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Protein

Pre-B-cell leukemia transcription factor-interacting protein 1

Gene

PBXIP1

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

Functioni

Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling.3 Publications

GO - Molecular functioni

  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • cell differentiation Source: UniProtKB
  • multicellular organism development Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-B-cell leukemia transcription factor-interacting protein 1
Alternative name(s):
Hematopoietic PBX-interacting protein
Gene namesi
Name:PBXIP1
Synonyms:HPIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:21199. PBXIP1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi615 – 6195LASLL → AASAA: Reduces interaction with ESR1. 1 Publication

Organism-specific databases

PharmGKBiPA134956095.

Polymorphism and mutation databases

BioMutaiPBXIP1.
DMDMi74751749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731Pre-B-cell leukemia transcription factor-interacting protein 1PRO_0000306115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei152 – 1521PhosphothreonineCombined sources
Modified residuei567 – 5671PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96AQ6.
MaxQBiQ96AQ6.
PaxDbiQ96AQ6.
PRIDEiQ96AQ6.

PTM databases

iPTMnetiQ96AQ6.
PhosphoSiteiQ96AQ6.
SwissPalmiQ96AQ6.

Expressioni

Tissue specificityi

Expressed in early hematopoietic precursors.1 Publication

Gene expression databases

BgeeiQ96AQ6.
CleanExiHS_PBXIP1.
ExpressionAtlasiQ96AQ6. baseline and differential.
GenevisibleiQ96AQ6. HS.

Organism-specific databases

HPAiHPA006949.

Interactioni

Subunit structurei

Interacts with TEX11 (By similarity). Interacts with ESR1, PBX1, PBX2 and PBX3.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC53Q9Y3C03EBI-740845,EBI-712969
CCNCP248633EBI-740845,EBI-395261
DAXXQ9UER73EBI-740845,EBI-77321
DEF6Q9H4E73EBI-740845,EBI-745369
ESR1P033729EBI-740845,EBI-78473
FLJ13057Q53SE73EBI-740845,EBI-10172181
MORF4L1Q9UBU83EBI-740845,EBI-399246
MORF4L1Q9UBU8-23EBI-740845,EBI-10288852
SGTAO437653EBI-740845,EBI-347996
UBQLN1Q9UMX0-23EBI-740845,EBI-10173939

Protein-protein interaction databases

BioGridi121486. 36 interactions.
DIPiDIP-46922N.
IntActiQ96AQ6. 19 interactions.
MINTiMINT-1438383.
STRINGi9606.ENSP00000357448.

Structurei

3D structure databases

ProteinModelPortaliQ96AQ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili270 – 34879Sequence analysisAdd
BLAST
Coiled coili377 – 41741Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi485 – 50521Nuclear localization signalSequence analysisAdd
BLAST
Motifi695 – 72026Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi160 – 1656Poly-Arg
Compositional biasi721 – 7299His-rich

Domaini

The C-terminal domain (AA 443-731) contains a nuclear export signal.
Association to the cytoskeleton through a N-terminal leucine rich-domain (AA 190-218).

