176-184; 275-282; 284-291; 294-302 AND 312-329, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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.
  13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-142; SER-155; SER-156; SER-248 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-441; SER-442 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHP1B3_HUMAN
AccessioniPrimary (citable) accession number: Q5SSJ5
Secondary accession number(s): A6NI71
, A8K5D7, B3KMZ8, B4E210, Q05BI0, Q5SSJ6, Q5SWC6, Q6PIM9, Q8NDF0, Q9UHY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 101 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi