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Q96BK5

- PINX1_HUMAN

UniProt

Q96BK5 - PINX1_HUMAN

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Protein
PIN2/TERF1-interacting telomerase inhibitor 1
Gene
PINX1, LPTL, LPTS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor.6 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. telomerase inhibitor activity Source: UniProtKB
  3. telomeric RNA binding Source: UniProtKB

GO - Biological processi

  1. mitotic metaphase plate congression Source: UniProtKB
  2. negative regulation of cell proliferation Source: UniProtKB
  3. negative regulation of telomerase activity Source: GOC
  4. regulation of telomerase activity Source: UniProtKB
  5. telomere maintenance via telomerase Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
PIN2/TERF1-interacting telomerase inhibitor 1
Alternative name(s):
Liver-related putative tumor suppressor
Pin2-interacting protein X1
Protein 67-11-3
TRF1-interacting protein 1
Gene namesi
Name:PINX1
Synonyms:LPTL, LPTS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:30046. PINX1.

Subcellular locationi

Nucleus. Nucleusnucleolus. Chromosometelomere. Chromosomecentromerekinetochore
Note: Localizes in nucleoli, at telomere speckles and to the outer plate of kinetochores. Localization to the kinetochore is mediated by its central region and depends on NDC80 and CENPE.3 Publications

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB-SubCell
  2. condensed chromosome kinetochore Source: UniProtKB-SubCell
  3. kinetochore Source: UniProtKB
  4. nuclear chromosome Source: UniProtKB
  5. nucleolus Source: UniProtKB
  6. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi291 – 2911L → A: Abolishes interaction with TERF1. 1 Publication
Mutagenesisi293 – 2931P → A: Does not affect interaction with TERF1. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA165585852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328PIN2/TERF1-interacting telomerase inhibitor 1
PRO_0000058443Add
BLAST

Proteomic databases

MaxQBiQ96BK5.
PaxDbiQ96BK5.
PRIDEiQ96BK5.

PTM databases

PhosphoSiteiQ96BK5.

Expressioni

Tissue specificityi

Ubiquitous; expressed at low levels. Not detectable in a number of hepatocarcinoma cell lines.

Gene expression databases

ArrayExpressiQ96BK5.
BgeeiQ96BK5.
GenevestigatoriQ96BK5.

Organism-specific databases

HPAiHPA023139.

Interactioni

Subunit structurei

Interacts with MCRS1, TERT, TERF1, NCL/nucleolin, and the telomerase RNA.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AHCYP235261EBI-721782,EBI-1053240
CALM1P621581EBI-721782,EBI-397435
CAPRIN1Q144441EBI-721782,EBI-1047080
GTPBP4Q9BZE41EBI-721782,EBI-1056249
HRNRQ86YZ31EBI-721782,EBI-1047017
PABPC1P119401EBI-721782,EBI-81531
PABPC4Q133101EBI-721782,EBI-372844
PLEKHJ1Q9NW611EBI-721782,EBI-1057560
RPL23AP627501EBI-721782,EBI-353254
RPL31P628991EBI-721782,EBI-1053664
RPS10P467831EBI-721782,EBI-354442
RPS16P622491EBI-721782,EBI-352480
RPS19P390191EBI-721782,EBI-354451
RPS28P628571EBI-721782,EBI-353027
RPS3AP612471EBI-721782,EBI-352378
TXNP105991EBI-721782,EBI-594644

Protein-protein interaction databases

BioGridi120319. 26 interactions.
IntActiQ96BK5. 9 interactions.
MINTiMINT-221403.

Structurei

3D structure databases

ProteinModelPortaliQ96BK5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 7247G-patch
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni254 – 32875Telomerase inhibitory domain (TID)
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi287 – 29711TBM
Add
BLAST

Domaini

The TID (telomerase inhibiting domain) domain is sufficient to bind TERT and inhibit its activity.1 Publication
The TBM domain mediates interaction with TERF1.1 Publication

Sequence similaritiesi

Belongs to the PINX1 family.
Contains 1 G-patch domain.

Phylogenomic databases

eggNOGiNOG242943.
HOVERGENiHBG061365.
InParanoidiQ96BK5.
KOiK11135.
OMAiEDCVWPP.
OrthoDBiEOG789CCG.
PhylomeDBiQ96BK5.
TreeFamiTF321918.