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410II9I. Eukaryota.
ENOG410YAJH. LUCA.
GeneTreeiENSGT00530000063862.
HOGENOMiHOG000115464.
HOVERGENiHBG108234.
InParanoidiQ96AQ6.
OMAiSEAWHQK.
OrthoDBiEOG7GXPBP.
PhylomeDBiQ96AQ6.
TreeFamiTF333202.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96AQ6-1) [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
MASCPDSDNS WVLAGSESLP VETLGPASRM DPESERALQA PHSPSKTDGK
60 70 80 90 100
ELAGTMDGEG TLFQTESPQS GSILTEETEV KGTLEGDVCG VEPPGPGDTV
110 120 130 140 150
VQGDLQETTV VTGLGPDTQD LEGQSPPQSL PSTPKAAWIR EEGRCSSSDD
160 170 180 190 200
DTDVDMEGLR RRRGREAGPP QPMVPLAVEN QAGGEGAGGE LGISLNMCLL
210 220 230 240 250
GALVLLGLGV LLFSGGLSES ETGPMEEVER QVLPDPEVLE AVGDRQDGLR
260 270 280 290 300
EQLQAPVPPD SVPSLQNMGL LLDKLAKENQ DIRLLQAQLQ AQKEELQSLM
310 320 330 340 350
HQPKGLEEEN AQLRGALQQG EAFQRALESE LQQLRARLQG LEADCVRGPD
360 370 380 390 400
GVCLSGGRGP QGDKAIREQG PREQEPELSF LKQKEQLEAE AQALRQELER
410 420 430 440 450
QRRLLGSVQQ DLERSLQDAS RGDPAHAGLA ELGHRLAQKL QGLENWGQDP
460 470 480 490 500
GVSANASKAW HQKSHFQNSR EWSGKEKWWD GQRDRKAEHW KHKKEESGRE
510 520 530 540 550
RKKNWGGQED REPAGRWKEG RPRVEESGSK KEGKRQGPKE PPRKSGSFHS
560 570 580 590 600
SGEKQKQPRW REGTKDSHDP LPSWAELLRP KYRAPQGCSG VDECARQEGL
610 620 630 640 650
TFFGTELAPV RQQELASLLR TYLARLPWAG QLTKELPLSP AFFGEDGIFR
660 670 680 690 700
HDRLRFRDFV DALEDSLEEV AVQQTGDDDE VDDFEDFIFS HFFGDKALKK
710 720 730
RSGKKDKHSQ SPRAAGPREG HSHSHHHHHR G
Length:731
Mass (Da):80,643
Last modified:December 1, 2001 - v1
Checksum:iD9AB1F22A12E178D
GO
Isoform 2 (identifier: Q96AQ6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:702
Mass (Da):77,684
Checksum:iD90E6A7742683C0F
GO
Isoform 3 (identifier: Q96AQ6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     566-634: Missing.

Show »
Length:662
Mass (Da):72,920
Checksum:iE41A0F9A58F7E9E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391I → F in BAB14059 (PubMed:14702039).Curated
Sequence conflicti268 – 2681M → I in AAG02026 (PubMed:10825160).Curated
Sequence conflicti268 – 2681M → I in BAB14471 (PubMed:14702039).Curated
Sequence conflicti381 – 3811L → P in BAB14059 (PubMed:14702039).Curated
Sequence conflicti595 – 5951A → P in AAG02026 (PubMed:10825160).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti356 – 3561G → D.
Corresponds to variant rs2061690 [ dbSNP | Ensembl ].
VAR_051263
Natural varianti357 – 3571G → D.2 Publications
Corresponds to variant rs2061690 [ dbSNP | Ensembl ].
VAR_035265

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_028418Add
BLAST
Alternative sequencei566 – 63469Missing in isoform 3. 1 PublicationVSP_028419Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221521 mRNA. Translation: AAG02026.1.
AK022497 mRNA. Translation: BAB14059.1.
AK023219 mRNA. Translation: BAB14471.1.
AL451085 Genomic DNA. Translation: CAI13238.1.
AL451085 Genomic DNA. Translation: CAI13239.1.
AL451085 Genomic DNA. Translation: CAI13240.1.
CH471121 Genomic DNA. Translation: EAW53175.1.
CH471121 Genomic DNA. Translation: EAW53176.1.
BC016852 mRNA. Translation: AAH16852.1.
CCDSiCCDS1074.1. [Q96AQ6-1]
RefSeqiNP_001304663.1. NM_001317734.1. [Q96AQ6-2]
NP_001304664.1. NM_001317735.1.
NP_065385.2. NM_020524.3. [Q96AQ6-1]
UniGeneiHs.505806.

