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Q96QH2

- PRAM_HUMAN

UniProt

Q96QH2 - PRAM_HUMAN

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Protein

PML-RARA-regulated adapter molecule 1

Gene

PRAM1

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

Functioni

May be involved in myeloid differentiation. May be involved in integrin signaling in neutrophils. Binds to PtdIns4P.

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. integrin-mediated signaling pathway Source: Ensembl
  2. regulation of neutrophil degranulation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
PML-RARA-regulated adapter molecule 1
Short name:
PRAM
Short name:
PRAM-1
Gene namesi
Name:PRAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:30091. PRAM1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718PML-RARA-regulated adapter molecule 1PRO_0000270171Add
BLAST

Post-translational modificationi

May be phosphorylated on tyrosines.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ96QH2.
PRIDEiQ96QH2.

PTM databases

PhosphoSiteiQ96QH2.

Expressioni

Tissue specificityi

Expressed in peripheral blood leukocytes and bone marrow. Expressed in monocytes, and to a lesser extent in granulocytes and lymphocytes. Not expressed in non hematopoietic tissues except in lung.1 Publication

Inductioni

Down-regulated by the PML-RARA oncogene, a fusion protein expressed in a vast majority of acute promyelocytic leukemia. Up-regulated by retinoic acid or arsenic trioxide in cells expressing PML-RARA.2 Publications

Gene expression databases

BgeeiQ96QH2.
CleanExiHS_PRAM1.
ExpressionAtlasiQ96QH2. baseline and differential.
GenevestigatoriQ96QH2.

Organism-specific databases

HPAiHPA050161.

Interactioni

Subunit structurei

Interacts with SKAP2, LCP2 and DBNL. May interact with LYN. Interacts with NEK6.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RNF32Q9H0A62EBI-2860740,EBI-724829

Protein-protein interaction databases

BioGridi123894. 20 interactions.
IntActiQ96QH2. 7 interactions.
STRINGi9606.ENSP00000255612.

Structurei

3D structure databases

ProteinModelPortaliQ96QH2.
SMRiQ96QH2. Positions 618-692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati70 – 81121Add
BLAST
Repeati82 – 93122Add
BLAST
Repeati94 – 105123Add
BLAST
Repeati106 – 117124Add
BLAST
Repeati118 – 129125Add
BLAST
Repeati130 – 141126Add
BLAST
Repeati142 – 153127Add
BLAST
Repeati154 – 165128Add
BLAST
Domaini622 – 69675SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 165968 X 12 AA repeats of K-P-P-[PQ]-P-[EQ]-[VAF]-T-D-L-P-KAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 511485Pro-richAdd
BLAST

Domaini

The SH3 domain binds to PtdIns4P.

Sequence similaritiesi

Contains 1 SH3 domain.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00530000063460.
HOGENOMiHOG000168515.
HOVERGENiHBG082165.
InParanoidiQ96QH2.
OMAiFQASQPE.
OrthoDBiEOG75QR3T.
PhylomeDBiQ96QH2.

Family and domain databases

InterProiIPR029294. hSH3.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14603. hSH3. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96QH2-1) [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
MAHHLPAAME SHQDFRSIKA KFQASQPEPS DLPKKPPKPE FGKLKKFSQP
60 70 80 90 100
ELSEHPKKAP LPEFGAVSLK PPQPQFTDLP KKPPPPEVTD LPKKPPPPEV
110 120 130 140 150
TDLPKKPPPP EVTDLPKKPP PPEVTDLPKK PPPPEVTDLP KKPPPPEVTD
160 170 180 190 200
LPKKPPPPEV TDLPKKPSKL ELSDLSKKFP QLGATPFPRK PLQPEVGEAP
210 220 230 240 250
LKASLPEPGA PARKPLQPDE LSHPARPPSE PKSGAFPRKL WQPEAGEATP
260 270 280 290 300
RSPQPELSTF PKKPAQPEFN VYPKKPPQPQ VGGLPKKSVP QPEFSEAAQT
310 320 330 340 350
PLWKPQSSEP KRDSSAFPKK ASQPPLSDFP KKPPQPELGD LTRTSSEPEV
360 370 380 390 400
SVLPKRPRPA EFKALSKKPP QPELGGLPRT SSEPEFNSLP RKLLQPERRG
410 420 430 440 450
PPRKFSQPEP SAVLKRHPQP EFFGDLPRKP PLPSSASESS LPAAVAGFSS
460 470 480 490 500
RHPLSPGFGA AGTPRWRSGG LVHSGGARPG LRPSHPPRRR PLPPASSLGH
510 520 530 540 550
PPAKPPLPPG PVDMQSFRRP SAASIDLRRT RSAAGLHFQD RQPEDIPQVP
560 570 580 590 600
DEIYELYDDV EPRDDSSPSP KGRDEAPSVQ QAARRPPQDP ALRKEKDPQP
610 620 630 640 650
QQLPPMDPKL LKQLRKAEKA EREFRKKFKF EGEIVVHTKM MIDPNAKTRR
660 670 680 690 700
GGGKHLGIRR GEILEVIEFT SNEEMLCRDP KGKYGYVPRT ALLPLETEVY
710
DDVDFCDPLE NQPLPLGR
Length:718
Mass (Da):79,245
Last modified:April 5, 2011 - v2
Checksum:i212A6BA694578F2D
GO
Isoform 2 (identifier: Q96QH2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-117: Missing.