Family and domain databases

InterProiIPR000467. G_patch_dom.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96BK5-1) [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

MSMLAERRRK QKWAVDPQNT AWSNDDSKFG QRMLEKMGWS KGKGLGAQEQ    50
GATDHIKVQV KNNHLGLGAT INNEDNWIAH QDDFNQLLAE LNTCHGQETT 100
DSSDKKEKKS FSLEEKSKIS KNRVHYMKFT KGKDLSSRSK TDLDCIFGKR 150
QSKKTPEGDA SPSTPEENET TTTSAFTIQE YFAKRMAALK NKPQVPVPGS 200
DISETQVERK RGKKRNKEAT GKDVESYLQP KAKRHTEGKP ERAEAQERVA 250
KKKSAPAEEQ LRGPCWDQSS KASAQDAGDH VQPPEGRDFT LKPKKRRGKK 300
KLQKPVEIAE DATLEETLVK KKKKKDSK 328
Length:328
Mass (Da):37,035
Last modified:June 20, 2002 - v2
Checksum:iA298B31AEA6D18E1
GO
Isoform 2 (identifier: Q96BK5-2) [UniParc]FASTAAdd to Basket

Also known as: PINY1

The sequence of this isoform differs from the canonical sequence as follows:
     133-174: KDLSSRSKTD...PEENETTTTS → RCQSLHSRGE...EQAPGSSSRV
     175-328: Missing.

Show »
Length:174
Mass (Da):19,714
Checksum:iC569D5959A04362C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061Q → H.
Corresponds to variant rs35530857 [ dbSNP | Ensembl ].
VAR_054024
Natural varianti215 – 2151R → I.1 Publication
Corresponds to variant rs17855458 [ dbSNP | Ensembl ].
VAR_054025
Natural varianti220 – 2201T → A.
Corresponds to variant rs17711777 [ dbSNP | Ensembl ].
VAR_054026
Natural varianti254 – 2541S → C.1 Publication
Corresponds to variant rs1078543 [ dbSNP | Ensembl ].
VAR_054027
Natural varianti315 – 3151E → A.
Corresponds to variant rs34656824 [ dbSNP | Ensembl ].
VAR_054028

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei133 – 17442KDLSS…TTTTS → RCQSLHSRGERNHDNQRLHH PGVLCQADGSTEEQAPGSSS RV in isoform 2.
VSP_003945Add
BLAST
Alternative sequencei175 – 328154Missing in isoform 2.
VSP_003946Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Q → H in AAH15479. 1 Publication
Sequence conflicti185 – 1862RM → PV in AAK31790. 1 Publication
Sequence conflicti204 – 2041E → V in CAC51436. 1 Publication
Sequence conflicti205 – 2051T → A in AAS19507. 1 Publication
Sequence conflicti259 – 2591E → K in AAK31790. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF205718 mRNA. Translation: AAG18009.1.
AY029161 mRNA. Translation: AAK31790.1.
AJ344104 mRNA. Translation: CAC51436.1.
AF418553 mRNA. Translation: AAN31333.1.
AY238941 mRNA. Translation: AAP37006.1.
AY523566 mRNA. Translation: AAS19507.1.
AK000572 mRNA. Translation: BAA91263.1.
AK313715 mRNA. Translation: BAG36458.1.
CH471157 Genomic DNA. Translation: EAW65596.1.
BC015479 mRNA. Translation: AAH15479.1.
BC093762 mRNA. Translation: AAH93762.1.
CCDSiCCDS47801.1. [Q96BK5-1]
CCDS64825.1. [Q96BK5-2]
RefSeqiNP_001271285.1. NM_001284356.1. [Q96BK5-2]
NP_060354.4. NM_017884.5. [Q96BK5-1]
UniGeneiHs.490991.
Hs.583894.

Genome annotation databases

EnsembliENST00000314787; ENSP00000318966; ENSG00000254093. [Q96BK5-1]
ENST00000519088; ENSP00000428853; ENSG00000254093. [Q96BK5-2]
GeneIDi54984.
KEGGihsa:54984.
UCSCiuc003wth.2. human. [Q96BK5-1]
uc003wti.2. human. [Q96BK5-2]

Polymorphism databases

DMDMi21542178.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF205718 mRNA. Translation: AAG18009.1 .
AY029161 mRNA. Translation: AAK31790.1 .
AJ344104 mRNA. Translation: CAC51436.1 .
AF418553 mRNA. Translation: AAN31333.1 .
AY238941 mRNA. Translation: AAP37006.1 .
AY523566 mRNA. Translation: AAS19507.1 .
AK000572 mRNA. Translation: BAA91263.1 .
AK313715 mRNA. Translation: BAG36458.1 .
CH471157 Genomic DNA. Translation: EAW65596.1 .
BC015479 mRNA. Translation: AAH15479.1 .
BC093762 mRNA. Translation: AAH93762.1 .
CCDSi CCDS47801.1. [Q96BK5-1 ]
CCDS64825.1. [Q96BK5-2 ]
RefSeqi NP_001271285.1. NM_001284356.1. [Q96BK5-2 ]
NP_060354.4. NM_017884.5. [Q96BK5-1 ]
UniGenei Hs.490991.
Hs.583894.

3D structure databases

ProteinModelPortali Q96BK5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120319. 26 interactions.
IntActi Q96BK5. 9 interactions.
MINTi MINT-221403.

PTM databases

PhosphoSitei Q96BK5.

Polymorphism databases

DMDMi 21542178.