Genome annotation databases

EnsembliENST00000368463; ENSP00000357448; ENSG00000163346. [Q96AQ6-1]
ENST00000368465; ENSP00000357450; ENSG00000163346. [Q96AQ6-2]
GeneIDi57326.
KEGGihsa:57326.
UCSCiuc001ffr.4. human. [Q96AQ6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221521 mRNA. Translation: AAG02026.1.
AK022497 mRNA. Translation: BAB14059.1.
AK023219 mRNA. Translation: BAB14471.1.
AL451085 Genomic DNA. Translation: CAI13238.1.
AL451085 Genomic DNA. Translation: CAI13239.1.
AL451085 Genomic DNA. Translation: CAI13240.1.
CH471121 Genomic DNA. Translation: EAW53175.1.
CH471121 Genomic DNA. Translation: EAW53176.1.
BC016852 mRNA. Translation: AAH16852.1.
CCDSiCCDS1074.1. [Q96AQ6-1]
RefSeqiNP_001304663.1. NM_001317734.1. [Q96AQ6-2]
NP_001304664.1. NM_001317735.1.
NP_065385.2. NM_020524.3. [Q96AQ6-1]
UniGeneiHs.505806.

3D structure databases

ProteinModelPortaliQ96AQ6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121486. 36 interactions.
DIPiDIP-46922N.
IntActiQ96AQ6. 19 interactions.
MINTiMINT-1438383.
STRINGi9606.ENSP00000357448.

PTM databases

iPTMnetiQ96AQ6.
PhosphoSiteiQ96AQ6.
SwissPalmiQ96AQ6.

Polymorphism and mutation databases

BioMutaiPBXIP1.
DMDMi74751749.

Proteomic databases

EPDiQ96AQ6.
MaxQBiQ96AQ6.
PaxDbiQ96AQ6.
PRIDEiQ96AQ6.

Protocols and materials databases

DNASUi57326.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368463; ENSP00000357448; ENSG00000163346. [Q96AQ6-1]
ENST00000368465; ENSP00000357450; ENSG00000163346. [Q96AQ6-2]
GeneIDi57326.
KEGGihsa:57326.
UCSCiuc001ffr.4. human. [Q96AQ6-1]

Organism-specific databases

CTDi57326.
GeneCardsiPBXIP1.
H-InvDBHIX0001107.
HGNCiHGNC:21199. PBXIP1.
HPAiHPA006949.
neXtProtiNX_Q96AQ6.
PharmGKBiPA134956095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410II9I. Eukaryota.
ENOG410YAJH. LUCA.
GeneTreeiENSGT00530000063862.
HOGENOMiHOG000115464.
HOVERGENiHBG108234.
InParanoidiQ96AQ6.
OMAiSEAWHQK.
OrthoDBiEOG7GXPBP.
PhylomeDBiQ96AQ6.
TreeFamiTF333202.

Miscellaneous databases

ChiTaRSiPBXIP1. human.
GenomeRNAii57326.
NextBioi63434.
PROiQ96AQ6.

Gene expression databases

BgeeiQ96AQ6.
CleanExiHS_PBXIP1.
ExpressionAtlasiQ96AQ6. baseline and differential.
GenevisibleiQ96AQ6. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA."
    Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C., Humphries R.K.
    J. Biol. Chem. 275:26172-26177(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PBX1; PBX2 AND PBX3, VARIANT ASP-357.
  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 2 AND 3), VARIANT ASP-357.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Pancreas.
  6. "Functional characterization of multiple domains involved in the subcellular localization of the hematopoietic Pbx interacting protein (HPIP)."
    Abramovich C., Chavez E.A., Lansdorp P.M., Humphries R.K.
    Oncogene 21:6766-6771(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION, SUBCELLULAR LOCATION.
  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-146; SER-147; SER-148 AND THR-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "An inherent role of microtubule network in the action of nuclear receptor."
    Manavathi B., Acconcia F., Rayala S.K., Kumar R.
    Proc. Natl. Acad. Sci. U.S.A. 103:15981-15986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ESR1, MUTAGENESIS OF 615-LEU--LEU-619.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-147 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-43, 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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPBIP1_HUMAN
AccessioniPrimary (citable) accession number: Q96AQ6
Secondary accession number(s): Q5T174
, Q5T176, Q9H8X6, Q9HA02, Q9HD85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 104 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
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations

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.