Note: No experimental confirmation available.

Show »
Length:670
Mass (Da):73,969
Checksum:i6C05FFBC05CE739F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → N in AAH28012. (PubMed:15489334)Curated
Sequence conflicti124 – 1241V → A in CAC17767. (PubMed:11301322)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571K → Q.1 Publication
Corresponds to variant rs4804305 [ dbSNP | Ensembl ].
VAR_029808
Natural varianti73 – 731Q → P.
Corresponds to variant rs4239541 [ dbSNP | Ensembl ].
VAR_029809
Natural varianti76 – 761F → V.
Corresponds to variant rs4239540 [ dbSNP | Ensembl ].
VAR_029810
Natural varianti183 – 1831G → E.
Corresponds to variant rs58466313 [ dbSNP | Ensembl ].
VAR_061692

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei70 – 11748Missing in isoform 2. 1 PublicationVSP_022178Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272324 mRNA. Translation: CAC17767.1.
AC092298 Genomic DNA. No translation available.
AC136469 Genomic DNA. No translation available.
BC028012 mRNA. Translation: AAH28012.1.
CCDSiCCDS45954.2. [Q96QH2-2]
RefSeqiNP_115528.4. NM_032152.4. [Q96QH2-2]
UniGeneiHs.465812.

Genome annotation databases

EnsembliENST00000423345; ENSP00000408342; ENSG00000133246. [Q96QH2-2]
GeneIDi84106.
KEGGihsa:84106.
UCSCiuc002mkd.3. human. [Q96QH2-2]

Polymorphism databases

DMDMi327478532.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272324 mRNA. Translation: CAC17767.1 .
AC092298 Genomic DNA. No translation available.
AC136469 Genomic DNA. No translation available.
BC028012 mRNA. Translation: AAH28012.1 .
CCDSi CCDS45954.2. [Q96QH2-2 ]
RefSeqi NP_115528.4. NM_032152.4. [Q96QH2-2 ]
UniGenei Hs.465812.

3D structure databases

ProteinModelPortali Q96QH2.
SMRi Q96QH2. Positions 618-692.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123894. 20 interactions.
IntActi Q96QH2. 7 interactions.
STRINGi 9606.ENSP00000255612.

PTM databases

PhosphoSitei Q96QH2.

Polymorphism databases

DMDMi 327478532.

Proteomic databases

PaxDbi Q96QH2.
PRIDEi Q96QH2.

Protocols and materials databases

DNASUi 84106.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000423345 ; ENSP00000408342 ; ENSG00000133246 . [Q96QH2-2 ]
GeneIDi 84106.
KEGGi hsa:84106.
UCSCi uc002mkd.3. human. [Q96QH2-2 ]

Organism-specific databases

CTDi 84106.
GeneCardsi GC19M008554.
H-InvDB HIX0202846.
HGNCi HGNC:30091. PRAM1.
HPAi HPA050161.
MIMi 606466. gene.
neXtProti NX_Q96QH2.
PharmGKBi PA142671137.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00530000063460.
HOGENOMi HOG000168515.
HOVERGENi HBG082165.
InParanoidi Q96QH2.
OMAi FQASQPE.
OrthoDBi EOG75QR3T.
PhylomeDBi Q96QH2.

Miscellaneous databases

ChiTaRSi PRAM1. human.
GeneWikii PRAM1.
GenomeRNAii 84106.
NextBioi 73367.
PROi Q96QH2.
SOURCEi Search...

Gene expression databases

Bgeei Q96QH2.
CleanExi HS_PRAM1.
ExpressionAtlasi Q96QH2. baseline and differential.
Genevestigatori Q96QH2.

Family and domain databases

InterProi IPR029294. hSH3.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF14603. hSH3. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells."
    Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F., Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.
    J. Biol. Chem. 276:22375-22381(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH SKAP2; LCP2 AND LYN, VARIANT GLN-57.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 2).
    Tissue: Blood.
  4. "PRAM-1 potentiates arsenic trioxide-induced JNK activation."
    Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.
    J. Biol. Chem. 280:9043-9048(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DBNL, INDUCTION.
  5. "Lipid-binding hSH3 domains in immune cell adapter proteins."
    Heuer K., Sylvester M., Kliche S., Pusch R., Thiemke K., Schraven B., Freund C.
    J. Mol. Biol. 361:94-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHOINOSITIDE-BINDING.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
    Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
    J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK6.

Entry informationi

Entry nameiPRAM_HUMAN
AccessioniPrimary (citable) accession number: Q96QH2
Secondary accession number(s): Q8N6W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: April 5, 2011
Last modified: November 26, 2014
This is version 91 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 19
    Human chromosome 19: 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