Proteomic databases

MaxQBi Q96BK5.
PaxDbi Q96BK5.
PRIDEi Q96BK5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314787 ; ENSP00000318966 ; ENSG00000254093 . [Q96BK5-1 ]
ENST00000519088 ; ENSP00000428853 ; ENSG00000254093 . [Q96BK5-2 ]
GeneIDi 54984.
KEGGi hsa:54984.
UCSCi uc003wth.2. human. [Q96BK5-1 ]
uc003wti.2. human. [Q96BK5-2 ]

Organism-specific databases

CTDi 54984.
GeneCardsi GC08M010659.
HGNCi HGNC:30046. PINX1.
HPAi HPA023139.
MIMi 606505. gene.
neXtProti NX_Q96BK5.
PharmGKBi PA165585852.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242943.
HOVERGENi HBG061365.
InParanoidi Q96BK5.
KOi K11135.
OMAi EDCVWPP.
OrthoDBi EOG789CCG.
PhylomeDBi Q96BK5.
TreeFami TF321918.

Miscellaneous databases

GeneWikii PINX1.
GenomeRNAii 54984.
NextBioi 58258.
PROi Q96BK5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96BK5.
Bgeei Q96BK5.
Genevestigatori Q96BK5.

Family and domain databases

InterProi IPR000467. G_patch_dom.
[Graphical view ]
Pfami PF01585. G-patch. 1 hit.
[Graphical view ]
SMARTi SM00443. G_patch. 1 hit.
[Graphical view ]
PROSITEi PS50174. G_PATCH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the gene for a novel liver-related putative tumor suppressor at a high-frequency loss of heterozygosity region of chromosome 8p23 in human hepatocellular carcinoma."
    Liao C., Zhao M., Song H., Uchida K., Yokoyama K.K., Li T.P.
    Hepatology 32:721-727(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Liver.
  2. "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor."
    Zhou X.Z., Lu K.P.
    Cell 107:347-359(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-254.
    Tissue: Cervix carcinoma.
  3. Schmidt T.
    Thesis (2001), University of Goettingen, Germany
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Identification of the gene LPTL, encoding for a new isoform of human putative tumor suppressor LPTS."
    Liao C., Zhao M., Li T.P.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. Qiang F.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  6. Fu Q., Cao Y., Zuo A., Liang D., Zhang Y., Wang B., Huang H., Wu Y., Zhu L., Wang P., Guo S., Guo G., Zhang J., Wang X.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "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] (ISOFORM 1), VARIANT ILE-215.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Uterus.
  10. "Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1 and reduces the telomere length."
    Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T., Zhao M.
    Biochem. Biophys. Res. Commun. 316:1116-1123(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCRS1.
  11. "Characterization of interactions between PinX1 and human telomerase subunits hTERT and hTR."
    Banik S.S.R., Counter C.M.
    J. Biol. Chem. 279:51745-51748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TERT AND THE TELOMERASE RNA.
  12. "Characterization of a novel effect of hPinX1 on hTERT nucleolar localization."
    Lin J., Jin R., Zhang B., Yang P.X., Chen H., Bai Y.X., Xie Y., Huang C., Huang J.
    Biochem. Biophys. Res. Commun. 353:946-952(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins."
    Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T., Lei M.
    Science 319:1092-1096(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TERF1, DOMAIN TBM, MUTAGENESIS OF LEU-291 AND PRO-293.
  15. "PinX1 is recruited to the mitotic chromosome periphery by nucleolin and facilitates chromosome congression."
    Li N., Yuan K., Yan F., Huo Y., Zhu T., Liu X., Guo Z., Yao X.
    Biochem. Biophys. Res. Commun. 384:76-81(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCL/NUCLEOLIN.
  16. "Silencing PinX1 compromises telomere length maintenance as well as tumorigenicity in telomerase-positive human cancer cells."
    Zhang B., Bai Y.X., Ma H.H., Feng F., Jin R., Wang Z.L., Lin J., Sun S.P., Yang P., Wang X.X., Huang P.T., Huang C.F., Peng Y., Chen Y.C., Kung H.F., Huang J.J.
    Cancer Res. 69:75-83(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "PinX1 is a novel microtubule-binding protein essential for accurate chromosome segregation."
    Yuan K., Li N., Jiang K., Zhu T., Huo Y., Wang C., Lu J., Shaw A., Thomas K., Zhang J., Mann D., Liao J., Jin C., Yao X.
    J. Biol. Chem. 284:23072-23082(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  18. "Human PinX1 mediates TRF1 accumulation in nucleolus and enhances TRF1 binding to telomeres."
    Yoo J.E., Oh B.-K., Park Y.N.
    J. Mol. Biol. 388:928-940(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  19. "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.
  20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPINX1_HUMAN
AccessioniPrimary (citable) accession number: Q96BK5
Secondary accession number(s): B2R9B1
, Q548A5, Q6QWG9, Q7Z7J8, Q96QD7, Q9HBU7, Q9NWW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 20, 2002
Last modified: July 9, 2014
This is version 112 of the entry and version 2 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 8
    Human chromosome 8: 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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